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1
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0026449003
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Picosecond phase grating spectroscopy of hemoglobin and myoglobin: Energetics and dynamics of global protein motion
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Richard L., Genberg L., Deak J., Chiu H.-L., Miller R.J.D. Picosecond phase grating spectroscopy of hemoglobin and myoglobin: energetics and dynamics of global protein motion. Biochemistry. 31:1992;10703-10715.
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Richard, L.1
Genberg, L.2
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Chiu, H.-L.4
Miller, R.J.D.5
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2
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0000907487
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Direct observations of ligand dynamics in hemoglobin by subpicosecond infrared spectroscopy
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Anfinrud P.A., Han C., Hochstrasser R.M. Direct observations of ligand dynamics in hemoglobin by subpicosecond infrared spectroscopy. Proc Natl Acad Sci USA. 86:1989;8347-8351.
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Anfinrud, P.A.1
Han, C.2
Hochstrasser, R.M.3
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3
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0000125188
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Relaxation methods
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S.L. Friess, E.S. Lewis, & A. Weissberger. New York: Interscience
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Eigen M., De Maeyer L.D. Relaxation methods. Friess S.L., Lewis E.S., Weissberger A. Techniques of Organic Chemistry. 1963;895-1054 Interscience, New York.
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Techniques of Organic Chemistry
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Eigen, M.1
De Maeyer, L.D.2
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4
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0000914570
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Kinetics of ligand interaction
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San Francisco: WH Freeman and Company
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Cantor C.R., Schimmel P.R. Kinetics of ligand interaction. Biophysical Chemistry. 3:1980;849-1371 WH Freeman and Company, San Francisco.
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Cantor, C.R.1
Schimmel, P.R.2
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6
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0000810764
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Infrared studies of fast events in protein folding
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Dyer R.B., Gai F., Woodruff W., Gilmanshin R., Callender R.H. Infrared studies of fast events in protein folding. Acc Chem Res. 31:1998;709-716.
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Acc Chem Res
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Dyer, R.B.1
Gai, F.2
Woodruff, W.3
Gilmanshin, R.4
Callender, R.H.5
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9
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0030046906
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Fast events in protein folding: Helix melting and formation in a small peptide
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Williams S., Causgrove T.P., Gilmanshin R., Fang K.S., Callender R., Woodruff W., Dyer R.B. Fast events in protein folding: helix melting and formation in a small peptide. Biochemistry. 35:1996;691-697.
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Biochemistry
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Williams, S.1
Causgrove, T.P.2
Gilmanshin, R.3
Fang, K.S.4
Callender, R.5
Woodruff, W.6
Dyer, R.B.7
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10
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0030789351
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Laser temperature jump study of the helix-coil kinetics of an alanine peptide interpreted with a "kinetic zipper" model
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Thompson P.A., Eaton W.A., Hofrichter J. Laser temperature jump study of the helix-coil kinetics of an alanine peptide interpreted with a "kinetic zipper" model. Biochemistry. 36:1997;9200-9210.
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Thompson, P.A.1
Eaton, W.A.2
Hofrichter, J.3
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11
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0035339911
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Core formation in apomyoglobin: Probing the upper reaches of the folding energy landscape
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Gulotta M., Gilmanshin R., Callender R.H., Dyer R.B. Core formation in apomyoglobin: probing the upper reaches of the folding energy landscape. Biochemistry. 40:2001;5137-5143.
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(2001)
Biochemistry
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Gulotta, M.1
Gilmanshin, R.2
Callender, R.H.3
Dyer, R.B.4
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13
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0028290484
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Non-resonance Raman difference spectroscopy: A general probe of protein structure, ligand binding, enzymatic catalysis, and the structures of other biomacromolecules
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Callender R., Deng H. Non-resonance Raman difference spectroscopy: a general probe of protein structure, ligand binding, enzymatic catalysis, and the structures of other biomacromolecules. Annu Rev Biophys Biomol Struct. 23:1994;215-245.
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Callender, R.1
Deng, H.2
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14
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0037066140
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Towards an understanding of the role of dynamics on enzymatic catalysis in lactate dehydrogenase
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This paper sets forth isotope editing approaches in performing IR absorption spectroscopy that allow the measurement of the kinetic response of structure-specific bonds within a protein.
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Gulotta M., Deng H., Deng H., Dyer R.B., Callender R.H. Towards an understanding of the role of dynamics on enzymatic catalysis in lactate dehydrogenase. Biochemistry. 41:2002;3353-3363. This paper sets forth isotope editing approaches in performing IR absorption spectroscopy that allow the measurement of the kinetic response of structure-specific bonds within a protein.
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(2002)
Biochemistry
, vol.41
, pp. 3353-3363
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Gulotta, M.1
Deng, H.2
Deng, H.3
Dyer, R.B.4
Callender, R.H.5
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15
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0033582287
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Chemical ligation of folded recombinant proteins: Segmental isotopic labeling of domains for NMR studies
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Xu R., Ayers B., Cowburn D., Muir T.W. Chemical ligation of folded recombinant proteins: segmental isotopic labeling of domains for NMR studies. Proc Natl Acad Sci USA. 96:1999;388-393.
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Proc Natl Acad Sci USA
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Xu, R.1
Ayers, B.2
Cowburn, D.3
Muir, T.W.4
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16
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0035799367
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The dynamics of protein ligand binding on multiple time scales: NADH binding to lactate dehydrogenase
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This paper reveals the rich dynamical nature of the process of NADH binding to LDH.
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Deng H., Zhadin N., Callender R. The dynamics of protein ligand binding on multiple time scales: NADH binding to lactate dehydrogenase. Biochemistry. 40:2001;3767-3773. This paper reveals the rich dynamical nature of the process of NADH binding to LDH.
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(2001)
Biochemistry
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, pp. 3767-3773
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Deng, H.1
Zhadin, N.2
Callender, R.3
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18
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0035967901
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The time scale of the catalytic loop motion in triosephosphate isomerase
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Rozovsky S., McDermott A.E. The time scale of the catalytic loop motion in triosephosphate isomerase. J Mol Biol. 310:2001;259-270.
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(2001)
J Mol Biol
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Rozovsky, S.1
McDermott, A.E.2
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19
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0035967856
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Solution-state NMR investigations of triosephosphate isomerase active site loop motion: Ligand release in relation to active site loop dynamics
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Rozovsky S., Jogl G., Tong L., McDermott A.E. Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics. J Mol Biol. 310:2001;271-280.
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(2001)
J Mol Biol
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, pp. 271-280
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Rozovsky, S.1
Jogl, G.2
Tong, L.3
McDermott, A.E.4
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