Published in Protein Sci on August 01, 1999
Protein folding and misfolding: mechanism and principles. Q Rev Biophys (2008) 1.68
Folding mechanism of the (H3-H4)2 histone tetramer of the core nucleosome. Protein Sci (2004) 1.13
Microsecond acquisition of heterogeneous structure in the folding of a TIM barrel protein. Proc Natl Acad Sci U S A (2008) 1.04
Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape. Biophys J (2005) 1.00
Domain stabilities in protein kinase R (PKR): evidence for weak interdomain interactions. Biochemistry (2008) 0.97
Unfolding studies on soybean agglutinin and concanavalin a tetramers: a comparative account. Biophys J (2004) 0.96
Structural analysis of kinetic folding intermediates for a TIM barrel protein, indole-3-glycerol phosphate synthase, by hydrogen exchange mass spectrometry and Gō model simulation. J Mol Biol (2007) 0.95
Topological frustration in beta alpha-repeat proteins: sequence diversity modulates the conserved folding mechanisms of alpha/beta/alpha sandwich proteins. J Mol Biol (2010) 0.91
The H2A.Z/H2B dimer is unstable compared to the dimer containing the major H2A isoform. Protein Sci (2005) 0.89
Microsecond barrier-limited chain collapse observed by time-resolved FRET and SAXS. J Mol Biol (2014) 0.89
The folding free-energy surface of HIV-1 protease: insights into the thermodynamic basis for resistance to inhibitors. J Mol Biol (2009) 0.88
NMR analysis of partially folded states and persistent structure in the alpha subunit of tryptophan synthase: implications for the equilibrium folding mechanism of a 29-kDa TIM barrel protein. J Mol Biol (2007) 0.86
Partially unfolded forms and non-two-state folding of a beta-sandwich: FHA domain from Arabidopsis receptor kinase-associated protein phosphatase. J Mol Biol (2006) 0.85
Thermodynamic characterization of yeast triosephosphate isomerase refolding: insights into the interplay between function and stability as reasons for the oligomeric nature of the enzyme. Biochem J (2003) 0.85
Partial NMR assignments and secondary structure mapping of the isolated alpha subunit of Escherichia coli tryptophan synthase, a 29-kD TIM barrel protein. Protein Sci (2003) 0.84
Interplay between drying and stability of a TIM barrel protein: a combined simulation-experimental study. J Am Chem Soc (2013) 0.81
Analysis of monomeric and dimeric phosphorylated forms of protein kinase R. Biochemistry (2010) 0.80
Rational stabilization of complex proteins: a divide and combine approach. Sci Rep (2015) 0.80
Long-range side-chain-main-chain interactions play crucial roles in stabilizing the (betaalpha)8 barrel motif of the alpha subunit of tryptophan synthase. Protein Sci (2007) 0.79
Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: Thermodynamic Stability Correlates with Rates of Unfolding Rather than Folding. J Biol Chem (2016) 0.78
Tracking Equilibrium and Nonequilibrium Shifts in Data with TREND. Biophys J (2017) 0.77
Lethal mutations in the major homology region and their suppressors act by modulating the dimerization of the rous sarcoma virus capsid protein C-terminal domain. Proteins (2012) 0.77
Folding and unfolding of gammaTIM monomers and dimers. Biophys J (2007) 0.76
Rat liver betaine-homocysteine S-methyltransferase equilibrium unfolding: insights into intermediate structure through tryptophan substitutions. Biochem J (2005) 0.75
Prediction of the secondary structure of proteins from their amino acid sequence. Adv Enzymol Relat Areas Mol Biol (1978) 29.77
Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol (1986) 12.22
Protein denaturation. Adv Protein Chem (1968) 11.58
Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci (1995) 9.23
Estimation of globular protein secondary structure from circular dichroism. Biochemistry (1981) 9.14
Intermediates in the folding reactions of small proteins. Annu Rev Biochem (1990) 6.42
Protein folding intermediates: native-state hydrogen exchange. Science (1995) 5.91
The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins (1989) 5.72
Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng (1993) 5.47
Molten globule and protein folding. Adv Protein Chem (1995) 4.33
Nucleotide sequences of trpA of Salmonella typhimurium and Escherichia coli: an evolutionary comparison. Proc Natl Acad Sci U S A (1979) 3.87
Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium. J Biol Chem (1988) 3.52
Laser temperature jump study of the helix<==>coil kinetics of an alanine peptide interpreted with a 'kinetic zipper' model. Biochemistry (1997) 2.83
NMR determination of residual structure in a urea-denatured protein, the 434-repressor. Science (1992) 2.83
Pathways of protein folding. Annu Rev Biochem (1993) 2.77
Side-chain entropy opposes alpha-helix formation but rationalizes experimentally determined helix-forming propensities. Proc Natl Acad Sci U S A (1992) 2.42
Hydrogen exchange: the modern legacy of Linderstrøm-Lang. Protein Sci (1997) 2.06
The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions. Nat Struct Biol (1997) 1.90
A continuous-flow capillary mixing method to monitor reactions on the microsecond time scale. Biophys J (1998) 1.87
Effect of point mutations on the folding of globular proteins. Methods Enzymol (1987) 1.87
Kinetic role of early intermediates in protein folding. Curr Opin Struct Biol (1997) 1.74
Protein denaturation: a small-angle X-ray scattering study of the ensemble of unfolded states of cytochrome c. Biochemistry (1998) 1.69
A peptide model of a protein folding intermediate. Nature (1988) 1.68
A protein dissection study of a molten globule. Biochemistry (1994) 1.44
Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels. Biochemistry (1999) 1.40
Ordered self-assembly of polypeptide fragments to form nativelike dimeric trp repressor. Science (1992) 1.36
Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of alpha-lactalbumin and lysozyme. Biochemistry (1986) 1.32
Protein folding and protein evolution: common folding nucleus in different subfamilies of c-type cytochromes? J Mol Biol (1998) 1.31
Dynamics of the quaternary conformational change in trout hemoglobin. Biochemistry (1991) 1.22
Nanosecond optical spectra of iron-cobalt hybrid hemoglobins: geminate recombination, conformational changes, and intersubunit communication. Biochemistry (1985) 1.22
Amide backbone and water-related H/D isotope effects on the dynamics of a protein folding reaction. Biochemistry (1997) 1.21
Resolution of multiphasic reactions by the combination of fluorescence total-intensity and anisotropy stopped-flow kinetic experiments. Biophys J (1994) 1.20
Relationship between thermodynamics and mechanism during photoinduced charge separation in reaction centers from Rhodobacter sphaeroides. Biochemistry (1994) 1.15
Tryptophan synthase from Escherichia coli and Salmonella typhimurium. Methods Enzymol (1987) 1.13
Touring the landscapes: partially folded proteins examined by hydrogen exchange. Structure (1997) 1.10
Characterization of folding intermediates of human carbonic anhydrase II: probing substructure by chemical labeling of SH groups introduced by site-directed mutagenesis. Biochemistry (1993) 1.10
Probing minimal independent folding units in dihydrofolate reductase by molecular dissection. Protein Sci (1997) 1.09
Characterization of a folding intermediate of apoplastocyanin trapped by proline isomerization. Biochemistry (1993) 1.05
Mapping the folding intermediate of human carbonic anhydrase II. Probing substructure by chemical reactivity and spin and fluorescence labeling of engineered cysteine residues. Biochemistry (1995) 1.02
An active proteolytic derivative of the alpha subunit of tryptophan synthase. Identification of the site of cleavage and characterization of the fragments. Biochemistry (1979) 0.99
Nonsequential unfolding of the alpha/beta barrel protein indole-3-glycerol-phosphate synthase. Biochemistry (1997) 0.96
Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthase. Biochemistry (1996) 0.95
The tryptophan synthase from Escherichia coli. An improved purification procedure for the alpha-subunit and binding studies with substrate analogues. Eur J Biochem (1975) 0.93
Guanidine hydrochloride induced unfolding of the alpha subunit of tryptophan synthase and of the two alpha proteolytic fragments: evidence for stepwise unfolding of the two alpha domains. Biochemistry (1982) 0.89
Further examination of the intermediate state in the denaturation of the tryptophan synthase alpha subunit. Evidence that the equilibrium denaturation intermediate is a molten globule. J Mol Biol (1993) 0.89
Stability of a thermophilic TIM-barrel enzyme: indole-3-glycerol phosphate synthase from the thermophilic archaeon Sulfolobus solfataricus. Biochem J (1997) 0.88
Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids. Biochemistry (1988) 0.88
Urea-induced unfolding of the alpha subunit of tryptophan synthase: evidence for a multistate process. Biochemistry (1981) 0.87
A test of the relationship between sequence and structure in proteins: excision of the heme binding site in apocytochrome b5. Protein Sci (1998) 0.87
Detection of an intermediate in the folding of the (beta alpha)8-barrel N-(5'-phosphoribosyl)anthranilate isomerase from Escherichia coli. Biochemistry (1994) 0.87
Urea-induced unfolding of the alpha subunit of tryptophan synthase: one-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration. Biochemistry (1993) 0.86
Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. Biochemistry (1993) 0.85
The B protein of Escherichia coli tryptophan synthetase. I. Effects of sulfhydryl modification on enzymatic activities and subunit interaction. J Biol Chem (1970) 0.84
Unfolding-refolding kinetics of the tryptophan synthase alpha subunit by CD and fluorescence measurements. J Mol Biol (1994) 0.84
The "pre-molten globule," a new intermediate in protein folding. J Protein Chem (1997) 0.82
Single-tryptophan mutants of monomeric tryptophan repressor: optical spectroscopy reveals nonnative structure in a model for an early folding intermediate. Biochemistry (1998) 0.80
Comparison of denaturation of tryptophan synthase alpha-subunits from Escherichia coli, Salmonella typhimurium, and an interspecies hybrid. Arch Biochem Biophys (1984) 0.79
Evidence for residual structures in an unfolded form of yeast phosphoglycerate kinase. Biochemistry (1995) 0.79
Steady state and time-resolved fluorescence study of residual structures in an unfolded form of yeast phosphoglycerate kinase. Biochemistry (1998) 0.77
Excimer fluorescence in liquid phenol, p-ethylphenol, and anisole. J Am Chem Soc (1965) 0.77
Aminoacyl-transfer RNA populations in mammalian cells chromatographic profiles and patterns of codon recognition. Biochim Biophys Acta (1979) 1.87
Effect of point mutations on the folding of globular proteins. Methods Enzymol (1987) 1.87
Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy. Biochemistry (1995) 1.78
Folding and stability of trp aporepressor from Escherichia coli. Biochemistry (1990) 1.59
Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants. Protein Sci (1993) 1.56
Folding of dihydrofolate reductase from Escherichia coli. Biochemistry (1986) 1.51
Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy. Biochemistry (1991) 1.47
Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels. Biochemistry (1999) 1.40
A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: verification and refinement of a four-channel model. Biochemistry (1993) 1.40
Barriers in protein folding reactions. Adv Protein Chem (2000) 1.24
Structure and stability of an early folding intermediate of Escherichia coli trp aporepressor measured by far-UV stopped-flow circular dichroism and 8-anilino-1-naphthalene sulfonate binding. Biochemistry (1993) 1.24
Preformed secondary structure drives the association reaction of GCN4-p1, a model coiled-coil system. J Mol Biol (2000) 1.23
Effect of single amino acid replacements on the folding and stability of dihydrofolate reductase from Escherichia coli. Biochemistry (1987) 1.22
Multistate equilibrium unfolding of Escherichia coli dihydrofolate reductase: thermodynamic and spectroscopic description of the native, intermediate, and unfolded ensembles. Biochemistry (2000) 1.19
The pentaammineruthenium(III)-histidine complex in ribonuclease A as an optical probe of conformational change. Biochim Biophys Acta (1980) 1.18
Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR. Protein Sci (1995) 1.16
Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL. Proc Natl Acad Sci U S A (1997) 1.10
Role of diffusion in the folding of the alpha subunit of tryptophan synthase from Escherichia coli. Biochemistry (1990) 1.10
Development of nonpolar surfaces in the folding of Escherichia coli dihydrofolate reductase detected by 1-anilinonaphthalene-8-sulfonate binding. Biochemistry (1994) 1.10
Probing minimal independent folding units in dihydrofolate reductase by molecular dissection. Protein Sci (1997) 1.09
Effects of multiple replacements at a single position on the folding and stability of dihydrofolate reductase from Escherichia coli. Biochemistry (1989) 1.06
Local and global dynamics during the folding of Escherichia coli dihydrofolate reductase by time-resolved fluorescence spectroscopy. Biochemistry (1995) 1.05
Long-range electrostatic interactions can influence the folding, stability, and cooperativity of dihydrofolate reductase. Biochemistry (1989) 1.04
Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein. Protein Sci (1999) 1.02
A strategy for testing the suitability of cysteine replacements in dihydrofolate reductase from Escherichia coli. J Biochem (1995) 1.00
Urea and thermal equilibrium denaturation studies on the dimerization domain of Escherichia coli Trp repressor. Biochemistry (1997) 1.00
Intramolecular catalysis of a proline isomerization reaction in the folding of dihydrofolate reductase. Biochemistry (1992) 0.98
Ligand binding is the principal determinant of stability for the p21(H)-ras protein. Biochemistry (1998) 0.98
Rehospitalization among home healthcare patients: results of a prospective study. Home Healthc Nurse (2001) 0.98
Thermodynamic properties of the transition state for the rate-limiting step in the folding of the alpha subunit of tryptophan synthase. Biochemistry (1994) 0.97
Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein. Biochemistry (1999) 0.97
Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthase. Biochemistry (1996) 0.95
Characterization of a slow folding reaction for the alpha subunit of tryptophan synthase. Proteins (1987) 0.95
The barriers in the bimolecular and unimolecular folding reactions of the dimeric core domain of Escherichia coli Trp repressor are dominated by enthalpic contributions. Biochemistry (1998) 0.94
Mapping the energy surface for the folding reaction of the coiled-coil peptide GCN4-p1. Biochemistry (2001) 0.94
Nuclear magnetic resonance study of the thermal denaturation of ribonuclease A: implications for multistate behavior at low pH. Proc Natl Acad Sci U S A (1973) 0.93
Testing the role of chain connectivity on the stability and structure of dihydrofolate reductase from E. coli: fragment complementation and circular permutation reveal stable, alternatively folded forms. Protein Sci (2001) 0.93
Effect of single amino acid substitutions on the thermal stability of the alpha subunit of tryptophan synthase. Biochemistry (1980) 0.93
Interresidue distance measurements in proteins. Fluorescent energy transfer between tryptophans and a Ru(III)(NH3)5-histidine complex in alpha-lytic protease and lysozyme. Biochim Biophys Acta (1982) 0.93
Tryptophan replacements in the trp aporepressor from Escherichia coli: probing the equilibrium and kinetic folding models. Protein Sci (1993) 0.93
Mechanism of folding of the dimeric core domain of Escherichia coli trp repressor: a nearly diffusion-limited reaction leads to the formation of an on-pathway dimeric intermediate. Biochemistry (1998) 0.92
Effect of a single amino acid substitution on the folding of the alpha subunit of tryptophan synthase. Biochemistry (1983) 0.92
The pentaammineruthenium(III)histidine complex in ribonuclease A: application to the assignment of histidine proton resonances. Anal Biochem (1981) 0.91
Construction and characterization of monomeric tryptophan repressor: a model for an early intermediate in the folding of a dimeric protein. Biochemistry (1997) 0.90
Amino acid replacements can selectively affect the interaction energy of autonomous folding units in the alpha subunit of tryptophan synthase. Biochemistry (1992) 0.90
A hydrophobic cluster forms early in the folding of dihydrofolate reductase. Proteins (1989) 0.89
Mutant sequences as probes of protein folding mechanisms. Bioessays (1987) 0.89
Rough energy landscapes in protein folding: dimeric E. coli Trp repressor folds through three parallel channels. J Mol Biol (2001) 0.89
Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids. Biochemistry (1988) 0.88
Characterization of the slow folding reactions of trp aporepressor from Escherichia coli by mutational analysis of prolines and catalysis by a peptidyl-prolyl isomerase. Biochemistry (1995) 0.87
Unraveling the mechanism of protein folding: new tricks for an old problem. Protein Eng (1993) 0.87
Mutagenic and toxic effects of ruthenium. Chem Biol Interact (1980) 0.87
Synergism in folding of a double mutant of the alpha subunit of tryptophan synthase. Biochemistry (1986) 0.87
Urea-induced unfolding of the alpha subunit of tryptophan synthase: evidence for a multistate process. Biochemistry (1981) 0.87
1H, 15N and 13C resonance assignments, secondary structure, and the conformation of substrate in the binary folate complex of Escherichia coli dihydrofolate reductase. J Biomol NMR (1994) 0.87
Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein. Biochemistry (1999) 0.87
Urea-induced unfolding of the alpha subunit of tryptophan synthase: one-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration. Biochemistry (1993) 0.86
Detection of a stable intermediate in the thermal unfolding of a cysteine-free form of dihydrofolate reductase from Escherichia coli. Biochemistry (1995) 0.85
Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase. Biochemistry (1993) 0.85
Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time. Biochemistry (1999) 0.85
Mutational analysis of protein folding mechanisms. Methods Enzymol (1991) 0.84
Collapse of parallel folding channels in dihydrofolate reductase from Escherichia coli by site-directed mutagenesis. Biochemistry (1993) 0.83
Characterization of an early intermediate in the folding of the alpha subunit of tryptophan synthase by hydrogen exchange measurement. Biochemistry (1985) 0.82
Folding under the influence. Nat Struct Biol (1999) 0.81
Proline isomerization and the slow folding reactions of the alpha subunit of tryptophan synthase from Escherichia coli. Biochim Biophys Acta (1987) 0.81
Multiple replacements at position 211 in the alpha subunit of tryptophan synthase as a probe of the folding unit association reaction. Biochemistry (1990) 0.81
The role of ligand binding in the kinetic folding mechanism of human p21(H-ras) protein. Biochemistry (1998) 0.81
Nuclear magnetic resonance studies of residual structure in thermally unfolded ribonuclease A. Biochemistry (1975) 0.80
Single-tryptophan mutants of monomeric tryptophan repressor: optical spectroscopy reveals nonnative structure in a model for an early folding intermediate. Biochemistry (1998) 0.80
Nuclear magnetic resonance titration curves of histidine ring protons. The effect of temperature on ribonuclease A. J Biol Chem (1975) 0.79
Construction and characterization of a single polypeptide chain containing two enzymatically active dihydrofolate reductase domains. Protein Eng (1992) 0.79
Prediction of the tertiary structure of the alpha-subunit of tryptophan synthase. Proteins (1987) 0.78
A Fourier transform NMR study of the thermal denaturation of ribonuclease A at low pH. Ann N Y Acad Sci (1973) 0.78
Characterization of the tryptophan binding site of Escherichia coli tryptophan holorepressor by phosphorescence and optical detection of magnetic resonance of a tryptophan-free mutant. Biochemistry (1995) 0.77
Luminescence studies with trp repressor and its single-tryptophan mutants. Biochemistry (1993) 0.76
Characterization of the slow steps in the folding of the alpha subunit of tryptophan synthase. Biochemistry (1981) 0.75
Site-directed mutagenesis and its application to protein folding. Biotechnology (1990) 0.75
The role of protein folding in the evolution of protein sequences. Cold Spring Harb Symp Quant Biol (1987) 0.75