Published in Proc Natl Acad Sci U S A on May 26, 1998
A simple model for calculating the kinetics of protein folding from three-dimensional structures. Proc Natl Acad Sci U S A (1999) 4.51
The free energy landscape for beta hairpin folding in explicit water. Proc Natl Acad Sci U S A (2001) 4.39
Molecular dynamics simulations of unfolding and refolding of a beta-hairpin fragment of protein G. Proc Natl Acad Sci U S A (1999) 3.61
Can a continuum solvent model reproduce the free energy landscape of a beta -hairpin folding in water? Proc Natl Acad Sci U S A (2002) 3.41
Understanding beta-hairpin formation. Proc Natl Acad Sci U S A (1999) 3.01
Mechanisms and kinetics of beta-hairpin formation. Proc Natl Acad Sci U S A (2000) 2.66
Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution. Proc Natl Acad Sci U S A (2009) 2.02
Simulations of beta-hairpin folding confined to spherical pores using distributed computing. Proc Natl Acad Sci U S A (2002) 1.99
Chemical, physical, and theoretical kinetics of an ultrafast folding protein. Proc Natl Acad Sci U S A (2008) 1.90
Non-Arrhenius kinetics for the loop closure of a DNA hairpin. Proc Natl Acad Sci U S A (2001) 1.71
Measuring internal friction of an ultrafast-folding protein. Proc Natl Acad Sci U S A (2008) 1.69
A molecular dynamics study of the 41-56 beta-hairpin from B1 domain of protein G. Protein Sci (1999) 1.62
Transition-path sampling of beta-hairpin folding. Proc Natl Acad Sci U S A (2003) 1.61
Conformational transition states of a beta-hairpin peptide between the ordered and disordered conformations in explicit water. Protein Sci (2002) 1.58
Rate theories for biologists. Q Rev Biophys (2010) 1.44
Understanding the key factors that control the rate of beta-hairpin folding. Proc Natl Acad Sci U S A (2004) 1.40
Insights into nucleic acid conformational dynamics from massively parallel stochastic simulations. Biophys J (2003) 1.39
Entropic barriers, transition states, funnels, and exponential protein folding kinetics: a simple model. Protein Sci (2000) 1.34
Mechanical unfolding of a beta-hairpin using molecular dynamics. Biophys J (2000) 1.23
The turn sequence directs beta-strand alignment in designed beta-hairpins. Protein Sci (1999) 1.23
Fast-folding protein kinetics, hidden intermediates, and the sequential stabilization model. Protein Sci (2002) 1.21
Hydrophobic aided replica exchange: an efficient algorithm for protein folding in explicit solvent. J Phys Chem B (2006) 1.20
Folding mechanism of the (H3-H4)2 histone tetramer of the core nucleosome. Protein Sci (2004) 1.13
Hairpin folding rates reflect mutations within and remote from the turn region. Proc Natl Acad Sci U S A (2005) 1.07
beta-hairpin-forming peptides; models of early stages of protein folding. Biophys Chem (2010) 1.07
The role of the turn in beta-hairpin formation during WW domain folding. Protein Sci (2007) 1.05
Kinetic pathways of beta-hairpin (un)folding in explicit solvent. Biophys J (2004) 1.05
Nanosecond temperature jump relaxation dynamics of cyclic beta-hairpin peptides. Biophys J (2003) 1.04
Microscopic events in β-hairpin folding from alternative unfolded ensembles. Proc Natl Acad Sci U S A (2011) 1.03
Factors involved in the stability of isolated beta-sheets: Turn sequence, beta-sheet twisting, and hydrophobic surface burial. Protein Sci (2004) 1.02
Making connections between ultrafast protein folding kinetics and molecular dynamics simulations. Proc Natl Acad Sci U S A (2011) 1.00
Position effect of cross-strand side-chain interactions on beta-hairpin formation. Protein Sci (2000) 0.97
A cross-strand Trp Trp pair stabilizes the hPin1 WW domain at the expense of function. Protein Sci (2007) 0.97
Understanding beta-hairpin formation by molecular dynamics simulations of unfolding. Biophys J (2001) 0.93
Kinesin's biased stepping mechanism: amplification of neck linker zippering. Biophys J (2006) 0.92
Testing simplified proteins models of the hPin1 WW domain. Biophys J (2006) 0.92
The ensemble folding kinetics of the FBP28 WW domain revealed by an all-atom Monte Carlo simulation in a knowledge-based potential. Proteins (2011) 0.90
Binary and ternary aggregation within tethered protein constructs. Biophys J (2006) 0.90
What can one learn from experiments about the elusive transition state? Protein Sci (2004) 0.90
Raising the speed limit for β-hairpin formation. J Am Chem Soc (2012) 0.89
Folding mechanisms of individual beta-hairpins in a Go model of Pin1 WW domain by all-atom molecular dynamics simulations. J Chem Phys (2008) 0.88
Mesoscopic modeling for nucleic acid chain dynamics. Phys Rev E Stat Nonlin Soft Matter Phys (2005) 0.87
Folding domain B of protein A on a dynamically partitioned free energy landscape. Proc Natl Acad Sci U S A (2008) 0.85
Local vs global motions in protein folding. J Chem Theory Comput (2013) 0.84
Kinesin: a molecular motor with a spring in its step. Proc Biol Sci (2002) 0.84
How does a beta -hairpin fold/unfold? competition between topology and heterogeneity in a solvable model. Proc Natl Acad Sci U S A (2000) 0.81
Energy landscape and dynamics of the beta-hairpin G peptide and its isomers: Topology and sequences. Protein Sci (2003) 0.81
A minimum-reaction-flux solution to master-equation models of protein folding. J Chem Phys (2008) 0.80
Protein beta-sheet nucleation is driven by local modular formation. J Biol Chem (2010) 0.80
Folding mechanism of β-hairpin trpzip2: heterogeneity, transition state and folding pathways. Int J Mol Sci (2009) 0.80
Role of native-state topology in the stabilization of intracellular antibodies. Biophys J (2001) 0.79
Worm-like Ising model for protein mechanical unfolding under the effect of osmolytes. Biophys J (2012) 0.78
Engineering folding dynamics from two-state to downhill: application to λ-repressor. J Phys Chem B (2013) 0.78
Optimization of the GB/SA solvation model for predicting the structure of surface loops in proteins. J Phys Chem B (2006) 0.78
Flow-induced beta-hairpin folding of the glycoprotein Ibalpha beta-switch. Biophys J (2010) 0.78
Like-charged residues at the ends of oligoalanine sequences might induce a chain reversal. Biopolymers (2011) 0.77
Infrared study of the stability and folding kinetics of a series of β-hairpin peptides with a common NPDG turn. J Phys Chem B (2011) 0.77
Dependence of internal friction on folding mechanism. J Am Chem Soc (2015) 0.77
Enthalpic barriers dominate the folding and unfolding of the human Cu, Zn superoxide dismutase monomer. J Mol Biol (2012) 0.76
A study of the influence of charged residues on β-hairpin formation by nuclear magnetic resonance and molecular dynamics. Protein J (2014) 0.76
Combinatorial pattern discovery approach for the folding trajectory analysis of a beta-hairpin. PLoS Comput Biol (2005) 0.76
Residual interactions in unfolded bile acid-binding protein by 19F NMR. Protein Sci (2011) 0.76
Organization of the multiaminoacyl-tRNA synthetase complex and the cotranslational protein folding. Protein Sci (2015) 0.75
When fast is better: protein folding fundamentals and mechanisms from ultrafast approaches. Biochem J (2016) 0.75
Multiscale implementation of infinite-swap replica exchange molecular dynamics. Proc Natl Acad Sci U S A (2016) 0.75
Microscopic nucleation and propagation rates of an alanine-based α-helix. Phys Chem Chem Phys (2017) 0.75
Adaptive local learning in sampling based motion planning for protein folding. BMC Syst Biol (2016) 0.75
Thermodynamics of protein folding using a modified Wako-Saitô-Muñoz-Eaton model. J Biol Phys (2012) 0.75
Helix-coil transition in terms of Potts-like spins. Eur Phys J E Soft Matter (2013) 0.75
Modeling the mechanism of CLN025 beta-hairpin formation. J Chem Phys (2017) 0.75
Principles that govern the folding of protein chains. Science (1973) 23.40
Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins (1995) 14.36
Spin glasses and the statistical mechanics of protein folding. Proc Natl Acad Sci U S A (1987) 11.69
Principles of protein folding--a perspective from simple exact models. Protein Sci (1995) 7.54
Folding dynamics and mechanism of beta-hairpin formation. Nature (1997) 7.30
The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding. J Mol Biol (1992) 6.10
A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G. Science (1991) 6.00
The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding. J Mol Biol (1995) 5.00
The role of solvent viscosity in the dynamics of protein conformational changes. Science (1992) 4.52
Fast events in protein folding: helix melting and formation in a small peptide. Biochemistry (1996) 4.39
A short linear peptide that folds into a native stable beta-hairpin in aqueous solution. Nat Struct Biol (1994) 4.17
"New view" of protein folding reconciled with the old through multiple unfolding simulations. Science (1997) 3.93
Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding. Proc Natl Acad Sci U S A (1996) 3.85
Protein folding funnels: the nature of the transition state ensemble. Fold Des (1996) 3.46
Fast events in protein folding initiated by nanosecond laser photolysis. Proc Natl Acad Sci U S A (1993) 3.45
Stability of alpha-helices. Adv Protein Chem (1995) 3.36
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
Identification and characterization of the unfolding transition state of chymotrypsin inhibitor 2 by molecular dynamics simulations. J Mol Biol (1996) 2.52
Exploring the folding free energy surface of a three-helix bundle protein. Proc Natl Acad Sci U S A (1997) 2.38
ON THE KINETICS OF THE HELIX-COIL TRANSITION OF POLYPEPTIDES IN SOLUTION. J Mol Biol (1965) 2.13
Simple model of protein folding kinetics. Proc Natl Acad Sci U S A (1995) 2.11
Theoretical studies of protein-folding thermodynamics and kinetics. Curr Opin Struct Biol (1997) 2.01
Theoretical studies of protein folding and unfolding. Curr Opin Struct Biol (1995) 1.89
Theoretical predictions of folding pathways by using the proximity rule, with applications to bovine pancreatic trypsin inhibitor. Proc Natl Acad Sci U S A (1995) 1.73
Fast events in protein folding. Structure (1996) 1.56
DETERMINATION OF THE PARAMETERS FOR HELIX FORMATION IN POLY-gamma-BENZYL-L-GLUTAMATE. Proc Natl Acad Sci U S A (1959) 1.52
High-energy channeling in protein folding. Biochemistry (1997) 1.45
Helix design, prediction and stability. Curr Opin Biotechnol (1995) 1.36
Factors governing the foldability of proteins. Proteins (1996) 1.18
Kinetics of the helix-coil transition of a polypeptide with non-ionic side groups, derived from ultrasonic relaxation measurements. Biophys Chem (1979) 1.11
Fast events in protein folding: relaxation dynamics and structure of the I form of apomyoglobin. Biochemistry (1997) 1.02
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
Sickle cell hemoglobin polymerization. Adv Protein Chem (1990) 4.48
Fast kinetics and mechanisms in protein folding. Annu Rev Biophys Biomol Struct (2000) 3.90
Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding. Proc Natl Acad Sci U S A (1996) 3.85
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
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
Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering. Proc Natl Acad Sci U S A (1999) 2.53
Polarized absorption and linear dichroism spectroscopy of hemoglobin. Methods Enzymol (1981) 2.51
Kinetics of sickle hemoglobin polymerization. I. Studies using temperature-jump and laser photolysis techniques. J Mol Biol (1985) 2.49
Hemoglobin S gelation and sickle cell disease. Blood (1987) 2.41
Nanosecond absorption spectroscopy of hemoglobin: elementary processes in kinetic cooperativity. Proc Natl Acad Sci U S A (1983) 2.30
Submillisecond protein folding kinetics studied by ultrarapid mixing. Proc Natl Acad Sci U S A (1997) 2.29
Supersaturation in sickle cell hemoglobin solutions. Proc Natl Acad Sci U S A (1976) 2.19
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
Submillisecond kinetics of protein folding. Curr Opin Struct Biol (1997) 2.01
Electronic spectrum of single crystals of ferricytochrome-c. J Chem Phys (1967) 2.00
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
Is cooperative oxygen binding by hemoglobin really understood? Nat Struct Biol (1999) 1.92
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
Requirement for therapeutic inhibition of sickle haemoglobin gelation. Nature (1978) 1.58
Oxygen binding by sickle cell hemoglobin polymers. J Mol Biol (1982) 1.58
Fast events in protein folding. Structure (1996) 1.56
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
Photocycles of bacteriorhodopsin in light- and dark-adapted purple membrane studied by time-resolved absorption spectroscopy. Biophys J (1989) 1.49
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
Molecular and cellular pathogenesis of hemoglobin SC disease. Proc Natl Acad Sci U S A (1982) 1.32
Two-state expansion and collapse of a polypeptide. J Mol Biol (2000) 1.31
Polarized single crystal absorption spectra of carboxy- and oxyhemoglobin. Ann N Y Acad Sci (1973) 1.31
Dynamics of intramolecular contact formation in polypeptides: distance dependence of quenching rates in a room-temperature glass. Phys Rev Lett (2001) 1.28
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
The biophysics of sickle cell hydroxyurea therapy. Science (1995) 1.25
Photoselection in polarized photolysis experiments on heme proteins. Biophys J (1993) 1.23