Crossref journal-article
Wiley
Biopolymers (311)
Abstract

AbstractThe theory, character, and properties of cooperative transitions are developed with special reference to the abrupt changes of state which occur in protein solutions. Comparisons of helix–coil processes and protein conformational reactions show that though cooperation dominates both of these processes, there are important differences. Tests of two types for the validity of the two‐state approximation are presented with specific applications to proteins. Available experimental evidence demonstrates that the thermally induced reversible transitions of ribonuclease, α‐chymotrypsin, and chymotrypsinogen A under conditions thus far examined are two‐state processes.

Bibliography

Lumry, R., Biltonen, R., & Brandts, J. F. (1966). Validity of the “two‐state” hypothesis for conformational transitions of proteins. Biopolymers, 4(8), 917–944. Portico.

Authors 3
  1. Rufus Lumry (first)
  2. Rodney Biltonen (additional)
  3. John F. Brandts (additional)
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Dates
Type When
Created 20 years, 7 months ago (Dec. 29, 2004, 5 a.m.)
Deposited 1 year, 10 months ago (Oct. 19, 2023, 12:15 p.m.)
Indexed 1 month, 1 week ago (July 16, 2025, 7:44 a.m.)
Issued 58 years, 11 months ago (Sept. 1, 1966)
Published 58 years, 11 months ago (Sept. 1, 1966)
Published Online 21 years, 6 months ago (Feb. 1, 2004)
Published Print 58 years, 11 months ago (Sept. 1, 1966)
Funders 0

None

@article{Lumry_1966, title={Validity of the “two‐state” hypothesis for conformational transitions of proteins}, volume={4}, ISSN={1097-0282}, url={http://dx.doi.org/10.1002/bip.1966.360040808}, DOI={10.1002/bip.1966.360040808}, number={8}, journal={Biopolymers}, publisher={Wiley}, author={Lumry, Rufus and Biltonen, Rodney and Brandts, John F.}, year={1966}, month=sep, pages={917–944} }