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J Biol Chem. 1973 Jul 10;248(13):4623-34 PMID: 4736979

Principles that govern the folding of protein chains.

Science. 1973 Jul 20;181(4096):223-30 PMID: 4124164

Intermediates in protein folding reactions and the mechanism of protein folding.

Annu Rev Biochem. 1975;44:453-75 PMID: 1094916

An electrophoretic study of reversible protein denaturation: chymotrypsinogen at high pressures.

Biochemistry. 1975 Jul 15;14(14):3257-64 PMID: 238588

Consideration of the Possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues.

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Reactivities of the cysteine residues of the reduced pancreatic trypsin inhibitor.

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Thermodynamic investigations of proteins. III. Thermodynamic description of lysozyme.

Biophys Chem. 1976 Jan;4(1):41-50 PMID: 2348

Structural patterns in globular proteins.

Nature. 1976 Jun 17;261(5561):552-8 PMID: 934293

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Proc Natl Acad Sci U S A. 1976 Jun;73(6):1853-7 PMID: 1064858

Effects of urea and guanidine-HCl on the folding and unfolding of pancreatic trypsin inhibitor.

J Mol Biol. 1977 Jun 25;113(2):313-28 PMID: 886612

Heat capacity and entropy changes in processes involving proteins.

Proc Natl Acad Sci U S A. 1977 Jun;74(6):2236-40 PMID: 196283

Thermal unfolding transition of ribonuclease A measured by 2'-CMP binding.

Biochemistry. 1977 Aug 9;16(16):3572-6 PMID: 19055

Stability of protein conformation: internal packing and enthalpy of fusion of model compounds.

J Theor Biol. 1977 Sep 7;68(1):139-42 PMID: 916701

Unfolding and refolding occur much faster for a proline-free proteins than for most proline-containing proteins.

Proc Natl Acad Sci U S A. 1977 Oct;74(10):4178-81 PMID: 22075

Immunochemical analysis of the conformational properties of intermediates trapped in the folding and unfolding of bovine pancreatic trypsin inhibitor.

J Mol Biol. 1978 Aug 5;123(2):129-47 PMID: 98640

Experimental studies of protein folding and unfolding.

Prog Biophys Mol Biol. 1978;33(3):231-97 PMID: 358273

Expression of functionality of alpha-chymotrypsin. Effects of guanidine hydrochloride and urea in the onset of denaturation.

Biochemistry. 1978 Dec 12;17(25):5460-8 PMID: 728409

Possible implications of many proline residues for the kinetics of protein unfolding and refolding.

J Mol Biol. 1978 Nov 5;125(3):401-6 PMID: 731701

Kinetics of the helix-coil transition of a polypeptide with non-ionic side groups, derived from ultrasonic relaxation measurements.

Biophys Chem. 1979 Jan;9(2):137-47 PMID: 427245

Detection of an early intermediate in the folding of ribonuclease A by protection of amide protons against exchange.

J Mol Biol. 1979 Nov 25;135(1):199-215 PMID: 43397

Kinetic study of protein unfolding and refolding using urea gradient electrophoresis.

J Mol Biol. 1980 Feb 15;137(1):61-80 PMID: 6245222

Stability of proteins: small globular proteins.

Adv Protein Chem. 1979;33:167-241 PMID: 44431

Ultraviolet difference spectroscopy of intermediates trapped in unfolding and refolding of bovine pancreatic trypsin inhibitor.

Biochemistry. 1980 Oct 14;19(21):4936-44 PMID: 7426636

Catalysis by protein-disulphide isomerase of the unfolding and refolding of proteins with disulphide bonds.

J Mol Biol. 1980 Sep 5;142(1):43-62 PMID: 7431409

Spectral evidence for a rapidly formed structural intermediate in the refolding kinetics of hen egg-white lysozyme.

Biochemistry. 1981 Mar 3;20(5):1080-5 PMID: 7225318

Formation of the intrachain disulfide bond in the constant fragment of the immunoglobulin light chain.

J Mol Biol. 1981 Mar 5;146(3):321-40 PMID: 6790712

Circular dichroism spectroscopy of bovine pancreatic trypsin inhibitor and five altered conformational states. Relationship of conformation and the refolding pathway of the trypsin inhibitor.

Biochemistry. 1981 Sep 29;20(20):5744-54 PMID: 7295701

Accessibilities and reactivities of cysteine thiols during refolding of reduced bovine pancreatic trypsin inhibitor.

J Mol Biol. 1981 Sep 5;151(1):211-3 PMID: 7328653

Preliminary circular dichroism study of the conformations of intermediates trapped during protein folding.

Biochimie. 1981 Nov-Dec;63(11-12):835-9 PMID: 7332747

Is there a single pathway for the folding of a polypeptide chain?

Proc Natl Acad Sci U S A. 1985 Jun;82(12):4028-30 PMID: 3858860

Effect of side chain-backbone electrostatic interactions on the stability of alpha-helices.

Proc Natl Acad Sci U S A. 1985 Sep;82(17):5585-7 PMID: 3862082

The study of conformational states of proteins by nuclear magnetic resonance.

Biochem J. 1985 Oct 1;231(1):1-10 PMID: 2998335

Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding.

Annu Rev Biochem. 1982;51:459-89 PMID: 6287919

Folding of ribonuclease A from a partially disordered conformation. Kinetic study under folding conditions.

Biochemistry. 1982 Oct 12;21(21):5155-63 PMID: 7171545

Stability of proteins. Proteins which do not present a single cooperative system.

Adv Protein Chem. 1982;35:1-104 PMID: 6762066

Transmission of conformational change in insulin.

Nature. 1983 Apr 7;302(5908):500-5 PMID: 6339948

Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor.

J Mol Biol. 1983 Apr 5;165(2):407-13 PMID: 6188846

Circular dichroism spectroscopy of the intermediates that precede the rate-limiting step of the refolding pathway of bovine pancreatic trypsin inhibitor. Relationship of conformation and the refolding pathway.

Biochemistry. 1983 May 10;22(10):2433-40 PMID: 6860640

Characterization of the distribution of internal motions in the basic pancreatic trypsin inhibitor using a large number of internal NMR probes.

Q Rev Biophys. 1983 Feb;16(1):1-57 PMID: 6878622

Evolutionary conservation and variation of protein folding pathways. Two protease inhibitor homologues from black mamba venom.

J Mol Biol. 1983 Aug 5;168(2):409-37 PMID: 6193277

An empirical approach to protein conformation stability and flexibility.

Biopolymers. 1983 Jan;22(1):49-58 PMID: 6673769

Proton NMR studies of denatured lysozyme.

FEBS Lett. 1984 Mar 26;168(2):331-4 PMID: 6723956

The disulphide folding pathway of ribonuclease T1.

J Mol Biol. 1986 Apr 5;188(3):477-86 PMID: 3735429

Use of a trypsin-pulse method to study the refolding pathway of ribonuclease.

Eur J Biochem. 1986 Sep 1;159(2):275-81 PMID: 3758063

Structural heterogeneity in protein crystals.

Biochemistry. 1986 Sep 9;25(18):5018-27 PMID: 3768328

Disulfide bonds as probes of protein folding pathways.

Methods Enzymol. 1986;131:83-106 PMID: 3773775

Temperature dependence of the hydrophobic interaction in protein folding.

Proc Natl Acad Sci U S A. 1986 Nov;83(21):8069-72 PMID: 3464944

Comparison between the unfolding rate and structural fluctuations in native lysozyme--effects of denaturants, ligand binding, and intrachain cross-linking on hydrogen exchange and unfolding kinetics.

Biopolymers. 1986 Oct;25(10):1981-96 PMID: 3779017

Cold denaturation of myoglobin.

J Mol Biol. 1986 Aug 5;190(3):487-98 PMID: 3783710

Folding/unfolding kinetics of mutant forms of iso-1-cytochrome c with replacement of proline-71.

Biochemistry. 1986 Nov 4;25(22):6959-64 PMID: 3026440

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 Nov 4;25(22):6965-72 PMID: 3801404

Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli.

J Biol Chem. 1987 Jun 5;262(16):7859-64 PMID: 3108260

The thermodynamic stability of proteins.

Annu Rev Biophys Biophys Chem. 1987;16:115-37 PMID: 3297085

Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism.

FEBS Lett. 1987 Aug 31;221(1):115-8 PMID: 3040467

Proline isomerism in staphylococcal nuclease characterized by NMR and site-directed mutagenesis.

Nature. 1987 Sep 17-23;329(6136):266-8 PMID: 3627269

Catalysis of protein folding by prolyl isomerase.

Nature. 1987 Sep 17-23;329(6136):268-70 PMID: 3306408

Temperature-sensitive mutations of bacteriophage T4 lysozyme occur at sites with low mobility and low solvent accessibility in the folded protein.

Biochemistry. 1987 Jun 30;26(13):3754-8 PMID: 3651410

Conformations of intermediates in the folding of the pancreatic trypsin inhibitor.

J Mol Biol. 1987 Jun 5;195(3):731-9 PMID: 2443711

Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme.

Nature. 1987 Nov 5-11;330(6143):41-6 PMID: 3118211

Sequential mechanism of refolding of carbonic anhydrase B.

FEBS Lett. 1987 Nov 16;224(1):9-13 PMID: 2824244

Activity change during unfolding of bovine pancreatic ribonuclease A in guanidine.

Biochim Biophys Acta. 1987 Dec 18;916(3):455-64 PMID: 3689804

Protein stability curves.

Biopolymers. 1987 Nov;26(11):1859-77 PMID: 3689874

Replacement of proline-76 with alanine eliminates the slowest kinetic phase in thioredoxin folding.

Biochemistry. 1987 Oct 20;26(21):6765-74 PMID: 3322388

Genetic and structural analysis of the protein stability problem.

Biochemistry. 1987 Nov 3;26(22):6885-8 PMID: 3427049

Folding and association of proteins.

Prog Biophys Mol Biol. 1987;49(2-3):117-237 PMID: 3327098

Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis.

Biochemistry. 1987 Dec 15;26(25):8031-7 PMID: 3442641

Heat-shock proteins. Coming in from the cold.

Nature. 1988 Apr 28;332(6167):776-7 PMID: 3282176

Disulphide bonds and protein stability.

Bioessays. 1988 Feb-Mar;8(2):57-63 PMID: 3282505

Contribution of hydrophobic interactions to protein stability.

Nature. 1988 Jun 23;333(6175):784-6 PMID: 3386721

Toward a better understanding of protein folding pathways.

Proc Natl Acad Sci U S A. 1988 Jul;85(14):5082-6 PMID: 2455892

Genetic studies of protein stability and mechanisms of folding.

Annu Rev Biophys Biophys Chem. 1988;17:481-507 PMID: 3293597

Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3.

Nature. 1988 Aug 4;334(6181):406-10 PMID: 3405287

Characterization of a helical protein designed from first principles.

Science. 1988 Aug 19;241(4868):976-8 PMID: 3043666

Thermodynamic study of the apomyoglobin structure.

J Mol Biol. 1988 Jul 5;202(1):127-38 PMID: 3172208

NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A.

Nature. 1988 Oct 20;335(6192):694-9 PMID: 2845278

Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR.

Nature. 1988 Oct 20;335(6192):700-4 PMID: 2845279

A peptide model of a protein folding intermediate.

Nature. 1988 Nov 3;336(6194):42-8 PMID: 3185721

Conformation of peptide fragments of proteins in aqueous solution: implications for initiation of protein folding.

Biochemistry. 1988 Sep 20;27(19):7167-75 PMID: 3061450

Protein structure determination in solution by nuclear magnetic resonance spectroscopy.

Science. 1989 Jan 6;243(4887):45-50 PMID: 2911719

Correct folding of circularly permuted variants of a beta alpha barrel enzyme in vivo.

Science. 1989 Jan 13;243(4888):206-10 PMID: 2643160

Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin.

Nature. 1989 Feb 2;337(6206):473-5 PMID: 2644542

Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins.

Nature. 1989 Feb 2;337(6206):476-8 PMID: 2492638

Conformational forces affecting the folding pathways of dendrotoxins I and K from black mamba venom.

Eur J Biochem. 1989 Jan 15;179(1):87-94 PMID: 2465150

Nature and distribution of sites of temperature-sensitive folding mutations in the gene for the P22 tailspike polypeptide chain.

J Mol Biol. 1988 Dec 5;204(3):607-19 PMID: 3225847

Mutational analysis of a protein-folding pathway.

Nature. 1989 Mar 9;338(6211):127-32 PMID: 2465497

Heat and cold denaturation of phosphoglycerate kinase (interaction of domains).

FEBS Lett. 1989 Feb 27;244(2):276-8 PMID: 2646151

Analysis of prepro-alpha-lytic protease expression in Escherichia coli reveals that the pro region is required for activity.

J Bacteriol. 1989 Mar;171(3):1320-5 PMID: 2646278

Unity in function in the absence of consensus in sequence: role of leader peptides in export.

Science. 1989 Mar 3;243(4895):1156-9 PMID: 2646712

Separation of the nativelike intermediate from unfolded forms during refolding of ribonuclease A.

Biochemistry. 1988 Dec 13;27(25):9037-42 PMID: 3233221

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Biophys Chem. 1988 Aug;31(1-2):155-62 PMID: 2466495

Protein denaturation.

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Formation of randomly paired disulfide bonds in des-(121-124)-ribonuclease after reduction and reoxidation.

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Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect.

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Proline isomerization during refolding of ribonuclease A is accelerated by the presence of folding intermediates.

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The relation between the divergence of sequence and structure in proteins.

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Immunological distinction between the possible origins of enzymatic activity in a polypeptide fragment of staphylococcal nuclease.

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The single-disulphide intermediates in the refolding of reduced pancreatic trypsin inhibitor.

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Experimental and theoretical aspects of protein folding.

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Probing the determinants of protein folding and stability with amino acid substitutions.

J Biol Chem. 1989 Apr 5;264(10):5315-8 PMID: 2647715

Heat capacity and conformation of proteins in the denatured state.

J Mol Biol. 1989 Feb 20;205(4):737-50 PMID: 2538636

Proline isomerism leads to multiple folded conformations of calbindin D9k: direct evidence from two-dimensional 1H NMR spectroscopy.

Proc Natl Acad Sci U S A. 1989 Apr;86(7):2195-8 PMID: 2928325

Interaction of cytidine 3'-monophosphate and uridine 3'-monophosphate with ribonuclease a at the denaturation temperature.

Biochemistry. 1988 Nov 1;27(22):8429-36 PMID: 3242592

A magnetization-transfer nuclear magnetic resonance study of the folding of staphylococcal nuclease.

Biochemistry. 1989 Jan 10;28(1):362-70 PMID: 2706262

Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin.

Biochemistry. 1989 Jan 10;28(1):7-13 PMID: 2706269

Stability of protein structure and hydrophobic interaction.

Adv Protein Chem. 1988;39:191-234 PMID: 3072868

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Adv Protein Chem. 1988;39:51-124 PMID: 3072869

Low-temperature unfolding of a mutant of phage T4 lysozyme. 1. Equilibrium studies.

Biochemistry. 1989 Jan 24;28(2):685-91 PMID: 2653427

Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations.

Biochemistry. 1989 Jan 24;28(2):691-9 PMID: 2653428

Residual structure in large fragments of staphylococcal nuclease: effects of amino acid substitutions.

Biochemistry. 1989 Feb 7;28(3):936-44 PMID: 2540825

Characterization of the critical state in protein folding. Effects of guanidine hydrochloride and specific Ca2+ binding on the folding kinetics of alpha-lactalbumin.

J Mol Biol. 1989 Apr 5;206(3):547-61 PMID: 2716061

Alternative packing arrangements in the hydrophobic core of lambda repressor.

Nature. 1989 May 4;339(6219):31-6 PMID: 2524006

Protein fragments as probes in the study of protein folding mechanisms: differential effects of dihydrofolate reductase fragments on the refolding of the intact protein.

Proc Natl Acad Sci U S A. 1989 May;86(9):3060-4 PMID: 2654934

Effects of multiple replacements at a single position on the folding and stability of dihydrofolate reductase from Escherichia coli.

Biochemistry. 1989 Mar 7;28(5):2083-93 PMID: 2655702

Thermodynamic problems of protein structure.

Annu Rev Biophys Biophys Chem. 1989;18:47-69 PMID: 2660833

The beta-sheet to coil transition.

Annu Rev Biophys Biophys Chem. 1989;18:93-111 PMID: 2660835

Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins.

Cell. 1989 Jun 30;57(7):1069-72 PMID: 2544299

Mapping the transition state and pathway of protein folding by protein engineering.

Nature. 1989 Jul 13;340(6229):122-6 PMID: 2739734

Further experimental studies of the disulfide folding transition of ribonuclease A.

Proteins. 1988;4(4):251-61 PMID: 3253735

Unusually stable helix formation in short alanine-based peptides.

Proc Natl Acad Sci U S A. 1989 Jul;86(14):5286-90 PMID: 2748584

Folding of a peptide corresponding to the alpha-helix in bovine pancreatic trypsin inhibitor.

Biochemistry. 1989 May 16;28(10):4343-7 PMID: 2765489

Energetics of complementary side-chain packing in a protein hydrophobic core.

Biochemistry. 1989 May 30;28(11):4914-22 PMID: 2669964

How does protein folding get started?

Trends Biochem Sci. 1989 Jul;14(7):291-4 PMID: 2672452

Mechanisms of cooperativity and allosteric regulation in proteins.

Q Rev Biophys. 1989 May;22(2):139-237 PMID: 2675171

A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin.

Nature. 1989 Oct 26;341(6244):755-7 PMID: 2477714

A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase.

Nature. 1989 Oct 26;341(6244):758-60 PMID: 2477715

Capping and alpha-helix stability.

Nature. 1989 Nov 16;342(6247):296-9 PMID: 2812029

Hydrophobic effect in protein folding and other noncovalent processes involving proteins.

Proc Natl Acad Sci U S A. 1989 Nov;86(21):8382-5 PMID: 2813394

Two types of rate-determining step in chemical and biochemical processes.

Biochem J. 1989 Nov 1;263(3):985-8 PMID: 2597141

A simple model for proteins with interacting domains. Applications to scanning calorimetry data.

Biochemistry. 1989 Oct 17;28(21):8588-96 PMID: 2690944

Theoretical study of the contribution of aromatic side chains to the circular dichroism of basic bovine pancreatic trypsin inhibitor.

Biochemistry. 1989 Oct 17;28(21):8609-13 PMID: 2481497

Common features of protein unfolding and dissolution of hydrophobic compounds.

Science. 1990 Feb 2;247(4942):559-61 PMID: 2300815

The unfolding and attempted refolding of mitochondrial aspartate aminotransferase from pig heart.

Biochem J. 1990 Jan 1;265(1):45-50 PMID: 2302172

The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure.

Proteins. 1989;6(2):87-103 PMID: 2695928

Protein sorting to mitochondria: evolutionary conservations of folding and assembly.

Science. 1990 Feb 23;247(4945):930-8 PMID: 2406905

The unfolding and attempted refolding of citrate synthase from pig heart.

Biochim Biophys Acta. 1990 Mar 1;1037(3):332-6 PMID: 2310749

Relative helix-forming tendencies of nonpolar amino acids.

Nature. 1990 Mar 15;344(6263):268-70 PMID: 2314462

Deciphering the message in protein sequences: tolerance to amino acid substitutions.

Science. 1990 Mar 16;247(4948):1306-10 PMID: 2315699

Evidence for a molten globule state as a general intermediate in protein folding.

FEBS Lett. 1990 Mar 12;262(1):20-4 PMID: 2318308

Role of two proline-containing turns in the folding of porcine ribonuclease.

J Mol Biol. 1990 Mar 5;212(1):185-96 PMID: 2319596

Role of a subdomain in the folding of bovine pancreatic trypsin inhibitor.

Nature. 1990 Apr 12;344(6267):685-8 PMID: 1691452

pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1.

Biochemistry. 1990 Mar 13;29(10):2564-72 PMID: 2110472

Multiple replacements at position 211 in the alpha subunit of tryptophan synthase as a probe of the folding unit association reaction.

Biochemistry. 1990 Feb 13;29(6):1539-45 PMID: 2185841

The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell.

Biochemistry. 1990 Mar 6;29(9):2205-12 PMID: 2186809

pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme.

Biochemistry. 1990 Mar 6;29(9):2403-8 PMID: 2337607

Synthesis, purification and initial structural characterization of octarellin, a de novo polypeptide modelled on the alpha/beta-barrel proteins.

Protein Eng. 1990 Mar;3(4):259-66 PMID: 2188263

Some factors in the interpretation of protein denaturation.

Adv Protein Chem. 1959;14:1-63 PMID: 14404936

An early intermediate in the folding of ribonuclease A is protected against cleavage by pepsin.

Biochemistry. 1984 May 8;23(10):2128-33 PMID: 6428447

Evolution and the tertiary structure of proteins.

Annu Rev Biophys Bioeng. 1984;13:453-92 PMID: 6378074

Ribonuclease A: carbon-13 nuclear magnetic resonance assignments, binding sites, and conformational flexibility.

Biochemistry. 1984 Jul 17;23(15):3515-21 PMID: 6466650

Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function.

J Mol Biol. 1984 Aug 15;177(3):531-57 PMID: 6332197

Principles that determine the structure of proteins.

Annu Rev Biochem. 1984;53:537-72 PMID: 6383199

Folding of ribonuclease A from a partially disordered conformation. Kinetic study under transition conditions.

Biochemistry. 1984 May 22;23(11):2470-7 PMID: 6477878

Hydrogen bonding in globular proteins.

Prog Biophys Mol Biol. 1984;44(2):97-179 PMID: 6385134

Kinetic role of a meta-stable native-like two-disulphide species in the folding transition of bovine pancreatic trypsin inhibitor.

J Mol Biol. 1984 Nov 5;179(3):497-526 PMID: 6210370

Characterization of the transition state of lysozyme unfolding. I. Effect of protein-solvent interactions on the transition state.

Biopolymers. 1984 Nov;23(11 Pt 2):2473-88 PMID: 6518262

Characterization of the transition state of lysozyme unfolding. II. Effects of the intrachain crosslinking and the inhibitor binding on the transition state.

Biopolymers. 1984 Nov;23(11 Pt 2):2489-98 PMID: 6518263

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