Published in Biochemistry on March 16, 1982
Harmonic dynamics of proteins: normal modes and fluctuations in bovine pancreatic trypsin inhibitor. Proc Natl Acad Sci U S A (1983) 5.27
Molecular dynamics of myoglobin at 298 degrees K. Results from a 300-ps computer simulation. Biophys J (1985) 1.08
The study of conformational states of proteins by nuclear magnetic resonance. Biochem J (1985) 1.01
Scaling in biological nuclear magnetic resonance spectral distributions. Biophys J (1986) 0.75
Protein-Protein Interactions in DNA Recognition: H-NMR Studies of Lambda cI Repressors Genetically Altered by Site-Directed Mutagenesis. Biophys J (1986) 0.75
All-atom empirical potential for molecular modeling and dynamics studies of proteins. J Phys Chem B (1998) 54.00
CHARMM: the biomolecular simulation program. J Comput Chem (2009) 27.71
Crystallographic R factor refinement by molecular dynamics. Science (1987) 15.90
Effective energy function for proteins in solution. Proteins (1999) 9.44
Dynamics of folded proteins. Nature (1977) 7.82
How does a protein fold? Nature (1994) 7.55
Evaluation of comparative protein modeling by MODELLER. Proteins (1995) 6.42
Backbone-dependent rotamer library for proteins. Application to side-chain prediction. J Mol Biol (1993) 6.26
pKa's of ionizable groups in proteins: atomic detail from a continuum electrostatic model. Biochemistry (1990) 5.92
Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature (1997) 5.47
Harmonic dynamics of proteins: normal modes and fluctuations in bovine pancreatic trypsin inhibitor. Proc Natl Acad Sci U S A (1983) 5.27
Multiple conformational states of proteins: a molecular dynamics analysis of myoglobin. Science (1987) 4.89
Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc Natl Acad Sci U S A (1999) 4.71
The internal dynamics of globular proteins. CRC Crit Rev Biochem (1981) 4.59
Dynamics of proteins: elements and function. Annu Rev Biochem (1983) 4.56
Collective motions in proteins: a covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations. Proteins (1991) 4.53
The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature (1992) 4.32
Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques. Biochemistry (1999) 4.12
Protein-folding dynamics. Nature (1976) 4.11
"New view" of protein folding reconciled with the old through multiple unfolding simulations. Science (1997) 3.93
Amyloid fibrils from muscle myoglobin. Nature (2001) 3.93
Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J (1999) 3.72
Modern spectrum analysis in nuclear magnetic resonance: alternatives to the Fourier transform. Methods Enzymol (1989) 3.62
Amyloid fibril formation by an SH3 domain. Proc Natl Acad Sci U S A (1998) 3.55
X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 A resolution. J Mol Biol (1986) 3.49
Ion transport in a model gramicidin channel. Structure and thermodynamics. Biophys J (1991) 3.38
Solvent effects on protein motion and protein effects on solvent motion. Dynamics of the active site region of lysozyme. J Mol Biol (1989) 3.37
Picosecond dynamics of tyrosine side chains in proteins. Biochemistry (1979) 3.35
Dynamics of ligand binding to heme proteins. J Mol Biol (1979) 3.35
Polar hydrogen positions in proteins: empirical energy placement and neutron diffraction comparison. Proteins (1988) 3.30
Conformational analysis of the backbone-dependent rotamer preferences of protein sidechains. Nat Struct Biol (1994) 3.20
Kinetics of protein folding. A lattice model study of the requirements for folding to the native state. J Mol Biol (1994) 3.16
Three key residues form a critical contact network in a protein folding transition state. Nature (2001) 3.09
Understanding beta-hairpin formation. Proc Natl Acad Sci U S A (1999) 3.01
Discrimination of the native from misfolded protein models with an energy function including implicit solvation. J Mol Biol (1999) 2.99
Dynamical theory of activated processes in globular proteins. Proc Natl Acad Sci U S A (1982) 2.94
Locally accessible conformations of proteins: multiple molecular dynamics simulations of crambin. Protein Sci (1998) 2.94
Effective energy functions for protein structure prediction. Curr Opin Struct Biol (2000) 2.92
Detection of transient protein folding populations by mass spectrometry. Science (1993) 2.85
Solvent mobility and the protein 'glass' transition. Nat Struct Biol (2000) 2.83
The hinge-bending mode in lysozyme. Nature (1976) 2.78
Understanding protein folding via free-energy surfaces from theory and experiment. Trends Biochem Sci (2000) 2.73
Hidden thermodynamics of mutant proteins: a molecular dynamics analysis. Science (1989) 2.72
Improved resolution in triple-resonance spectra by nonlinear sampling in the constant-time domain. J Biomol NMR (1994) 2.72
Molecular dynamics simulations of the gramicidin channel. Annu Rev Biophys Biomol Struct (1994) 2.65
An analysis of incorrectly folded protein models. Implications for structure predictions. J Mol Biol (1984) 2.64
Forced unfolding of fibronectin type 3 modules: an analysis by biased molecular dynamics simulations. J Mol Biol (1999) 2.61
Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop. Science (1990) 2.60
Normal modes for specific motions of macromolecules: application to the hinge-bending mode of lysozyme. Proc Natl Acad Sci U S A (1985) 2.58
Side-chain torsional potentials: effect of dipeptide, protein, and solvent environment. Biochemistry (1979) 2.57
Prediction of the folding of short polypeptide segments by uniform conformational sampling. Biopolymers (1987) 2.53
Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations. J Mol Biol (1996) 2.50
The contribution of vibrational entropy to molecular association. The dimerization of insulin. J Mol Biol (1994) 2.45
Small-world view of the amino acids that play a key role in protein folding. Phys Rev E Stat Nonlin Soft Matter Phys (2002) 2.43
Active site dynamics in protein molecules: a stochastic boundary molecular-dynamics approach. Biopolymers (1985) 2.43
Interpreting the folding kinetics of helical proteins. Nature (1999) 2.39
Calculation of pi-pi excited state conformations and vibronic structure of retinal and related molecules. J Am Chem Soc (1974) 2.36
Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nat Struct Biol (1999) 2.34
Structural determinants of protein dynamics: analysis of 15N NMR relaxation measurements for main-chain and side-chain nuclei of hen egg white lysozyme. Biochemistry (1995) 2.31
Thermal expansion of a protein. Biochemistry (1987) 2.25
Early postnatal dexamethasone treatment and increased incidence of cerebral palsy. Arch Dis Child Fetal Neonatal Ed (2000) 2.24
Unfolding proteins by external forces and temperature: the importance of topology and energetics. Proc Natl Acad Sci U S A (2000) 2.24
Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy. Protein Sci (2000) 2.23
Protein secondary structure prediction with a neural network. Proc Natl Acad Sci U S A (1989) 2.21
A dynamic model for the allosteric mechanism of GroEL. J Mol Biol (2000) 2.20
Effect of anisotropy and anharmonicity on protein crystallographic refinement. An evaluation by molecular dynamics. J Mol Biol (1986) 2.16
Effects of macromolecular crowding on protein folding and aggregation. EMBO J (1999) 2.15
Sidechain torsional potentials and motion of amino acids in porteins: bovine pancreatic trypsin inhibitor. Proc Natl Acad Sci U S A (1975) 2.14
Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin. Biochemistry (1989) 2.11
A mathematical model for structure-function relations in hemoglobin. J Mol Biol (1972) 2.10
Functionality maps of binding sites: a multiple copy simultaneous search method. Proteins (1991) 2.08
Dynamics of DNA oligomers. J Biomol Struct Dyn (1983) 2.08
The allosteric mechanism of the chaperonin GroEL: a dynamic analysis. Proc Natl Acad Sci U S A (1998) 2.07
The fundamentals of protein folding: bringing together theory and experiment. Curr Opin Struct Biol (1999) 2.05
Following protein folding in real time using NMR spectroscopy. Nat Struct Biol (1995) 2.04
Domain association in immunoglobulin molecules. The packing of variable domains. J Mol Biol (1985) 2.03
Protein structural fluctuations during a period of 100 ps. Nature (1979) 1.96
Molecular switch in signal transduction: reaction paths of the conformational changes in ras p21. Proc Natl Acad Sci U S A (1997) 1.95
Fluorescence depolarization of tryptophan residues in proteins: a molecular dynamics study. Biochemistry (1983) 1.93
Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain. J Mol Biol (2000) 1.90
Folding thermodynamics of a model three-helix-bundle protein. Proc Natl Acad Sci U S A (1997) 1.89
A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modules. J Mol Biol (1997) 1.89
Molecular dynamics of an alpha-helical polypeptide: Temperature dependence and deviation from harmonic behavior. Proc Natl Acad Sci U S A (1982) 1.89
A refined solution structure of hen lysozyme determined using residual dipolar coupling data. Protein Sci (2001) 1.88
Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry. J Mol Biol (1998) 1.88
Mutational analysis of the propensity for amyloid formation by a globular protein. EMBO J (2000) 1.86
Solution conformations and thermodynamics of structured peptides: molecular dynamics simulation with an implicit solvation model. J Mol Biol (1998) 1.85
Ion transport in the gramicidin channel: molecular dynamics study of single and double occupancy. Biophys J (1995) 1.83
Dynamics of myoglobin: comparison of simulation results with neutron scattering spectra. Proc Natl Acad Sci U S A (1990) 1.82
Mechanism of tertiary structural change in hemoglobin. Proc Natl Acad Sci U S A (1977) 1.82
Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell. EMBO J (2000) 1.81
Electronic structure of cyanide complexes of hemes and heme proteins. J Mol Biol (1971) 1.79
Hydrogen exchange in native and denatured states of hen egg-white lysozyme. Proteins (1992) 1.79
Crystal structures of two closely related but antigenically distinct HLA-A2/melanocyte-melanoma tumor-antigen peptide complexes. J Immunol (2001) 1.77
Uracil-DNA glycosylase acts by substrate autocatalysis. Nature (2001) 1.77
Molecular dynamics simulation of protein denaturation: solvation of the hydrophobic cores and secondary structure of barnase. Proc Natl Acad Sci U S A (1994) 1.76
A residue-specific NMR view of the non-cooperative unfolding of a molten globule. Nat Struct Biol (1997) 1.76
Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea. Biochemistry (1997) 1.75