Published in Proc Natl Acad Sci U S A on April 01, 1983
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Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering. Nat Methods (2008) 2.00
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Nanosecond optical rotatory dispersion spectroscopy: application to photolyzed hemoglobin-CO kinetics. Biophys J (1995) 0.87
Experiments on Hemoglobin in Single Crystals and Silica Gels Distinguish among Allosteric Models. Biophys J (2015) 0.86
The effect of water on the rate of conformational change in protein allostery. Biophys J (2001) 0.86
Spontaneous quaternary and tertiary T-R transitions of human hemoglobin in molecular dynamics simulation. PLoS Comput Biol (2010) 0.86
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The use of principal component analysis to resolve the spectra and kinetics of cytochrome c oxidase reduction by 5,10-dihydro-5-methyl phenazine. Biophys J (1985) 0.79
The Monod-Wyman-Changeux allosteric model accounts for the quaternary transition dynamics in wild type and a recombinant mutant human hemoglobin. Proc Natl Acad Sci U S A (2012) 0.79
Motion of proximal histidine and structural allosteric transition in soluble guanylate cyclase. Proc Natl Acad Sci U S A (2015) 0.79
Real-time tracking of CO migration and binding in the α and β subunits of human hemoglobin via 150-ps time-resolved Laue crystallography. Chem Phys (2013) 0.78
Linkage between ligand binding and the dimer-tetramer equilibrium in the Monod-Wyman-Changeux model of hemoglobin. Proc Natl Acad Sci U S A (1986) 0.77
Quaternary structure dynamics and carbon monoxide binding kinetics of hemoglobin valency hybrids. Biophys J (1996) 0.77
Five-coordinate H64Q neuroglobin as a ligand-trap antidote for carbon monoxide poisoning. Sci Transl Med (2016) 0.75
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Geminate recombination of O2 and hemoglobin. Proc Natl Acad Sci U S A (1980) 1.97
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Kinetics of hemoglobin and transition state theory. Proc Natl Acad Sci U S A (1978) 1.46
Transient Raman study of CO-haemoprotein photolysis: origin of the quantum yield. Nature (1980) 1.43
Stopped-flow, rapid mixing measurements of ligand binding to hemoglobin and red cells. Methods Enzymol (1981) 1.24
Differences in spectra of alpha and beta chains of hemoglobin between isolated state and in tetramer. J Biol Chem (1975) 1.11
A structural model for the kinetic behavior of hemoglobin. Science (1979) 1.11
Rate of quaternary structure change in hemoglobin measured by modulated excitation. Proc Natl Acad Sci U S A (1976) 1.02
Spin equilibrium and quaternary structure change in hemoglobin A. Experiments on a quantitative probe of the stereochemical mechanism of hemoglobin cooperativity. Biochemistry (1979) 1.02
Dependence of the quantum efficiency for photolysis of carboxyhemoglobin on the degree of ligation. J Biol Chem (1979) 1.01
Kinetic studies on the binding affinity of human hemoglobin for the 4th carbon monoxide molecule, L4. J Biol Chem (1976) 1.00
Transient haem-globin interactions in photodeligated carboxyhaemoglobin and subunits. Nature (1980) 0.91
Recombination kinetics following nanosecond laser photolysis of carbonmonoxyhaemogloblin. Biochim Biophys Acta (1982) 0.85
Folding dynamics and mechanism of beta-hairpin formation. Nature (1997) 7.30
The role of solvent viscosity in the dynamics of protein conformational changes. Science (1992) 4.52
A simple model for calculating the kinetics of protein folding from three-dimensional structures. Proc Natl Acad Sci U S A (1999) 4.51
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Kinetics of sickle hemoglobin polymerization. II. A double nucleation mechanism. J Mol Biol (1985) 3.74
Measuring the rate of intramolecular contact formation in polypeptides. Proc Natl Acad Sci U S A (2000) 3.64
Fast events in protein folding initiated by nanosecond laser photolysis. Proc Natl Acad Sci U S A (1993) 3.45
A statistical mechanical model for beta-hairpin kinetics. Proc Natl Acad Sci U S A (1998) 3.28
Kinetics and mechanism of deoxyhemoglobin S gelation: a new approach to understanding sickle cell disease. Proc Natl Acad Sci U S A (1974) 3.22
Laser temperature jump study of the helix<==>coil kinetics of an alanine peptide interpreted with a 'kinetic zipper' model. Biochemistry (1997) 2.83
Conformational relaxation and ligand binding in myoglobin. Biochemistry (1994) 2.71
Molecular dynamics simulations of cooling in laser-excited heme proteins. Proc Natl Acad Sci U S A (1986) 2.54
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Submillisecond protein folding kinetics studied by ultrarapid mixing. Proc Natl Acad Sci U S A (1997) 2.29
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Kinetic studies on photolysis-induced gelation of sickle cell hemoglobin suggest a new mechanism. Biophys J (1980) 2.18
Spectroscopic studies of oxy- and carbonmonoxyhemoglobin after pulsed optical excitation. Proc Natl Acad Sci U S A (1978) 2.15
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Thermodynamics of gelation of sickle cell deoxyhemoglobin. J Mol Biol (1977) 1.97
Molecular dynamics simulation of photodissociation of carbon monoxide from hemoglobin. Proc Natl Acad Sci U S A (1985) 1.94
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Protein reaction kinetics in a room-temperature glass. Science (1995) 1.77
Geminate recombination of carbon monoxide to myoglobin. J Mol Biol (1983) 1.75
Structure of hemoglobin S fibers: optical determination of the molecular orientation in sickled erythrocytes. Proc Natl Acad Sci U S A (1973) 1.72
Calorimetric and optical characterization of sickle cell hemoglobin gelation. J Mol Biol (1975) 1.67
Delay time of hemoglobin S polymerization prevents most cells from sickling in vivo. Science (1987) 1.61
Gelation of sickle cell hemoglobin in mixtures with normal adult and fetal hemoglobins. J Mol Biol (1979) 1.58
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Crystals of haemoglobin with the T quaternary structure bind oxygen noncooperatively with no Bohr effect. Nature (1991) 1.56
Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scattering. J Mol Biol (1999) 1.55
Kinetics of sickle hemoglobin polymerization. III. Nucleation rates determined from stochastic fluctuations in polymerization progress curves. J Mol Biol (1986) 1.55
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Single-crystal spectra of ferrimyoglobin complexes in polarized light. J Chem Phys (1968) 1.47
Reversible steps in the bacteriorhodopsin photocycle. Proc Natl Acad Sci U S A (1992) 1.40
A multiparameter analysis of sickle erythrocytes in patients undergoing hydroxyurea therapy. Blood (1996) 1.39
Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin. Proc Natl Acad Sci U S A (1991) 1.37
The effect of quaternary structure on the kinetics of conformational changes and nanosecond geminate rebinding of carbon monoxide to hemoglobin. Proc Natl Acad Sci U S A (1988) 1.36
Speed of intersubunit communication in proteins. Biochemistry (1992) 1.35
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Molecular dynamics simulations of fluorescence polarization of tryptophans in myoglobin. Proc Natl Acad Sci U S A (1987) 1.27
Editorial: Delay time of gelation: a possible determinant of clinical severity in sickle cell disease. Blood (1976) 1.26
Ligand binding and the gelation of sickle cell hemoglobin. J Mol Biol (1979) 1.25
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