Finding intermediates in protein folding

Principles that Govern the Folding of Protein Chains

1973 • 6,771 citations

Are there pathways for protein folding?

1968 • 1,496 citations

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

1989 • 1,446 citations

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

1975 • 1,108 citations

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

1988 • 823 citations

Formation of a Molten Globule Intermediate Early in the Kinetic Folding Pathway of Apomyoglobin

1993 • 735 citations

α‐lactalbumin: compact state with fluctuating tertiary structure?

1981 • 611 citations

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

1988 • 583 citations

Co-operative non-enzymatic base recognition III. Kinetics of the helix—coil transition of the oligoribouridylic · oligoriboadenylic acid system and of oligoriboadenylic acid alone at acidic pH

1971 • 433 citations

Validity of the “two‐state” hypothesis for conformational transitions of proteins

1966 • 363 citations

The Configurational Changes of Poly-L-proline in Solution

1960 • 261 citations

A peptide model of a protein folding intermediate

1988 • 252 citations

Pulsed H/D-exchange studies of folding intermediates

1993 • 245 citations

Acid catalysis of the formation of the slow-folding species of RNase A: Evidence that the reaction is proline isomerization

1978 • 229 citations

Denaturation of Bovine Carbonic Anhydrase B by Guanidine Hydrochloride

1973 • 189 citations

Early folding intermediate of ribonuclease A.

1990 • 180 citations

A folding model of α-lactalbumin deduced from the three-state denaturation mechanism

1977 • 173 citations

A quantitative treatment of the kinetics of the folding transition of ribonuclease A

1976 • 167 citations

Role of proline isomerization in folding of ribonuclease A at low temperatures

1979 • 161 citations

Both the Fast and Slow Refolding Reactions of Ribonuclease A Yield Native Enzyme

1973 • 157 citations

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

1979 • 154 citations

Test of the extended two-state model for the kinetic intermediates observed in the folding transition of ribonuclease A

1978 • 137 citations

Kinetic Evidence for Incorrectly Folded Intermediate States in the Refolding of Denatured Proteins

1971 • 135 citations

Intermediates in the refolding of reduced pancreatic trypsin inhibitor

1974 • 97 citations

Folding of staphylococcal nuclease: Kinetic studies of two processes in acid renaturation

1971 • 93 citations

Structural intermediates trapped during the folding of ribonuclease A by amide proton exchange

1980 • 86 citations

Guanidine-unfolded state of ribonuclease A contains both fast- and slow-refolding species.

1976 • 82 citations

Proton NMR assignments and regular backbone structure of bovine pancreatic ribonuclease A in aqueous solution

1989 • 71 citations

The Sequential Unfolding of Ribonuclease A: Detection of a Fast Initial Phase in the Kinetics of Unfolding

1971 • 61 citations

Role of accessory proteins in protein folding

1993 • 56 citations

Effects of solvent viscosity and different guanidine salts on the kinetics of ribonuclease A chain folding

1978 • 52 citations

Properties of the Refolding and Unfolding Reactions of Ribonuclease A

1972 • 46 citations