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

Lumry, Rufus, Biltonen, Rodney, Brandts, John F.·1966·Biopolymers

Abstract

The 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.

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Metadata

Authors
Lumry, R., Biltonen, R., & Brandts, J. F.
Venue
Biopolymers
Publisher
Wiley
Published
1966-09
Volume
4
Issue
8
Pages
917-944
ISSN
  • 0006-3525 (ISSN-L)
  • 1097-0282
OpenAlex
W2090604290
Cited by
359
References
0
FWCI
4.00
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Validity of the “two‐state” hypothesis for conformational transitions of proteins. https://app.cochat.ai/papers/10.1002/bip.1966.360040808
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Lumry, R., Biltonen, R., & Brandts, J. F. (1966). Validity of the “two‐state” hypothesis for conformational transitions of proteins. Biopolymers. https://doi.org/10.1002/bip.1966.360040808

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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