{"id":25,"date":"2017-04-13T18:23:07","date_gmt":"2017-04-13T18:23:07","guid":{"rendered":"https:\/\/scholarblogs.emory.edu\/dyerlab\/?page_id=25"},"modified":"2022-07-05T13:01:54","modified_gmt":"2022-07-05T17:01:54","slug":"publications","status":"publish","type":"page","link":"https:\/\/scholarblogs.emory.edu\/dyerlab\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"

Google Scholar Bibliography<\/a><\/strong><\/span><\/p>\n

NCBI Pub Med Bibliography<\/a><\/strong><\/span><\/p>\n

“Time-Resolved Infrared Spectroscopy Reveals the pH-Independence of the First Electron Transfer Step in the [FeFe] Hydrogenase Catalytic Cycle” M. L. K. Sanchez; S. Wiley; E. Reijerse; W. Lubitz; J. A. Birrell; and R. B. Dyer. J. Phys. Chem. Lett. <\/i>2022, link<\/a><\/b><\/p>\n

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“Efficient, Light-Driven Reduction of CO2<\/sub> to CO by a Carbon Monoxide Dehydrogenase\u2013CdSe\/CdS Nanorod Photosystem” D. W. White; D. Esckilsen; S. K. Lee; S. W. Ragsdale; and R. B. Dyer. J. Phys. Chem. Lett. <\/i>2022, link<\/a><\/b><\/p>\n

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“Stability of HA2 Prefusion Structure and pH-Induced Conformational Changes in the HA2 Domain of H3N2 Hemagglutinin.” M. W. Eller; H. M. H. Siaw; R. B. Dyer. Biochemistry <\/i>2021,<\/b> link<\/strong><\/a><\/p>\n

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“Acceleration of catalysis in dihydrofolate reductase by transient, site-specific photothermal excitation,” R. Kozlowski; J. Zhao; R.B. Dyer. PNAS<\/em>, 2021, link<\/a><\/strong><\/p>\n

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“Shape-Shifting Peptide Nanomaterials: Surface Asymmetry Enables pH-Dependent Formation and Interconversion of Collagen Tubes and Sheets,” A.D. Merg; G. Touponse; E. van Genderen; T.B. Blum; X. Zuo; A. Bazrafshan; H.M.H. Siaw; A. McCanna; R.B. Dyer; K. Salaita; J.P. Abrahams; V.P. Conticello. JACS<\/em>, 2020, link<\/a><\/strong><\/span><\/div>\n<\/div>\n
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\"Abstract<\/div>\n
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“The Laser-Induced Potential Jump: A Method for Rapid Electron Injection into Oxidoreductase Enzymes,” M.L.K. Sanchez; S.E. Konecny; S.M. Narehood; E.J. Reijerse; W. Lubitz; J.A. Birrell; R.B. Dyer. J. Phys. Chem. B., <\/em>2020 link<\/a><\/strong><\/span><\/div>\n<\/div>\n
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\"Abstract<\/div>\n
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“Surface-Ligand \u201cLiquid\u201d to \u201cCrystalline\u201d Phase Transition Modulates the Solar H2<\/sub> Production Quantum Efficiency of CdS Nanorod\/Mediator\/Hydrogenase Assemblies,” W. Yang; G.E. Vansuch; Y. Liu; T. Jin; Q. Liu; A. Ge; M.L.K. Sanchez; D.K. Haja; M.W.W. Adams; R.B. Dyer; T. Lian. ACS Applied Materials & Interfaces<\/em>, 2020, link<\/a><\/strong><\/span><\/div>\n<\/div>\n<\/div>\n
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\"Abstract<\/div>\n
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“Polymer Force Clamps for the Mechanical Unfolding of Target Molecules,” H. Su; J. Brockman; A. Blanchard; T. Meyer; Y. Duan; Z. Liu; J. Zhao; Y. Liu; V. P. Ma; K. Galior; R.B. Dyer; Y. Ke; K. Salaita. Biophysical Journal<\/em>, 2020, link<\/a><\/strong><\/span><\/div>\n
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“Site-Specific Tryptophan Labels Reveal Local Microsecond\u2013Millisecond Motions of Dihydrofolate Reductase,” M.B. Vaughn; C. Biren; Q. Li; A. Ragupathi; R.B. Dyer. Molecules<\/em>, 2020<\/strong>, link<\/strong><\/span><\/a><\/p>\n

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“Metal\u2013ligand cooperativity in the soluble hydrogenase-1 from Pyrococcus furiosus,” G. E. Vansuch; C. Wu; D. K. Haja; S. A. Blair; B. Chica; M. K. Johnson; M.W.W. Adams; R.B. Dyer. Chemical Science<\/em>, 2020 <\/strong>link<\/span><\/strong><\/a><\/p>\n

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“An Abrupt Change of Configuration of Surface Ligands Affects the H 2 Production Efficiency of Mediator-Based CdS Nanorod\/Hydrogenase Assemblies,” W. Yang; G.E. Vansuch; Y. Liu; T. Jin; A. Ge; M.L.K Sanchez; R.B. Dyer; T Lian. 236th ECS Meeting (October 13-17, 2019)<\/em>, link<\/strong><\/span><\/a><\/p>\n

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“Investigating the Kinetic Competency of CrHydA1 [FeFe] Hydrogenase Intermediate States via Time-resolved Infrared Spectroscopy,” M.L.K. Sanchez; C. Sommer; E. Reijerse; J.A. Birrell; W. Lubitz; R.B. Dyer. JACS<\/em>, 2019 link<\/a><\/strong><\/p>\n

\"Abstract<\/p>\n

“Kinetics of Histidine-Tagged Protein Association to Nickel-Decorated Liposome Surfaces,” G. Raghunath; R.B. Dyer. Langmuir, <\/em> 2019<\/strong> , 35,<\/em>  12550-12561 link<\/strong><\/a><\/p>\n

\"Abstract<\/p>\n

“Active Site Glu165 Activation in Triosephosphate Isomerase and its Deprotonation Kinetics,” H. Deng; R.B. Dyer; R. Callender. J. Phys. Chem. B., <\/em>2019<\/strong> link<\/strong><\/span><\/a><\/span><\/p>\n

\"Abstract<\/p>\n

“Optimizing electron transfer from CdSe QDs to hydrogenase for photocatalytic H2 production,” M. Sanchez; Wu, C.; Adams, M.W.W.; R.B. Dyer. ChemComm<\/em>, 2019 link\"Graphical<\/a><\/span><\/strong><\/span><\/p>\n

“Localized Nanoscale Heating Leads to Ultrafast Hydrogel Volume-Phase Transition,” J. Zhao; H. Su; G. E. Vansuch; Z. Liu; K. Salaita; R.B. Dyer. ACS Nano<\/em>, 2018 link<\/span><\/a><\/strong><\/span><\/p>\n

\"Abstract<\/p>\n

“Dynamics of hemagglutinin-mediated membrane fusion,” M.W. Eller, R.B. Dyer. PNAS<\/em>, 2018 link<\/a><\/strong><\/span><\/p>\n

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“Heterogeneity in the Folding of Villin Headpiece Subdomain HP36,” S. Nagarajan, S. Xiao, D.P. Raleigh, R.B. Dyer. J. Phys. Chem. B, <\/em>2018 <\/strong>Just Accepted link<\/a><\/strong><\/span><\/p>\n

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“Small molecule cores demonstrate non-competitive inhibition of lactate dehydrogenase,” B. Andrews, R.B. Dyer Med. Chem. Comm., <\/em>2018 <\/strong>Accepted link<\/a><\/strong><\/span><\/p>\n

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“Characterizing the Surface Coverage of Protein-Gold Nanoparticle Bioconjugates,” R. B. Kozlowski; A. Ragupathi; R.B. Dyer Bioconjugate Chemistry<\/em>, 2018<\/strong>, 29<\/i>, 2691\u20132700. link<\/a><\/strong><\/span><\/p>\n

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\u201cA New Era for Electron Bifurcation,\u201d J. W. Peters, D. N. Beratan, B. Bothner, R. B. Dyer, C. S. Harwood, Z. M. Heiden, R. Hille, A. K. Jones, P. W. King, Y. Lu, C. E. Lubner, S. D. Minteer, D. W. Mulder, S. Raugei, G. J. Schut, L. C. Seefeldt, M. Tokmina-Lukaszewska, O. Zadvornyy, P. Zhang, and M. W. W. Adams, Curr. Opin. Chem. Biol.<\/em> 2018<\/strong>, 47, 32-38<\/em> link<\/strong><\/a><\/span><\/p>\n

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“Peripheral Protein Unfolding Drives Membrane Bending,” Siaw, H.M.H.; Raghunath, G.; Dyer, R.B. Langmuir<\/em>, 2018, <\/strong>34<\/i>, <\/strong>8400\u20138407. link<\/a><\/strong><\/span><\/p>\n

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“Light-Responsive Polymer Particles as Force Clamps for the Mechanical Unfolding of Target Molecules,” Su, H.; Liu, Z.; Liu, Y.; Ma, V.P.; Blanchard, A.; Zhao, J.; Dyer, R.B.; Salaita, K. Nano Letters<\/em>, 2018<\/strong>, 18<\/em>, 2630-2636. link<\/a><\/strong><\/span><\/span><\/p>\n

\"Abstract
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Dyer, R. B.; Reddish, M. J.; Callender, R. “Protein Dynamics in Enzymatic Catalysis.” In Catalysis in Chemistry and Biology. Proceedings of the 24th International Solvay Conference on Chemistry<\/i>; W\u00fcthrich, K., Grubbs, R. H., Eds., 2018; pp 303-308<\/span><\/p>\n

“Binding, folding and insertion of a \u03b2-hairpin peptide at a lipid bilayer surface: Influence of electrostatics and lipid tail packing,” Reid, K.A.; Davis, C.M.; Dyer, R.B.; Kindt, J.T. Biochimica et Biophysica Acta- Biomembranes<\/em>, 2018<\/strong>, 3, 792- 800 link<\/strong><\/a><\/span><\/p>\n

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“Activity-Related Microsecond Dynamics Revealed by Temperature-Jump F\u00f6rster Resonance Energy Transfer Measurements on Thermophilic Alcohol Dehydrogenase,”Vaughn, M. B.; Zhang, J.; Spiro, T. G.; Dyer, R. B.; Klinman, J. P., Activity-Related Microsecond Dynamics Revealed by T-Jump FRET Measurements on Thermophilic Alcohol Dehydrogenase. J Am Chem Soc <\/i>2018,<\/b> 140<\/i>, 900\u2013903. link<\/strong><\/a><\/span><\/span><\/p>\n

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“Applications of Photogating and Time Resolved Spectroscopy to Mechanistic Studies of Hydrogenases,” Greene, B.L.; Vansuch, G.E.; Adams, M.W.W.; Dyer, R.B. Accounts of Chemical Research<\/em>, 2017, <\/strong>50<\/i>, 2718\u20132726.link<\/strong><\/a><\/span><\/span><\/p>\n

\"Abstract<\/p>\n

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“Balancing electron transfer rate and driving force for efficient photocatalytic hydrogen production in CdSe\/CdS nanorod-[NiFe] hydrogenase assemblies,” Chica, B.; Wu C.; Liu, Y.; Adams, M.W.W.; Lian T.; Dyer, R. B. Energy & Environmental Science, 2017<\/strong>,10<\/i>, 2245 – 2255.link<\/a><\/strong><\/span><\/p>\n

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“Parallel folding pathways of Fip35 WW domain explained by infrared spectra and their computer simulation,” Zanetti-Polzi, L.; Davis, C.M.; Gruebele, M.; Dyer, R.B.; Amadei, A.; Diadone, I. FEBS Letters, 2017, <\/strong>591<\/i>, 3265\u20133275.link<\/a><\/strong><\/span><\/p>\n

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“Resolution of Submillisecond Kinetics of Multiple Reaction Pathways for Lactate Dehydrogenase”, M. J. Reddish, R. Callender, and R. B. Dyer, Biophys. J. 2017<\/strong>, 112(9), 1852-1862 link<\/strong><\/a>\"\"<\/span><\/p>\n

“Proton Transport Mechanism of M2 Proton Channel Studied by Laser-Induced pH Jump”, B. Jeong and R. B. Dyer, J. Am. Chem. Soc. 2017<\/strong>, 139<\/i>, 6621\u20136628. PMID28467842\"\"<\/strong><\/a><\/span><\/p>\n

“Pre-Steady-State Kinetics of Catalytic Intermediates of an [FeFe]-Hydrogenase”, B. L. Greene, G. J. Schut, M. W. Adams and R. B. Dyer, ACS Catalysis 2017<\/strong>, 7(3), 2145-2150.Link<\/strong><\/a><\/span><\/p>\n

\"Abstract
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“Dual time-resolved temperature-jump fluorescence and infrared spectroscopy for the study of fast protein dynamics”, C. M. Davis, M. J. Reddish and R. B. Dyer, Spectrochim. Acta Mol. Biomol. Spectrosc. 2017<\/strong>, 178, 185-191 Link<\/strong><\/a><\/span><\/p>\n

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“Glutamate Gated Proton-Coupled Electron Transfer Activity of a [NiFe]-Hydrogenase”, B. L. Greene, G. E. Vansuch, C. H. Wu, M. W. Adams and R. B. Dyer, J. Am. Chem. Soc. 2016<\/strong>, 138 (39), 13013\u201313021 PMID27617712<\/strong><\/a><\/span><\/p>\n

\"Abstract
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“Submillisecond Dynamics of Mastoparan X Insertion into Lipid Membranes”, E. E. Schuler, S. Nagarajan, and R. B. Dyer, J. Phys. Chem. Lett. 2016<\/strong>, 7 (17), 3365\u20133370 PMID27513014<\/strong><\/a><\/span><\/p>\n

\"Abstract
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“Proton Inventory and Dynamics in the Nia-S to Nia-C Transition of a [NiFe] Hydrogenase”, B. L. Greene, C. H. Wu, G. E. Vansuch, M. W. Adams and R. B. Dyer, Biochemistry <\/span>2016<\/strong>, 55 (12), 1813\u20131825 <\/span>PMID26956769<\/strong><\/a><\/span><\/p>\n

\"Abstract
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“Ligand Dependent Conformational Dynamics of Dihydrofolate Reductase”, M. J. Reddish, M. B. Vaughn, R. Fu, and R. B. Dyer, Biochemistry.<\/span> 2016<\/strong>, 55 (10), 1485\u20131493 <\/span>PMID26901612<\/strong><\/a><\/span><\/p>\n

\"Abstract
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“Synthesis and Catalytic Reactivity of a Dicopper(II) \u03bc-\u03b72:\u03b72-Peroxo Species Supported by 1,4,7-Tri-tert-butyl-1,4,7-triazacyclononane.”, G. J. Karahalis, A. Thangavel, B. Chica, J. Bacsa, R. B. Dyer, C. C. Scarborough, Inorg. Chem. 2016<\/strong>, 55(3), 1102\u20131107. PMID26789550<\/strong><\/a><\/span><\/p>\n

\"Abstract
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“The Role of Electrostatic Interactions in Folding of \u03b2-Proteins.”, C. M. Davis, R. B. Dyer, J. Am. Chem. Soc. 2016<\/strong>, 138(4), 1456\u20131464. PMID26750867<\/strong><\/a><\/span><\/p>\n

\"Abstract
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“Sandwich-format 3D printed microfluidic mixers: a flexible platform for multi-probe analysis”, D. Kise, M. J. Reddish, R. B. Dyer, J. Micromech. Microeng.2015<\/strong>, 25, 124002. (http:\/\/iopscience.iop.org\/0960-1317\/25\/12\/124002\/media<\/a>)<\/span><\/p>\n

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“Proton-Coupled Electron Transfer Dynamics in the Catalytic Mechanism of a [NiFe]-Hydrogenase”, B. L. Greene, C.-H. Wu, P. M. McTernan, M. W. W. Adams, and R. B. Dyer, J. Am. Chem. Soc. 2015<\/strong>, 137, 4558-4566. PMID25790178<\/strong><\/a><\/span><\/p>\n

\"Abstract
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“The Pathway of O2<\/sub> to the Active Site in Heme-Copper Oxidases”, \u00d3. Einarsd\u00f3ttir, W. McDonald, C. Funatogawa, W. H. Woodruff and R. B. Dyer, Biochim. Biophys. Acta Bioenergetics 2015<\/strong>, 1847, 109\u2212118. PMID24998308<\/strong><\/a><\/span><\/p>\n

“Fast Helix Formation in the B Domain of Protein A Revealed by Site-Specific Infrared Probes.”, C. M. Davis, A. K. Cooper, R. B. Dyer, Biochemistry 2015<\/strong>, 54(9), 1758-1766. PMID25706439<\/strong><\/a><\/span><\/p>\n

\"Abstract
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“The Dynamical Nature of Enzymatic Catalysis”, R. Callender, R. B. Dyer, Acc. Chem. Res. 2015<\/strong>, 48(2), 407-413. PMID25149276<\/strong><\/a><\/span><\/p>\n

“Direct Evidence of Catalytic Heterogeneity in Lactate Dehydrogenase by Temperature Jump Infrared Spectroscopy”, M. Reddish, H.-L. Peng, H. Deng, K. S. Panwar, R. Callender, and R. B. Dyer, J. Phys. Chem. B 2014<\/strong>, 118(37), 10854\u221210862. PMID25149276<\/strong><\/a><\/span><\/p>\n

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“All-inorganic Networks and Tetramer based on Tin(II)-containing Polyoxometalates: Tuning Structural and Spectral Properties with Lone Pairs”, C. Zhao, E. N. Glass, B. Chica, D. G. Musaev, J. M. Sumliner, R. B. Dyer, T. Lian, C. L. Hill, J. Am. Chem. Soc. 2014<\/strong>, 136, 12085\u221212091. PMID25076405<\/strong><\/a><\/span><\/p>\n

\"Abstract
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\u201cCO2<\/sub> Reduction Catalyzed by Mercaptopteridine on Glassy Carbon\u201d, D. Xiang, D. Magana, R. B. Dyer, J. Am. Chem. Soc. 2014<\/strong>, 136, 14007\u221214010. PMID25259884<\/strong><\/a><\/span><\/p>\n

\"Abstract
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\u201cWW Domain folding complexity revealed by infrared spectroscopy\u201d, C.M. Davis, R. B. Dyer, Biochemistry 2014<\/strong>, 53 <\/em>(34), 5476-5484.PMID25121968<\/strong><\/a><\/span><\/p>\n


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\u201cQuantum dots encapsulated within phospholipid membranes: phase-dependent structure, photostability, and site-selective functionalization\u201d, W. Zheng, Y. Liu, A. West, E. Schuler, K. Yehl, R. B. Dyer, J. T. Kindt, K. Salaita, J. Am. Chem. Soc. 2014<\/strong>, 136<\/em> (5), 1992-1999.PMID24417287<\/strong><\/a><\/span><\/p>\n


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\u201cThe Energy Landscape of Lactate Dehydrogenase: Relationship to Catalytic Mechanism\u201d, Peng, H.-L.; Deng, H.; Dyer, R. B.; Callender, R. Biochemistry 2014<\/strong>, 53(11):1849-57 PMID24576110<\/strong><\/a><\/span><\/p>\n

\u201cThe Fate of Excited-State Charge Transfer in Push-Pull Chromophores Depends on the Initial Charge Distribution\u201d, G. Li, D. Magana, C. Kumar and R. B. Dyer, J. Phys. Chem. B 2014.<\/span><\/p>\n

\u201cDynamics of an Ultrafast Folding Subdomain in the Context of a Larger Protein Fold\u201d, C. M. Davis and R. B. Dyer, J. Am. Chem. Soc. 2013<\/strong>, 135<\/em> (51), 19260-19267. PMID24320936<\/strong><\/a><\/span><\/p>\n

\"Abstract
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\u201cSubmillisecond mixing in a continuous-flow, microfluidic mixer utilizing mid-infrared hyperspectral imaging detection\u201d D. Kise, D. Magana, M. Reddish, R. B. Dyer, Lab Chip <\/em>2014<\/strong>, 14<\/em>, 584-591. PMID24302515<\/strong><\/a><\/span><\/p>\n

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\u201cAnisotropic Energy Flow and Allosteric Ligand Binding in Albumin\u201d, G. Li, D. Magana, and R. B. Dyer, Nat Commun.<\/em> 2014<\/strong>, 5<\/em>, 3100.PMID24445265<\/strong><\/a><\/span><\/p>\n

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\u201cA simple three-dimensional-focusing, continuous-flow mixer for the study of fast protein dynamics\u201d, K. Burke, D. Parul, M. Reddish, R. B. Dyer, Lab Chip<\/em> 2013<\/strong>, 13<\/em>, 2912-2921. PMC3733270<\/strong><\/a><\/span><\/p>\n

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\u201cDynamics of the gel to fluid phase transformation in unilamellar lipid bilayer vesicles,\u201d S. Nagarajan, E. E. Schuler, K. Ma, J. T. Kindt and R. B Dyer, J. Phys. Chem. B<\/em> 2012<\/strong>, 116<\/em> (46), pp 13749\u201313756. PMC3508262<\/a><\/strong> (http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/jp309832u<\/a>)<\/span><\/p>\n

\u201cTemperature Dependence of Water Interactions with the Amide Carbonyls of \u03b1-Helices,\u201d S. H. Brewer, S. Gnanakaran, Y. Tang, D. M. Vu, D. P. Raleigh, R. B. Dyer, Biochemistry <\/em>2012<\/strong>, 51<\/em> (26), pp 5293\u20135299. PMC3448027<\/a><\/strong><\/span><\/p>\n

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\u201cDirect evidence of active site reduction and photo-driven catalysis in sensitized hydrogenase assemblies,\u201d R. Dyer, B. L. Greene C. A. Joseph M. J. Maroney J. Am. Chem. Soc.<\/em> 2012<\/strong>, 134, 11108\u221211111. PMC3394927<\/a><\/strong> <\/a>
\n\"An<\/a><\/span><\/p>\n

\u201cRaising the speed limit for \u03b2-Hairpin formation,\u201d C. M. Davis, S. Xiao, D. P. Raleigh and R. B. Dyer, J. Am. Chem. Soc.<\/em> 2012<\/strong>, 134<\/em> (35), 14476\u201314482. PMC3443077<\/a><\/strong><\/span><\/p>\n

\"An<\/span><\/p>\n

\u201cDirect Observation and Control of Ultrafast Photoinduced Twisted Intramolecular Charge Transfer (TICT) in Triphenyl-Methane Dyes\u201d G. Li, D. Magana and R. B. Dyer J. Phys. Chem. B<\/em>, 2012<\/strong>, 116(41): 12590\u201312596. PMC3475756<\/a><\/strong><\/span><\/p>\n

\u201cCatalytic Deoxyribozyme-Modified Nanoparticles for RNAi-Independent Gene Regulation,\u201d K. Yehl, J. P. Joshi, B. L. Greene, R. B. Dyer, R. Nahta, K. Salaita, ACS Nano <\/em>2012<\/strong>, 6 (10), 9150\u20139157. (http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/nn3034265<\/a>)<\/span><\/p>\n

\"Abstract
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\u201cEarly turn formation and chain collapse drive fast folding of the major cold shock protein CspA of E.<\/em> coli<\/em>,\u201d D. M. Vu, S. H. Brewer, R. B. Dyer, Biochemistry<\/em> 2012<\/strong>, 51<\/em> (45), pp 9104\u20139111. (http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/bi301296y<\/a>)<\/span><\/p>\n

\"Abstract
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\u201cPhotoinduced Electron Transfer in Folic Acid Investigated by Ultrafast Infrared Spectroscopy,\u201d G. Li, D. Magana, and R. B. Dyer, J. Phys. Chem. B<\/em>, 2012<\/strong>, 116<\/em>, 3467-3475. PMC3311227<\/a><\/strong><\/span><\/p>\n

\"An<\/a><\/span><\/p>\n

\u201cFast Events in Protein Folding,\u201d R. B. Dyer, D. M. Vu. In: Edward H. Egelman, editor: Comprehensive Biophysics, Vol 3, The Folding of Proteins and Nucleic Acids, Valerie Daggett. Oxford: Academic Press, 2012<\/strong>, pp. 34-42. link<\/a><\/strong><\/span><\/p>\n

\u201cTime-resolved spectroscopic studies of protein dynamics,\u201d R. Callender; R. B. Dyer, in Encyclopedia of Biophysics<\/em>, Gordon C. K. Roberts, Editor, 2012<\/strong>.<\/span><\/p>\n

\u201cDifferential Ordering of the Protein Backbone and Side Chains during Protein Folding Revealed by Site-Specific Recombinant Infrared Probes S. Nagarajan, H. Taskent-Sezgin, D. Parul, I. Carrico, D. P. Raleigh, and R. B. Dyer, J. Am. Chem. Soc.<\/em> 2011<\/strong>, 133<\/em>, 20335\u201320340. PMC3241911<\/a><\/strong><\/span><\/p>\n

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Deng, H., D.V. Vu, K. Clinch, R. Desamero, R.B. Dyer, and R. Callender, Conformational heterogeneity within the Michaelis complex of lactate dehydrogenase <\/span>J. Phys. Chem. B<\/em>, <\/span>2011<\/strong>, 115 (23), pp 7670\u20137678. <\/span>link<\/strong><\/a><\/span><\/p>\n

\"Abstract
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\u201cImplementation of Time-Resolved Step-Scan Fourier Transform Infrared (FT-IR) Spectroscopy Using a kHz Repetition Rate Pump Laser\u201d, D. Magana, D. Parul, R. B. Dyer, A. P. Shreve, Appl. Spect.<\/em> 2011<\/strong>, 65<\/em>, 535-542. PMC3233350<\/a><\/strong><\/span><\/p>\n

\u201cFormation and Stabilization of Fluorescent Gold Nanoclusters Using Small Molecules\u201d Y. Bao, H.-C. Yeh, C. Zhong, S. A. Ivanov, J. K. Sharma, M. L. Neidig, D. M. Vu, A. P. Shreve, R. B. Dyer, J. H. Werner and J. S. Martinez, J. Phys. Chem. C<\/em> 2010<\/strong>, 11<\/em>, 15879-15882. link<\/strong><\/a><\/span><\/p>\n

\"Abstract
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\u201cAzidohomoalanine: A Conformationally Sensitive IR Probe of Protein Folding, Protein Structure and Electrostatics,\u201d H. Taskent-Sezgin, J. Chung, P. S. Banerjee, S. Nagarajan, R. B. Dyer, I. Carrico and D. P. Raleigh, Angew. Chem. IE<\/em> 2010<\/strong>, 49<\/em>, 7473\u20137475. (or Angew. Chem. <\/em>122, 7635-7637) PMC3233359<\/a><\/strong><\/span><\/p>\n

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 <\/p>\n

2000-2009<\/strong><\/span><\/p>\n

\u201cLaser-Induced Temperature Jump Infrared Measurements of RNA Folding,\u201d Dyer, RB; Brauns, EB, Methods in Enzymology: Biophysical, Chemical, and Functional Probes of RNA Structure, Interactions and Folding, Pt B<\/em> 2009<\/strong>, 469<\/em>, 353-372. PMC3233360<\/a><\/strong><\/span><\/p>\n

\u201cFabrication of fluorescent cellular probes: Hybrid dendrimer\/gold nanoclusters,\u201d Zhong, C; Bao, YP; Vu, DM; Dyer, RB; Martinez, JS Matls. Res. Soc. Symp. Proc.<\/em> 2008,<\/strong> 1007<\/em>, 265-270.<\/span><\/p>\n

\u201cOn the pathway of forming enzymatically productive ligand-protein complexes in lactate dehydrogenase,\u201d Deng, H., Brewer, S., Vu, D. M., Clinch, K., Callender, R., Dyer, R. B., <\/strong>Biophys. J.<\/em> 2008,<\/strong> 95, 804-813.<\/span><\/p>\n

\u201cA simple and economical method for the production of 13C, 18O-labeled Fmoc-amino acids with high levels of enrichment: applications to isotope-edited IR studies of proteins,\u201d J. Marecek, B. Song, S. Brewer, J. Belyea, R. B. Dyer and D. P. Raleigh, Org. Lett.<\/em> 2007<\/strong>, 9<\/em>, 4935-4937.<\/span><\/p>\n

R. B. Dyer and W. H. Woodruff (2007) \u201cVibrational Spectroscopy,\u201d in Applications of Physical Methods to Inorganic and Bioinorganic Chemistry edited by Robert A. Scott and Charles M. Lukehart. Chichester, UK: John Wiley & Sons, Ltd. pp. 489-512.<\/span><\/p>\n

\u201cNanoparticle free synthesis of fluorescent gold nanoclusters at physiological temperature,\u201d J. S. Martinez, Y. Bao, C. Zhong, D. M. Vu, J. P. Temirov, R. B. Dyer, J. Phys. Chem. C <\/em>2007<\/strong>, 111,<\/em> 12194-12198<\/a>. [1]<\/strong><\/span><\/p>\n

\u201cThe helix-turn-helix motif as an ultrafast independently folding domain: The pathway of folding of engrailed homeodomain,\u201d T. L. Religa, C. M. Johnson, D. M. Vu, S. H. Brewer, R. B. Dyer, A. R. Fersht, Proc. Natl. Acad. Sci. USA<\/em> 2007<\/strong>, 104<\/em>, 9272-9277. [10]<\/strong><\/span><\/p>\n

\u201cResidue Specific Resolution of Protein Folding Dynamics Using Isotope-Edited Infrared Temperature Jump Spectroscopy,\u201d S. H. Brewer, B. Song, D. P. Raleigh, and R. B. Dyer, Biochemistry<\/em> 2007<\/strong>, 46<\/em>, 3279-3285. [10]<\/strong><\/span><\/p>\n

\u201cUltrafast and Downhill Folding,\u201d R. B. Dyer, Curr. Opin. Struct. Biol. <\/em>2007<\/strong>, 17, 38-47. [6]<\/strong><\/span><\/p>\n

\u201cMicrofluidic Flow-Flash: Method for Investigating Protein Dynamics,\u201d M. W. Toepke, S. H. Brewer, D. M. Vu, K. D. Rector, J. E. Morgan, R. B. Gennis, P. J. A. Kenis, and R. B. Dyer, Anal. Chem.<\/em> 2007<\/strong>, 79<\/em>, 122-128. [4]<\/strong><\/span><\/p>\n

\u201cAdvances in time-resolved approaches to characterize the dynamical nature of enzymatic catalysis,\u201d R. H. Callender, R. B. Dyer, Chem. Rev.<\/em> 2006<\/strong>, 106<\/em>, 3031-3042. [11]<\/strong><\/span><\/p>\n

\u201cFourier Transform Hyperspectral Visible Imaging and the Nondestructive Analysis of Potentially Fraudulent Documents,\u201d E. B. Brauns and R. B. Dyer, Appl. Spect. <\/em>2006<\/strong>, 60<\/em>, 833-840. [1]<\/strong><\/span><\/p>\n

\u201cA two-dimensional view of the folding energy landscape of cytochrome c,\u201d J. H. Werner, R. Joggerst, R. Keller, R. B. Dyer, P. M. Goodwin, Proc. Natl. Acad. Sci. USA<\/em> 2006<\/strong>, 103<\/em>, 11130-11135. [9]<\/strong><\/span><\/p>\n

\u201cTime-resolved vibrational spectroscopy detects protein-based intermediates in the photosynthetic oxygen-evolving cycle,\u201d B. A. Barry, I. B. Cooper, A. DeRiso, S. H. Brewer, D. M. Vu, R. B. Dyer, Proc. Natl. Acad. Sci. USA<\/em> 2006<\/strong>, 103<\/em>, 7288-7291. [7]<\/strong><\/span><\/p>\n

\u201cNonequilibrium protein folding dynamics: laser-induced pH-jump studies of the helix\u2013coil transition,\u201d T. P. Causgrove and R. B. Dyer, Chem. Phys<\/em>. 2006<\/strong>, 323<\/em>, 2-10. [9]<\/strong><\/span><\/p>\n

\u201cEffect of modulating unfolded state structure on the folding kinetics of the villin headpiece subdomain,\u201d S. H. Brewer, D. M. Vu, Y. Tang, Y. Li, S. Franzen, D. P. Raleigh and R. B. Dyer, Proc. Natl. Acad. Sci. USA<\/em> 2005<\/strong>, 102<\/em>, 16662-16667. [18]<\/strong><\/span><\/p>\n

\u201cStudies of Helix Fraying and Solvation using 13C Isotopomers,\u201d R. M. Fesinmeyer, E. S. Peterson, R. B. Dyer and N. H. Andersen, Prot. Sci.<\/em> 2005<\/strong>, 14<\/em>, 2324-2332. [7]<\/strong><\/span><\/p>\n

\u201cTime-resolved infrared spectroscopy of RNA folding,\u201d E. B. Brauns, R. B. Dyer, Biophys. J. 2005<\/strong>, 89<\/em>, 3523-3530. [4]<\/strong><\/span><\/p>\n

\u201cHairpin folding dynamics: the cold denatured state is predisposed for rapid refolding, \u201c R. B. Dyer, S. J. Maness, S. Franzen, R. M. Fesinmeyer, K. A. Olsen, N. H. Andersen, Biochemistry<\/em> 2005,<\/strong> 44<\/em>, 10406 \u2013 10415. [16]<\/strong><\/span><\/p>\n

\u201cStructural Transformations in the Dynamics of Michaelis Complex Formation in Lactate Dehydrogenase,\u201d S. McClendon, D. M. Vu, K. Clinch, R. H. Callender, R. B. Dyer, Biophys. J. <\/em>2005<\/strong>, 89<\/em>, L7-L9. [7] PMC1289277<\/a><\/strong><\/span><\/p>\n

\u201cThe mechanism of b-hairpin formation,\u201d R. B. Dyer, S. J. Maness, E. S. Peterson, S. Franzen, R. M. Fesinmeyer, N. H. Andersen, Biochemistry<\/em> 2004<\/strong>, 43<\/em>, 11560-11566<\/a>. [37]<\/strong><\/span><\/p>\n

\u201cExperimental resolution of early steps in protein folding: testing MD simulations,\u201d D. M. Vu, E. S. Peterson, R. B. Dyer, J. Am. Chem. Soc.<\/em> 2004<\/strong>, 126<\/em>, 6546-6547. [13]<\/strong><\/span><\/p>\n

\u201cProbing the folding and unfolding dynamics of secondary and tertiary structures in a three-helix bundle protein,\u201d D. M. Vu, J. K. Myers, T. G. Oas, R. B. Dyer Biochemistry<\/em>, 2004<\/strong>, 43<\/em>, 3582-3589. [27]<\/strong><\/span><\/p>\n

\u201cFTIR Studies of Internal Proton Transfer Reactions Linked to Inter-heme Electron Transfer in Bovine Cytochrome c Oxidase,\u201d B. H. McMahon, M. Fabian, F. Tomson, T. P. Causgrove, J. A. Bailey, F. N. Rein, R. B. Dyer, G. Palmer, R. B. Gennis and W. H. Woodruff, Biochim. Biophys. Acta<\/em> 2004<\/strong>, 1655<\/em>, 321-331. [25]<\/strong><\/span><\/p>\n

\u201cNMR and Temperature Jump measurements of de novo <\/em>designed proteins demonstrate rapid folding in the absence of explicit selection for kinetics,\u201d B. Gillespie, D. M. Vu, P. S. Shah, S. A. Marshall, R. B. Dyer, S. L. Mayo, K. W. Plaxco, J. Mol. Biol<\/em>. 2003<\/strong>, 330<\/em>, 813-819. [25]<\/strong><\/span><\/p>\n

\u201cNanosecond temperature jump relaxation dynamics of cyclic b-hairpin peptides,\u201d S.J. Maness, S. Franzen, A. C. Gibbs, T. P. Causgrove and R. B. Dyer, Biophys. J.<\/em> 2003<\/strong>, 84<\/em>, 3874-3882. [18]<\/strong><\/span><\/p>\n

\u201cPrimary folding dynamics of sperm whale apomyoglobin: core formation,\u201d M. Gulotta, E. Rogatsky , R. H. Callender and R. B. Dyer, Biophys. J.<\/em> 2003<\/strong>, 84<\/em>, 1909-1918. [14]<\/strong><\/span><\/p>\n

\u201cProbing protein dynamics using temperature jump relaxation spectroscopy,\u201d Callender, R., Dyer, R.B. Curr. Opin. Struct. Biol.<\/em> 2002<\/strong>, 12<\/em>, 628-633. [27]<\/strong><\/span><\/p>\n

\u201cDirect Infrared Detection of the Covalently Ring-Linked His-Tyr Structure in the Active Site of the Heme-Copper Oxidases,\u201d F. Tomson, J. A. Bailey, R. B. Gennis, C. J. Unkefer, Z. Li, L. A. Silks, R. A. Martinez, R. J. Donohoe, R. B. Dyer, and W. H. Woodruff, Biochemistry<\/em> 2002<\/strong>, 41<\/em>, 14383-14390. [30]<\/strong><\/span><\/p>\n

\u201cTowards an Understanding of the Role of Dynamics on Enzymatic Catalysis in Lactate Dehydrogenase,\u201d M. Gulotta, H. Deng, H. Deng, R. B. Dyer, and R. H. Callender, Biochemistry<\/em> 2002<\/strong>, 41<\/em>, 3353-3363. [21]<\/strong><\/span><\/p>\n

\u201cTime-Resolved Step-Scan Fourier Transform Infrared Spectroscopy of the CO Adducts of Bovine Cytochrome c Oxidase and of Cytochrome bo3 from Escherichia coli<\/em>,\u201d J. A. Bailey, S. L. Mecklenburg, G. M. MacDonald, A. Katsonouri, A. Puustinen, M. Wikstr\u00f6m, R. B. Dyer, R. B. Gennis and W. H. Woodruff, Biochemistry<\/em> 2002<\/strong>, 41<\/em>, 2675-2683. [27]<\/strong><\/span><\/p>\n

\u201cPhotoacoustic cavitation and heat transfer effects in the laser-induced temperature jump in water,\u201d W. O. Wray, T. Aida, R. B. Dyer, Appl. Phys.B<\/em>. 2002<\/strong>, 74<\/em>, 57\u201366.<\/em> [25]<\/strong><\/span><\/p>\n

\u201cDynamics of the Primary processes of protein folding: Helix nucleation,\u201d J. H. Werner, R. B. Dyer, R. M. Fesinmeyer, N. H. Andersen, J. Phys. Chem. B <\/em>2002<\/strong>, 106, 487-494.<\/em> [47]<\/strong><\/span><\/p>\n

ldquo;There is communication between all four Ca2+ binding sites of Calcineurin B,\u201d S. C. Gallagher, Z.-H. Gao, S. Li, R. B. Dyer, J. Trewhella, C. B. Klee, Biochemistry<\/em> 2001<\/strong>, 40<\/em>, 12094-12102. [7]<\/strong><\/span><\/p>\n

\u201cHuman flap endonuclease-1: Conformational change upon binding to the flap DNA substrate and location of Mg2+ binding site,\u201d C.-Y. Kim, M. S. Park and R. B. Dyer, Biochemistry<\/em> 2001<\/strong>, 40<\/em>, 3208-3214. [14]<\/strong><\/span><\/p>\n

\u201cA Photolysis-Triggered Heme Ligand Switch in H93G Myoglobin,\u201d S. Franzen, J. Bailey, R. B. Dyer, W. H. Woodruff, R. B. Hu, M. R. Thomas, and S. G. Boxer, Biochemistry<\/em>2001<\/strong>, 40<\/em>, 5299-5305<\/a>. [14]<\/strong><\/span><\/p>\n

\u201cCore Formation in Apomyoglobin: Probing the Upper Reaches of the Folding Energy Landscape,\u201d R. B. Dyer, R. Gilmanshin, M. Gulotta, R. H. Callender, Biochemistry<\/em> 2001<\/strong>, 40<\/em>, 5137-5143. [28]<\/strong><\/span><\/p>\n

\u201cStructures of Apomyoglobin\u2019s Various Acid Destabilized Forms,\u201d R. Gilmanshin, M. Gulotta, R. B. Dyer, R. H. Callender, Biochemistry<\/em> 2001<\/strong>, 40<\/em>, 5127-5136. [26]<\/strong><\/span><\/p>\n

\u201cResonance Raman Studies of Heme Axial Ligation in H93G Myoglobin,\u201d S. Franzen, S. G. Boxer, R. B. Dyer and W. H. Woodruff, J. Phys. Chem. B<\/em> 2000<\/strong>, 104<\/em>, 10359-10367. [18]<\/strong><\/span><\/p>\n

\u201cProtein Folding and Unfolding on a Complex Energy Landscape,\u201d D. Thorn-Leeson, F. Gai, H.M. Rodriguez, L. M. Gregoret, R. B. Dyer, Proc. Natl. Acad. Sci. USA<\/em> 2000<\/strong>, 97<\/em>, 2527-2532. [66]<\/strong><\/span><\/p>\n

\u201cHigh Spatial Resolution for IR Imaging Using an IR Diode Laser,\u201d J. A. Bailey, R. B. Dyer, D. K Graff, J. R. Schoonover, Appl. Spect.<\/em> 2000<\/strong>, 54<\/em>, 159-163. [10]<\/strong><\/span><\/p>\n

Pre 2000<\/span><\/p>\n

\u201cEffect of Hexafluoroisoproponal on the Thermodynamics of Peptide Secondary Structure Formation,\u201d N. H. Andersen, R. B. Dyer, R. M. Fesinmeyer, F. Gai, Z. Liu, J. W. Neidign, H. Tong, J. Am. Chem. Soc.<\/em> 1999<\/strong>, 121<\/em>, 9879-9880. [40]<\/strong><\/span><\/p>\n

\u201cDependence of NO Recombination Dynamics on Solution Glycerol Content in Horse Myoglobin,\u201d A. P. Shreve, S. Franzen, M. C. Simpson, and R. B. Dyer, J. Phys. Chem. <\/em>1999<\/strong>, 103<\/em>, 7969-7975. [21]<\/strong><\/span><\/p>\n

\u201cMid-Infrared Spectrum of [Ru(phen)3]2+*,\u201d K. M. Omberg, J. R. Schoonover, S. Bernhard, J. A. Moss, J. A. Treadway, E. M. Kober, R. B. Dyer and T. J. Meyer, Inorg. Chem.<\/em> 1998<\/strong>, 37<\/em>, 3505-3508. [11]<\/strong><\/span><\/p>\n

\u201cThe Unusual Reactivities of Amphitrite Ornata<\/em> Dehaloperoxidase and Notomastus lobatus<\/em> Chloroperoxidase Do Not Arise From a Histidine Imidazolate Proximal Heme Iron Ligand,\u201d Franzen, S.; Roach, M. P.; Chen, Y.-P.; Dyer, R. B.; Woodruff, W.H.; Dawson, J.H. J. Am. Chem. Soc.<\/em> 1998<\/strong>, 120<\/em>, 4658-4661. [27]<\/strong><\/span><\/p>\n

\u201cThe Core of Apomyoglobin E-form Folds at the Diffusion Limit,\u201d Gilmanshin, R., Callender, R. H., Dyer, R. B. Nat. Struct. Biol. <\/em>1998<\/strong>, 5<\/em>, 363-365. [33]<\/strong><\/span><\/p>\n

\u201cInfrared Studies of Fast Events in Protein Folding,\u201d Dyer, R. B., Feng, G., Woodruff, W. H., Gilmanshin, R., Callender, R. H. Acc. Chem. Res. <\/em>1998<\/strong>, 31<\/em>, 709-716. [121]<\/strong><\/span><\/p>\n

\u201cFast Events in Protein Folding: The Time Evolution of Primary Processes,\u201d R. H. Callender, R. Gilmanshin, R.B. Dyer, and W.H. Woodruff, Ann. Rev. Phys. Chem.<\/em> 1998<\/strong>, 49<\/em>, 173-202. [142]<\/strong><\/span><\/p>\n

\u201cTime-Resolved Infrared Studies on Two Isomeric Ruthenium(II)\/Rhenium(I) Complexes Containing a Nonsymmetric Quaterpyridine Bridging Ligand,\u201d J. R. Schoonover, A. P. Shreve, R. B. Dyer, R. L. Cleary, M. D. Ward, C. A. Bignozzi, Inorg. Chem<\/em>. 1998<\/strong>, 37<\/em>,2598-2601. [8]<\/strong><\/span><\/p>\n

\u201cCyanide Binding and Active Site Structure in Heme-Copper Oxidases: Normal Coordinate Analysis of Iron-Cyanide Vibrations of a32+CN- Complexes of Cytochromes ba3<\/em> and aa3<\/em>,\u201d Y. Kim, G. T. Babcock, K.K. Surerus, J. A. Fee, R. B. Dyer, W. H. Woodruff, W. A. Oertling, Biospectroscopy<\/em> 1998<\/strong>, 4<\/em>, 1-15. [5]<\/strong><\/span><\/p>\n

\u201cBound Water in the Proton Translocation Mechanism of the Haem-Copper Oxidases,\u201d S. Riistama, G. Hummer, A. Puustinen, R. B. Dyer, W. H. Woodruff, M. Wikstrom, FEBS Lett.<\/em>1997<\/strong>, 414<\/em>, 275-280. [115]<\/strong><\/span><\/p>\n

\u201cFourier Transform Infrared Evidence for Connectivity Between CuB and Glutamic Acid 286 in Cytochrome bo3<\/em> from E. Coli<\/em>,\u201d A. Puustinen, J. A. Bailey, R. B. Dyer, S. L. Mecklenburg, M. Wikstrom, W. H. Woodruff Biochemistry<\/em> 1997<\/strong>,36<\/em>, 13195-13200. [106]<\/strong><\/span><\/p>\n

\u201cFast Events In Protein Folding: Relaxation Dynamics and Structure of the ‘I’ Form of Apomyoglobin,\u201d R. Gilmanshin, S. Williams, R. H. Callender, W. H. Woodruff and R. B. Dyer Biochemistry<\/em> 1997<\/strong>, 36<\/em>, 15006-12. [48]<\/strong><\/span><\/p>\n

\u201cMid-Infrared Spectrum of [Ru(bpy)3]2+*,\u201d K. M. Omberg, J. R. Schoonover, J. A. Treadway, R. M. Leasure, R. B. Dyer, T. J. Meyer J. Am. Chem. Soc.<\/em> 1997<\/strong>, 119<\/em>, 7013-7018. [43]<\/strong><\/span><\/p>\n

\u201cStructural Heterogeneity of the Various Forms of Apomyoglobin: Implications for Protein Folding,\u201d R. Gilmanshin, R. B. Dyer, and R. H. Callender, Protein Science<\/em> 1997<\/strong>, 6<\/em>, 2134-42. [34]<\/strong><\/span><\/p>\n

\u201cFast Events In Protein Folding: Relaxation Dynamics Of Secondary And Tertiary Structure In Native Apomyoglobin,\u201d R. Gilmanshin, S. Williams, R. H. Callender, W. H. Woodruff, and R. B. Dyer, Proc. Natl. Acad. Sci. USA<\/em>, 1997<\/strong>, 94<\/em>, 3709-3713. [155]<\/strong><\/span><\/p>\n

\u201cTime-Resolved, Step-Scan FTIR Spectroscopy of Excited-States of Transition Metal Complexes\u201d, Schoonover, J. R.; Strouse, G. F.; Omberg, K. M.; Dyer, R. B. Comments on Inorganic Chem.<\/em> 1996<\/strong>, 18<\/em>, 165-188. [54]<\/strong><\/span><\/p>\n

\u201cTrans Effects in Nitric Oxide Binding to Myoglobin Cavity Mutant H93G\u201d, Decatur, S. M.; Franzen, S.; DePillis, G. D.; Dyer, R. B.; Woodruff, W. H.; Boxer, S. G. Biochemistry<\/em>1996<\/strong>, 35<\/em>, 4939-44. [48]<\/strong><\/span><\/p>\n

\u201cPicosecond Structural Dynamics of Myoglobin Following Photolysis of Carbon Monoxide\u201d, T. P. Causgrove and R. B. Dyer, J. Phys. Chem<\/em>. 1996<\/strong>, 100<\/em>, 3273-7. [33]<\/strong><\/span><\/p>\n

\u201cApplication of Time-Resolved Vibrational Spectroscopy to the Study of Excited-State Intercomponent Processes in Supramolecular Systems\u201d, C. A. Bignozzi, J. R. Schoonover and R. B. Dyer, invited article, Comm. Inorg. Chem.<\/em>, 1996<\/strong>, 18<\/em>, 77-100. [12]<\/strong><\/span><\/p>\n

\u201cFast Events in Protein Folding: Helix Melting and Formation in a Small Peptide\u201d, S. Williams, T. P. Causgrove, R. Gilmanshin, K. S. Fang, R. H. Callender, W. H. Woodruff and R. B. Dyer, Biochemistry<\/em> 1996<\/strong>, 35<\/em>, 691-7. [490]<\/strong><\/span><\/p>\n

\u201cApplication of Time-Resolved Step-Scan Fourier Transform Infrared Spectroscopy to Excited-State Electronic Structure in Polypyridyl Complexes of Re(I)\u201d, J. R. Schoonover, G. F. Strouse, R. B. Dyer, W. D. Bates, P. Chen and T. J. Meyer, Inorg. Chem.<\/em> 1996<\/strong>, 35<\/em>, 273-4. [80]<\/strong><\/span><\/p>\n

\u201cFast events in protein folding initiated by laser-induced temperature jump and probed by time-resolved infrared spectroscopy\u201d, S. Williams, T. P. Causgrove, R. Gilmanshin, R. B. Dyer, W. H. Woodruff, R. H. Callender, Spectrosc. Biol. Mol., Eur. Conf., 6th (1995), Editor(s): Merlin, Jean Claude; Turrell, Sylvia; Huvenne, Jean Pierre. Publisher: Kluwer, Dordrecht, Neth. 105-6.<\/span><\/p>\n

\u201cProbing the fast events of protein folding\/unfolding\u201d, R. Callender, R. Gilmanshin, T. Causgrove, S. Williams, K. Fang, R. B. Dyer and W. Woodruff in “Frontiers in Interdisciplinary Physics: Biological Physics”, La Jolla International School of Physics, (1995).<\/span><\/p>\n

\u201cProtein Physics\u201d, R. Callender, R. Gilmanshin, B. Dyer and W. Woodruff, Physics World <\/em>1994<\/strong>, 7(8)<\/em>, 41-45. [10]<\/strong><\/span><\/p>\n

\u201cProtein response to ligation reactions in myoglobin,\u201d T. P. Causgrove & R. B. Dyer, Springer Proc. Phys.<\/em> 1994<\/strong>, 74 <\/em>(Time-Resolved Vibrational Spectroscopy VI), 262-5. [1]<\/strong><\/span><\/p>\n

\u201cSpectroscopic characterization of cytochrome ba3<\/em>, a terminal oxidase from Thermus thermophilus<\/em>: Comparison of the a3\/CuB site to that of bovine cytochrome aa3<\/em>\u201d Oertling, W. A.; Surerus, K. K.; Einarsdottir, O.; Fee, J. A.; Dyer, R. B.; Woodruff, W. H. Biochemistry<\/em> 1994<\/strong>, 33<\/em>, 3128-41. [38]<\/strong><\/span><\/p>\n

\u201cVibrational and Electronic Spectroscopy of Electronically Excited Polychromophoric Ruthenium (II) Complexes,\u201d C. A. Bignozzi, R. Argazzi, C. Chiorboli, F. Scandola, R. B. Dyer, J. R. Schoonover, T. J. Meyer, Inorg. Chem.<\/em> 1994<\/strong>, 33<\/em>, 1652-1659. [62]<\/strong><\/span><\/p>\n

\u201cApplication of Transient Resonance Raman Spectroscopy to the Structure of a Photoinduced Electron-Transfer Intermediate\u201d J. R. Schoonover, Chen, D. Bates, R. B. Dyer, and T. J. Meyer Inorg. Chem.<\/em> 1994<\/strong>, 33<\/em>, 793-797. [47]<\/strong><\/span><\/p>\n

\u201cPicosecond Infrared Study of the Photodynamics of Carbonmonoxy Cytochrome c Oxidase\u201d, R. B. Dyer, K. A. Peterson, P. O. Stoutland and W. H. Woodruff, Biochemistry<\/em>1994<\/strong>, 33<\/em>, 500-507.  [42]<\/strong><\/span><\/p>\n

\u201cProtein response to ligation reactions in myoglobin,\u201d T. P. Causgrove & R. B. Dyer, Proc. SPIE-Int. Soc. Opt. Eng.<\/em> 1993<\/strong>, 1890<\/em>(Biomolecular Spectroscopy III), 64-72.<\/span><\/p>\n

\u201cOxidation chemistry of energetic materials in supercritical water\u201d, Harradine, D. M.; Buelow, S.J.; Dell’Orco, P. C.; Dyer, R. B.; Foy, B. R.; Robinson, J. M.; Sanchez, J. A.; Spontarelli, T.; Wander, J.D. Hazard. Waste Hazard. Mater.<\/em> 1993<\/strong>, 10<\/em>, 233-46. [40]<\/strong><\/span><\/p>\n

\u201cPhotodissociation and Recombination of Carbonmonoxy Cytochrome Oxidase: Dynamics from Picoseconds to Kiloseconds\u201d, Einarsd\u00f3ttir, \u00b4O., Dyer, R.B., Killough, P.M., Fee, J.A., L\u00f3pez-Garriga, J.J., Atherton, S.J., Hubig, S.M., Palmer, G., and Woodruff, W. H., Biochemistry<\/em> 1993<\/strong>, 32<\/em>, 12013-12024. [94]<\/strong><\/span><\/p>\n

\u201cProtein Response to Photodissociation of CO from Carbonmonoxymyoglobin Probed by Time-Resolved Infrared of the Amide I Band\u201d, T. P. Causgrove and R. B. Dyer, Biochemistry<\/em> 1993<\/strong>, 32<\/em>, 11985-11991. [24]<\/strong><\/span><\/p>\n

\u201cIn Situ Raman Spectroscopy of Reactions in Supercritical Water,\u201d D. A. Masten, B. R. Foy, D. M. Harradine and R. B. Dyer, J. Phys. Chem.<\/em> 1993<\/strong>, 97<\/em>, 8557-8559. [33]<\/strong><\/span><\/p>\n

\u201cUltrafast Electron Transfer and Coupled Vibrational Dynamics in Cyanide Bridged Mixed-Valence Transition-Metal Dimers,\u201d S. K. Doorn, R. B. Dyer, P. O. Stoutland and W. H. Woodruff, J. Am. Chem. Soc.<\/em> 1993<\/strong>, 115<\/em>, 6398-6405. [83]<\/strong><\/span><\/p>\n

\u201cApplication of Transient Infrared Spectroscopy to intramolecular Energy Transfer in [(phen)(CO)3ReI(NC)RuII(CN)(bpy)2]+\u201d, J. R. Schoonover, K. C. Gordon, R. Argazzi, C. A. Bignozzi, R. B. Dyer, and T.J. Meyer, J. Am. Chem. Soc.<\/em> 1993<\/strong>,115<\/em>, 10996-7. [73]<\/strong><\/span><\/p>\n

\u201cIR Thermal Imaging of a Monkey’s Head: Local Temperature Changes in Response to Somatosensory Stimulation\u201d, J. S. George, J. D. Lewine, A. S. Goggin, R. B. Dyer and E. R. Flynn, Adv. Exp. Med. Biol.<\/em> 1993<\/strong>, 333<\/em>, 125-136. [5]<\/strong><\/span><\/p>\n

\u201cThe application of time-resolved step-scan FT-IR to the photodynamics of transition metal complexes and heme proteins\u201d, Palmer, R. A.; Plunkett, S. E.; Dyer, R. B.; Schoonover, J. R.; Meyer, T. J.; Chao, J. L. Proc.<\/em> SPIE-Int. Soc. Opt. Eng.<\/em> 1993<\/strong>, 2089<\/em>, 488-9. [1]<\/strong><\/span><\/p>\n

\u201cSpectroscopy, Dynamics and Function of Cytochrome Oxidase\u201d, W. H. Woodruff, R. B. Dyer and O. Einarsdottir, in “Biomolecular Spectroscopy” (Advances in Spectroscopy, v21, Part B) R. J. H. Clark and R. E. Hester, eds., London, John Wiley & Sons Ltd., pp. 189-233 (1993<\/strong>).<\/span><\/p>\n

\u201cPicosecond infrared study of carbonmonoxy cytochrome c oxidase: ligand transfer dynamics and binding orientations,\u201d K. A. Peterson, P. O. Stoutland, R. B. Dyer, and W. H. Woodruff, Springer Proc. Phys.<\/em> 1992<\/strong>, 68<\/em> (Time-Resolved Vib. Spectrosc. V), 24-7.<\/span><\/p>\n

\u201cResonance Raman studies of Rieske-type proteins,\u201d D. Kuila, J. R. Schoonover, R. B. Dyer, C. J. Batie, D. P. Ballou, J. A. Fee and W. H. Woodruff, Biochim. Biophys. Acta<\/em>1992<\/strong>, 1140<\/em>, 175-183. [41]<\/strong><\/span><\/p>\n

\u201cElectronic Coupling in Cyano-Bridged Ruthenium Polypyridine Complexes and Role of Electronic Effects on Cyanide Stretching Frequencies\u201d, C. A. Bignozzi, R. Argazzi, J. R. Schoonover, K. Gordon, R. B. Dyer, F. Scandola, Inorg. Chem.<\/em> 1992<\/strong>, 31<\/em>, 5260-5267. [138]<\/strong><\/span><\/p>\n

\u201cUltrafast Infrared Spectroscopy\u201d, P. O. Stoutland, R. B. Dyer, W. H. Woodruff, Science<\/em>1992<\/strong>, 257<\/em>, 1913-1917. [57]<\/strong><\/span><\/p>\n

\u201cPicosecond Infrared Study of Ultrafast Electron Transfer and Vibrational Energy Relaxation in a Mixed-Valent Ruthenium Dimer\u201d, Doorn, S. K.; Stoutland, P. O.; Dyer, R. B.; Woodruff, W. H. J. Am. Chem. Soc.<\/em> 1992<\/strong>, 114<\/em>, 3133-4. [60]<\/strong><\/span><\/p>\n

\u201cThe time-resolved infrared spectroscopy of Rh2(1,3-diisocyanopropane)4(BPh4)2\u201d, Doorn, S. K.; Gordon, K. C.; Dyer, R. B.; Woodruff, W. H. Inorg. Chem<\/em>. 1992<\/strong>, 31<\/em>, 2284-5. [15]<\/strong><\/span><\/p>\n

\u201cReaction of cyanide with cytochrome ba3<\/em> from Thermus thermophilus: spectroscopic characterization of the Fe(II)a3\u2022CN::CuB(II)\u2022CN complex indicates four N atoms are coordinated to CuB\u201d, Surerus, K. K.; Oertling, W. A.; Fan, C.; Gurbiel, R. J.; Einarsdottir, O.; Antholine, W. E.; Dyer, R. B.; Hoffman, B. M.; Woodruff, W. H.; Fee, J. A. Proc. Natl. Acad. Sci. U. S. A.<\/em> 1992<\/strong>, 89<\/em>, 3195-3199. [43]<\/strong><\/span><\/p>\n

\u201cNature and functional implications of the cytochrome a3<\/em> transients after photodissociation of carbon monoxide-cytochrome oxidase\u201d, Woodruff, W. H.; Einarsdottir, O.; Dyer, R. B.; Bagley, K. A.; Palmer, G.; Atherton, S. J.; Goldbeck, R. A.; Dawes, T. D.; Kliger, D. S. Proc. Natl. Acad. Sci. U. S. A.<\/em> 1991<\/strong>, 88(6)<\/em>, 2588-92. [126]<\/strong><\/span><\/p>\n

\u201cUltrafast photoinduced ligand transfer in carbonmonoxy cytochrome c oxidase. Observation by picosecond infrared spectroscopy\u201d, Dyer, R. B.; Peterson, K. A.; Stoutland, P. O.; Woodruff, W. H. J. Am. Chem. Soc<\/em>. 1991<\/strong>, 113(16)<\/em>, 6276-7. [41]<\/strong><\/span><\/p>\n

\u201cTime-resolved infrared studies of the dynamics of ligand binding to cytochrome c oxidase\u201d, Dyer, R. Brian; Peterson, Kristen A.; Stoutland, Page O.; Einarsdottir, Olof; Woodruff, William H. Proc. SPIE-Int. Soc. Opt. Eng.<\/em> 1991<\/strong>, 1432<\/em>(Biomol. Spectrosc. 2), 197-204.<\/span><\/p>\n

\u201cUltrafast and not-so fast dynamics of cytochrome oxidase: the ligand shuttle and its possible functional significance\u201d, Woodruff, William H.; Dyer, R. Brian; Einarsdottir, Olof; Peterson, K. A.; Stoutland, P. O.; Bagley, K. A.; Palmer, Graham; Schoonover, J. R.; Kliger, David S. Proc. SPIE-Int. Soc. Opt. Eng.<\/em> 1991<\/strong>, 1432<\/em>(Biomol. Spectrosc. 2), 205-10.<\/span><\/p>\n

\u201cNear-infrared-excitation resonance Raman spectra of the primary electron donor in photosynthetic reaction centers from Rhodobacter sphaeroides\u201d, Donohoe, R. J.; Dyer, R. B.; Swanson, B. I.; Violette, C. A.; Frank, H. A.; Bocian, D. F. J. Am. Chem. Soc.<\/em> 1990<\/strong>, 112(18)<\/em>, 6716-18. [32]<\/strong><\/span><\/p>\n

\u201cSpectroscopy and Structure of Quadruply Bonded Complexes Re2X82- (X = F, Cl and Br) and Mo2Cl4(PMe3)4 Under Extreme Pressure\u201d, D. E. Morris, C. D. Tait, R. B. Dyer, J. R. Schoonover, M. D. Hopkins, A. P. Sattelberger and W. H. Woodruff, Inorg. Chem.<\/em>1990<\/strong>, 29<\/em>, 3447-52. [4]<\/strong><\/span><\/p>\n

\u201cThe Red and Near-Infrared Resonance Raman Spectroscopy of Photo-Induced Defects in the Mixed-Valence Linear Chain Complex [PtII(en)2][PtIV(en)2Cl2][ClO4]4\u201d, R. J. Donohoe, R. B. Dyer and B. I. Swanson, Solid State Commun<\/em>. 1990<\/strong>, 73<\/em>, 521-5. [23]<\/strong><\/span><\/p>\n

\u201cFourier Transform Infrared and Resonance Raman Characterization of Cytochrome ba3 from Thermus Thermophilus<\/em>,\u201d \u00b4O. Einarsd\u00f3ttir, R. B. Dyer, P. M. Killough, J. A. Fee, and W. H. Woodruff, Proc. SPIE-Int. Soc. Opt. Eng.<\/em> 1989<\/strong>, 1055<\/em>, 254-62. [1]<\/strong><\/span><\/p>\n

\u201cThe Orientation of CO in Carbonmonoxy Cytochrome Oxidase and its Transient Photoproducts. Direct Evidence from Time-Resolved Infrared Linear Dichroism\u201d, R. B. Dyer, J. J. L\u00f3pez-Garriga, \u00b4O. Einarsd\u00f3ttir and W. H. Woodruff, J. Am. Chem. Soc<\/em>. 1989<\/strong>, 111<\/em>, 8962-3. [16]<\/strong><\/span><\/p>\n

\u201cTransient Binding of Photodissociated CO to CuB+ of Eukaryotic Cytochrome Oxidase at Ambient Temperature. Direct Evidence from Time-Resolved Infrared Spectroscopy\u201d, R. B. Dyer, P. M. Killough, \u00b4O. Einarsd\u00f3ttir, J. J. L\u00f3pez-Garriga and W. H. Woodruff, J. Am. Chem. Soc.<\/em> 1989<\/strong>, 111<\/em>, 7657-59. [93]<\/strong><\/span><\/p>\n

\u201cA Comparison of the Resonance Raman Properties of the Fast and Slow Forms of Cytochrome Oxidase\u201d, J. R. Schoonover, R. B. Dyer, W. H. Woodruff, G. M. Baker, M. Noguchi and G. Palmer, Biochemistry<\/em> 1988<\/strong>, 27<\/em>, 5433-40. [23]<\/strong><\/span><\/p>\n

\u201cResonance Raman Spectroscopy of Blue Copper Proteins,\u201d W. H. Woodruff, R. B. Dyer, and J. R. Schoonover, in “Biological Applications of Raman Spectroscopy,” vol. III, T. G. Spiro, Ed., New York, Wiley, 1988, pp. 413-439.<\/span><\/p>\n

\u201cCircular Dichroism Studies of the Solution Structures of Chiral Pyridine Substituted Crowns and Their Complexes\u201d, R. B. Dyer, R. G. Ghirardelli, R. A. Palmer, B. A. Jones and J. S. Bradshaw, J. Am. Chem. Soc.<\/em> 1987<\/strong>, 109<\/em>, 4780-4786. [14]<\/strong><\/span><\/p>\n

\u201cOptical Activity (CD and CPL) As a Probe of Ion Pairing and Solution Structure of Macrocycle Complexes\u201d, R. B. Dyer, R. A. Palmer, R. C. Carter, R. G. Ghirardelli and D. H. Metcalf, in “Understanding Molecular Properties”, A. E. Hansen, J. Avery and J. P. Dahl, Eds.; D. Riedel Publishing Co.: Boston, 1986.<\/span><\/p>\n

\u201cCrown Ether Complexed Ion Pairs: The Solution and Solid State Structures of the (2S,6S)-2,6-dimethyl-1,4,7,10,13,16-hexaoxacyclooctadecane Complex of Potassium Nitrate\u201d, R. B. Dyer, E. M. Holt, R. G. Ghirardelli and R. A. Palmer, Inorg. Chem.<\/em> 1986<\/strong>, 25<\/em>, 3184-3188. [16]<\/strong><\/span><\/p>\n

\u201cCircular Dichroism Studies of Crown Complexed Ion Pairs: A Comparison of the Alkali and Alkaline Earth Nitrate Complexes of Chiral Crown Ethers\u201d, R. B. Dyer, D. H. Metcalf, R. G. Ghirardelli, R. A. Palmer and E. M. Holt, J. Am. Chem. Soc.<\/em> 1986<\/strong>, 108<\/em>, 3621-3629. [32]<\/strong><\/span><\/p>\n","protected":false},"excerpt":{"rendered":"

Google Scholar Bibliography NCBI Pub Med Bibliography “Time-Resolved Infrared Spectroscopy Reveals the pH-Independence of the First Electron Transfer Step in the [FeFe] Hydrogenase Catalytic Cycle” M. L. K. Sanchez; S. Wiley; E. Reijerse; W. Lubitz; J. A. Birrell; and R. B. Dyer. J. Phys. Chem. Lett. 2022, link “Efficient, Light-Driven Reduction of CO2 to CO by a Carbon … <\/p>\n

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