Published in Anal Biochem on July 01, 2002
The efficiency of different salts to screen charge interactions in proteins: a Hofmeister effect? Biophys J (2004) 1.13
Electrostatic contributions to the stability of the GCN4 leucine zipper structure. J Mol Biol (2007) 0.97
Osmolyte-induced folding of an intrinsically disordered protein: folding mechanism in the absence of ligand. Biochemistry (2010) 0.94
Probing the influence on folding behavior of structurally conserved core residues in P. aeruginosa apo-azurin. Protein Sci (2004) 0.86
Effect of temperature and guanidine hydrochloride on ferrocytochrome c at neutral pH. J Biol Inorg Chem (2003) 0.86
Contribution of individual histidines to the global stability of human prolactin. Protein Sci (2009) 0.85
Detection of native-state nonadditivity in double mutant cycles via hydrogen exchange. J Am Chem Soc (2010) 0.80
Experimental identification of downhill protein folding. Science (2002) 2.43
Probing the chemistry of thioredoxin catalysis with force. Nature (2007) 2.17
Estimating free-energy barrier heights for an ultrafast folding protein from calorimetric and kinetic data. J Phys Chem B (2008) 1.34
Single-molecule paleoenzymology probes the chemistry of resurrected enzymes. Nat Struct Mol Biol (2011) 1.32
Hyperstability and substrate promiscuity in laboratory resurrections of Precambrian β-lactamases. J Am Chem Soc (2013) 1.32
Role of residual structure in the unfolded state of a thermophilic protein. Proc Natl Acad Sci U S A (2003) 1.27
Exploring protein-folding ensembles: a variable-barrier model for the analysis of equilibrium unfolding experiments. Proc Natl Acad Sci U S A (2004) 1.21
L-phenylalanine binding and domain organization in human phenylalanine hydroxylase: a differential scanning calorimetry study. Biochemistry (2002) 1.20
Robustness of downhill folding: guidelines for the analysis of equilibrium folding experiments on small proteins. Biochemistry (2005) 1.18
Protein folding drives disulfide formation. Cell (2012) 1.18
Energetic evidence for formation of a pH-dependent hydrophobic cluster in the denatured state of Thermus thermophilus ribonuclease H. J Mol Biol (2003) 1.15
The efficiency of different salts to screen charge interactions in proteins: a Hofmeister effect? Biophys J (2004) 1.13
Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. J Mol Biol (2006) 1.12
Diversity of chemical mechanisms in thioredoxin catalysis revealed by single-molecule force spectroscopy. Nat Struct Mol Biol (2009) 1.11
Electrostatic interactions in ubiquitin: stabilization of carboxylates by lysine amino groups. Biochemistry (2002) 1.11
Relation between protein stability, evolution and structure, as probed by carboxylic acid mutations. J Mol Biol (2004) 1.10
Role of solvation barriers in protein kinetic stability. J Mol Biol (2006) 1.04
Expanding the realm of ultrafast protein folding: gpW, a midsize natural single-domain with alpha+beta topology that folds downhill. J Am Chem Soc (2008) 1.03
Thermodynamic and kinetic characterization of a germ line human lambda6 light-chain protein: the relation between unfolding and fibrillogenesis. J Mol Biol (2009) 0.98
Direct measurement of barrier heights in protein folding. J Am Chem Soc (2005) 0.97
Human cystathionine β-synthase (CBS) contains two classes of binding sites for S-adenosylmethionine (SAM): complex regulation of CBS activity and stability by SAM. Biochem J (2013) 0.96
Modulation of buried ionizable groups in proteins with engineered surface charge. J Am Chem Soc (2010) 0.95
Between-species variation in the kinetic stability of TIM proteins linked to solvation-barrier free energies. J Mol Biol (2008) 0.93
Role of low native state kinetic stability and interaction of partially unfolded states with molecular chaperones in the mitochondrial protein mistargeting associated with primary hyperoxaluria. Amino Acids (2010) 0.92
Dwell time analysis of a single-molecule mechanochemical reaction. Langmuir (2007) 0.91
Engineering proteins with tunable thermodynamic and kinetic stabilities. Proteins (2008) 0.91
Phenotypic comparisons of consensus variants versus laboratory resurrections of Precambrian proteins. Proteins (2014) 0.89
Conservation of protein structure over four billion years. Structure (2013) 0.87
Force-clamp spectroscopy detects residue co-evolution in enzyme catalysis. J Biol Chem (2008) 0.87
A designed protein as experimental model of primordial folding. Proc Natl Acad Sci U S A (2009) 0.87
Large-scale modulation of thermodynamic protein folding barriers linked to electrostatics. Proc Natl Acad Sci U S A (2008) 0.86
The effect of charge-introduction mutations on E. coli thioredoxin stability. Biophys Chem (2004) 0.85
A stability pattern of protein hydrophobic mutations that reflects evolutionary structural optimization. Biophys J (2005) 0.84
Energetic and structural consequences of desolvation/solvation barriers to protein folding/unfolding assessed from experimental unfolding rates. Biophys J (2006) 0.84
Using multi-objective computational design to extend protein promiscuity. Biophys Chem (2010) 0.83
Navigating the downhill protein folding regime via structural homologues. J Am Chem Soc (2010) 0.82
A simple tool to explore the distance distribution of correlated mutations in proteins. Biophys Chem (2005) 0.82
Structural and stability effects of phosphorylation: Localized structural changes in phenylalanine hydroxylase. Protein Sci (2004) 0.82
Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation. J Mol Biol (2004) 0.81
Dissecting structural and electrostatic interactions of charged groups in alpha-sarcin. An NMR study of some mutants involving the catalytic residues. Biochemistry (2003) 0.81
Empirical parametrization of pK values for carboxylic acids in proteins using a genetic algorithm. Biophys Chem (2004) 0.81
Mechanism of protein kinetic stabilization by engineered disulfide crosslinks. PLoS One (2013) 0.80
The peripheral binding of 14-3-3γ to membranes involves isoform-specific histidine residues. PLoS One (2012) 0.80
Role of conservative mutations in protein multi-property adaptation. Biochem J (2010) 0.80
Highly anomalous energetics of protein cold denaturation linked to folding-unfolding kinetics. PLoS One (2011) 0.80
Proteolytic scanning calorimetry: a novel methodology that probes the fundamental features of protein kinetic stability. Biophys J (2010) 0.80
Thermostable and promiscuous Precambrian proteins. Environ Microbiol (2014) 0.79
Probing the mutational interplay between primary and promiscuous protein functions: a computational-experimental approach. PLoS Comput Biol (2012) 0.79
Estimation of protein folding free energy barriers from calorimetric data by multi-model Bayesian analysis. Phys Chem Chem Phys (2011) 0.78
Different contribution of conserved amino acids to the global properties of triosephosphate isomerases. Proteins (2013) 0.78
Molecular determinants of expansivity of native globular proteins: a pressure perturbation calorimetry study. J Phys Chem B (2014) 0.77
How many ionizable groups can sit on a protein hydrophobic core? Proteins (2011) 0.77
Three-state thermal unfolding of onconase. Biophys Chem (2011) 0.77
Are protein folding intermediates the evolutionary consequence of functional constraints? J Phys Chem B (2015) 0.76
Beyond Lumry-Eyring: an unexpected pattern of operational reversibility/irreversibility in protein denaturation. Proteins (2008) 0.76