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Cited by 1,249

The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.

Theory for the folding and stability of globular proteins

Dill, Ken A.·1985·Biochemistry
DOI 10.1021/bi00327a032
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Abstract

Using lattice statistical mechanics, we develop theory to account for the folding of a heteropolymer molecule such as a protein to the globular and soluble state. Folding is assumed to be driven by the association of solvophobic monomers to avoid solvent and opposed by the chain configurational entropy. Theory predicts a phase transition as a function of temperature or solvent character. Molecules that are too short or too long or that have too few solvophobic residues are predicted not to fold. Globular molecules should have a largely solvophobic core, but there is an entropic tendency for some residues to be "out of place", particularly in small molecules. For long chains, molecules comprised of globular domains are predicted to be thermodynamically more stable than spherical molecules. The number of accessible conformations in the globular state is calculated to be an exceedingly small fraction of the number available to the random coil. Previous estimates of this number, which have motivated kinetic theories of folding, err by many tens of orders of magnitude.

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Metadata

Authors
Dill, K. A.
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
1985-03-12
Volume
24
Issue
6
Pages
1501-1509
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi00327a032
OpenAlex
W2080382112
Cited by
1,249
References
62
FWCI
2.63
Type
journal article
Language
en
Open access
closed

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

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.