Published in J Mol Biol on April 05, 1992
Cooperativity in protein-folding kinetics. Proc Natl Acad Sci U S A (1993) 2.87
Prediction of protein-folding mechanisms from free-energy landscapes derived from native structures. Proc Natl Acad Sci U S A (1999) 2.86
Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding. Proc Natl Acad Sci U S A (1994) 2.59
Phi-value analysis and the nature of protein-folding transition states. Proc Natl Acad Sci U S A (2004) 2.53
Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation. Biophys J (2001) 2.25
Evolution-like selection of fast-folding model proteins. Proc Natl Acad Sci U S A (1995) 1.83
Single versus parallel pathways of protein folding and fractional formation of structure in the transition state. Proc Natl Acad Sci U S A (1994) 1.78
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
Characterization of residual structure in the thermally denatured state of barnase by simulation and experiment: description of the folding pathway. Proc Natl Acad Sci U S A (1997) 1.51
Molecular simulations of cotranslational protein folding: fragment stabilities, folding cooperativity, and trapping in the ribosome. PLoS Comput Biol (2006) 1.50
Characterization of protein-folding pathways by reduced-space modeling. Proc Natl Acad Sci U S A (2007) 1.24
Solvation in protein folding analysis: combination of theoretical and experimental approaches. Proc Natl Acad Sci U S A (2004) 1.16
Determination of the folding transition states of barnase by using PhiI-value-restrained simulations validated by double mutant PhiIJ-values. Proc Natl Acad Sci U S A (2005) 1.05
Implicit solvation in the self-consistent mean field theory method: sidechain modelling and prediction of folding free energies of protein mutants. J Comput Aided Mol Des (2001) 1.04
Trimeric domain-swapped barnase. Proc Natl Acad Sci U S A (1999) 1.03
Kinetic epitope mapping of the chicken lysozyme.HyHEL-10 Fab complex: delineation of docking trajectories. Protein Sci (1998) 1.03
A kinetically significant intermediate in the folding of barnase. Proc Natl Acad Sci U S A (2000) 1.01
Phi-value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy. Proc Natl Acad Sci U S A (2007) 1.00
Refolding of barnase mutants and pro-barnase in the presence and absence of GroEL. EMBO J (1993) 0.99
UV-Vis spectroscopy of tyrosine side-groups in studies of protein structure. Part 2: selected applications. Biophys Rev (2016) 0.95
Using thioamides to site-specifically interrogate the dynamics of hydrogen bond formation in β-sheet folding. J Am Chem Soc (2012) 0.95
Absence of stable intermediates on the folding pathway of barnase. Proc Natl Acad Sci U S A (2000) 0.94
What can one learn from experiments about the elusive transition state? Protein Sci (2004) 0.90
Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways. Proc Natl Acad Sci U S A (1993) 0.89
From independent modules to molten globules: observations on the nature of protein folding intermediates. Proc Natl Acad Sci U S A (1993) 0.86
Effect of the protein import machinery at the mitochondrial surface on precursor stability. Proc Natl Acad Sci U S A (2000) 0.85
p25alpha is flexible but natively folded and binds tubulin with oligomeric stoichiometry. Protein Sci (2005) 0.85
Biological function in a non-native partially folded state of a protein. EMBO J (2008) 0.84
Surfing on protein folding energy landscapes. Proc Natl Acad Sci U S A (2002) 0.82
Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerization by human cytosolic cyclophilin (Cyp18). Protein Sci (1999) 0.81
Backbone dynamics of free barnase and its complex with barstar determined by 15N NMR relaxation study. J Biomol NMR (2000) 0.80
How general is the nucleation-condensation mechanism? Proteins (2008) 0.79
Mechanical Folding and Unfolding of Protein Barnase at the Single-Molecule Level. Biophys J (2016) 0.78
Temperature control for kinetic refolding of heat-denatured ovalbumin. Protein Sci (1997) 0.78
Real-time NMR studies on a transient folding intermediate of barstar. Protein Sci (1999) 0.78
Microscopic interpretation of folding ϕ-values using the transition path ensemble. Proc Natl Acad Sci U S A (2016) 0.76
An error analysis for two-state protein-folding kinetic parameters and phi-values: progress toward precision by exploring pH dependencies on Leffler plots. Biophys J (2008) 0.75
Fold and flexibility: what can proteins' mechanical properties tell us about their folding nucleus? J R Soc Interface (2015) 0.75
Characterization of the Folding of a 52-Knotted Protein Using Engineered Single-Tryptophan Variants. Biophys J (2016) 0.75
Engineering stability in gene networks by autoregulation. Nature (2000) 12.88
Positive feedback in eukaryotic gene networks: cell differentiation by graded to binary response conversion. EMBO J (2001) 7.03
Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry (1991) 6.55
Hydrogen bonding and biological specificity analysed by protein engineering. Nature (1985) 6.20
The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding. J Mol Biol (1992) 6.10
Mapping the transition state and pathway of protein folding by protein engineering. Nature (1989) 5.44
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 use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus). Cell (1984) 4.75
Rapid, electrostatically assisted association of proteins. Nat Struct Biol (1996) 4.72
Elucidating the folding problem of helical peptides using empirical parameters. Nat Struct Biol (1994) 4.66
A short linear peptide that folds into a native stable beta-hairpin in aqueous solution. Nat Struct Biol (1994) 4.17
Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles. J Mol Biol (1995) 3.76
Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins. J Mol Biol (1990) 3.40
The FHA domain is a modular phosphopeptide recognition motif. Mol Cell (1999) 3.16
The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. J Mol Biol (1992) 3.02
Structure-function-rescue: the diverse nature of common p53 cancer mutants. Oncogene (2007) 2.96
Rescuing the function of mutant p53. Nat Rev Cancer (2001) 2.95
Transient folding intermediates characterized by protein engineering. Nature (1990) 2.95
The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat Struct Biol (1999) 2.93
Thermodynamic stability of wild-type and mutant p53 core domain. Proc Natl Acad Sci U S A (1997) 2.90
Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: comparison with Zimm-Bragg and Lifson-Roig formalisms. Biopolymers (1997) 2.86
Obligatory steps in protein folding and the conformational diversity of the transition state. Nat Struct Biol (1998) 2.81
Elucidating the folding problem of alpha-helices: local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters. J Mol Biol (1998) 2.78
Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy. Oncogene (2000) 2.65
Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP binding. Nature (1982) 2.63
Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation. Biochemistry (1993) 2.61
Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding. Proc Natl Acad Sci U S A (1994) 2.59
Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles. Biochemistry (1990) 2.59
Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering. Biochemistry (1993) 2.54
Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comparison with experimental scales. Proteins (1994) 2.52
Strength and co-operativity of contributions of surface salt bridges to protein stability. J Mol Biol (1990) 2.52
Editing mechanisms in protein synthesis. Rejection of valine by the isoleucyl-tRNA synthetase. Biochemistry (1977) 2.48
Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2. Biochemistry (1993) 2.46
Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides. J Mol Biol (1995) 2.43
Protein-protein recognition: crystal structural analysis of a barnase-barstar complex at 2.0-A resolution. Biochemistry (1994) 2.38
Structure of the transition state for folding of a protein derived from experiment and simulation. J Mol Biol (1996) 2.36
Hydrogen exchange at equilibrium: a short cut for analysing protein-folding pathways? Trends Biochem Sci (1997) 2.36
Capping and alpha-helix stability. Nature (1989) 2.35
Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation. Proc Natl Acad Sci U S A (2000) 2.35
The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. J Mol Biol (1992) 2.34
Solution structure of a protein denatured state and folding intermediate. Nature (2005) 2.33
Energetics of complementary side-chain packing in a protein hydrophobic core. Biochemistry (1989) 2.33
Site-directed mutagenesis as a probe of enzyme structure and catalysis: tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutation. Biochemistry (1983) 2.31
Fidelity of replication of phage phi X174 DNA by DNA polymerase III holoenzyme: spontaneous mutation by misincorporation. Proc Natl Acad Sci U S A (1979) 2.31
Controlled proteolysis of tubulin by subtilisin: localization of the site for MAP2 interaction. Biochemistry (1984) 2.30
Kinetic basis of spontaneous mutation. Misinsertion frequencies, proofreading specificities and cost of proofreading by DNA polymerases of Escherichia coli. J Mol Biol (1982) 2.29
Semirational design of active tumor suppressor p53 DNA binding domain with enhanced stability. Proc Natl Acad Sci U S A (1998) 2.28
Design of a 20-amino acid, three-stranded beta-sheet protein. Science (1998) 2.27
Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability. J Mol Biol (1993) 2.26
Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding. Proc Natl Acad Sci U S A (1993) 2.25
Negative activation enthalpies in the kinetics of protein folding. Proc Natl Acad Sci U S A (1995) 2.24
Retracted Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold. Nature (2000) 2.21
Active site titration and aminoacyl adenylate binding stoichiometry of aminoacyl-tRNA synthetases. Biochemistry (1975) 2.18
Contribution of hydrophobic interactions to protein stability. Nature (1988) 2.18
Effect of active site residues in barnase on activity and stability. J Mol Biol (1992) 2.17
Folding of protein G B1 domain studied by the conformational characterization of fragments comprising its secondary structure elements. Eur J Biochem (1995) 2.15
Electrostatic enhancement of diffusion-controlled protein-protein association: comparison of theory and experiment on barnase and barstar. J Mol Biol (1998) 2.13
De novo design and structural analysis of a model beta-hairpin peptide system. Nat Struct Biol (1996) 2.13
Involvement of the carboxyl-terminal domain of tubulin in the regulation of its assembly. Proc Natl Acad Sci U S A (1984) 2.11
Conformational equilibria in -and -chymotrypsin. The energetics and importance of the salt bridge. J Mol Biol (1972) 2.07
The changing nature of the protein folding transition state: implications for the shape of the free-energy profile for folding. J Mol Biol (1998) 2.04
SmartCell, a framework to simulate cellular processes that combines stochastic approximation with diffusion and localisation: analysis of simple networks. Syst Biol (Stevenage) (2004) 2.03
Protein folding from a highly disordered denatured state: the folding pathway of chymotrypsin inhibitor 2 at atomic resolution. Proc Natl Acad Sci U S A (2001) 1.99
Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding. Biochemistry (1991) 1.98
Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. J Mol Biol (1992) 1.98
Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition. Biochemistry (1994) 1.97
Catalysis, binding and enzyme-substrate complementarity. Proc R Soc Lond B Biol Sci (1974) 1.94
Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates. J Mol Biol (1997) 1.94
Enzyme hyperspecificity. Rejection of threonine by the valyl-tRNA synthetase by misacylation and hydrolytic editing. Biochemistry (1976) 1.90
DNA polymerase accuracy and spontaneous mutation rates: frequencies of purine.purine, purine.pyrimidine, and pyrimidine.pyrimidine mismatches during DNA replication. Proc Natl Acad Sci U S A (1981) 1.90
Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2. Fold Des (1996) 1.90
Effect of alanine versus glycine in alpha-helices on protein stability. Nature (1992) 1.88
Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: a critical test of the protein engineering method of analysis. Biochemistry (1993) 1.86
Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. J Mol Biol (1992) 1.82
A structural model for GroEL-polypeptide recognition. Proc Natl Acad Sci U S A (1997) 1.82
Contribution of 3' leads to 5' exonuclease activity of DNA polymerase III holoenzyme from Escherichia coli to specificity. J Mol Biol (1983) 1.80
Stabilization of protein structure by interaction of alpha-helix dipole with a charged side chain. Nature (1988) 1.79
Quantitative determination of helical propensities from trifluoroethanol titration curves. Biochemistry (1994) 1.75
Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding. J Mol Biol (2000) 1.74
Hot-spot mutants of p53 core domain evince characteristic local structural changes. Proc Natl Acad Sci U S A (1999) 1.73
Rational modification of enzyme catalysis by engineering surface charge. Nature (1987) 1.71
Synergy between simulation and experiment in describing the energy landscape of protein folding. Proc Natl Acad Sci U S A (1998) 1.69
Oxidative refolding chromatography: folding of the scorpion toxin Cn5. Nat Biotechnol (1999) 1.69
Three-dimensional crystal structure of the transcription factor PhoB receiver domain. J Mol Biol (1999) 1.69
Co-operative interactions during protein folding. J Mol Biol (1992) 1.68
Stability and function: two constraints in the evolution of barstar and other proteins. Structure (1994) 1.67
Detection and characterization of a folding intermediate in barnase by NMR. Nature (1990) 1.64
Elucidating the folding problem of helical peptides using empirical parameters. III. Temperature and pH dependence. J Mol Biol (1995) 1.62
Stability and folding of the tumour suppressor protein p16. J Mol Biol (1999) 1.61
Fluorescence spectrum of barnase: contributions of three tryptophan residues and a histidine-related pH dependence. Biochemistry (1991) 1.60
Structural and energetic responses to cavity-creating mutations in hydrophobic cores: observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities. Biochemistry (1996) 1.60
Alternative pathways for editing non-cognate amino acids by aminoacyl-tRNA synthetases. Nucleic Acids Res (1981) 1.59
Thermodynamics of the interaction of barnase and barstar: changes in free energy versus changes in enthalpy on mutation. J Mol Biol (1997) 1.59
Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability. J Mol Biol (1992) 1.57