Natively unfolded proteins: A point where biology waits for physics

Vladimir N. Uversky

doi:10.1110/ps.4210102

journal article Open Access Apr 01, 2002

Natively unfolded proteins: A point where biology waits for physics

Vladimir N. Uversky

Protein Science Vol. 11 No. 4 pp. 739-756 · Wiley

View at Publisher Save 10.1110/ps.4210102

Abstract

AbstractThe experimental material accumulated in the literature on the conformational behavior of intrinsically unstructured (natively unfolded) proteins was analyzed. Results of this analysis showed that these proteins do not possess uniform structural properties, as expected for members of a single thermodynamic entity. Rather, these proteins may be divided into two structurally different groups: intrinsic coils, and premolten globules. Proteins from the first group have hydrodynamic dimensions typical of random coils in poor solvent and do not possess any (or almost any) ordered secondary structure. Proteins from the second group are essentially more compact, exhibiting some amount of residual secondary structure, although they are still less dense than native or molten globule proteins. An important feature of the intrinsically unstructured proteins is that they undergo disorder–order transition during or prior to their biological function. In this respect, the Protein Quartet model, with function arising from four specific conformations (ordered forms, molten globules, premolten globules, and random coils) and transitions between any two of the states, is discussed.

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Details

Published: Apr 01, 2002
Vol/Issue: 11(4)
Pages: 739-756
License: View

Authors

V

Vladimir N. Uversky

University of South Florida

Cite This Article

Vladimir N. Uversky (2002). Natively unfolded proteins: A point where biology waits for physics. Protein Science, 11(4), 739-756. https://doi.org/10.1110/ps.4210102

Natively unfolded proteins: A point where biology waits for physics

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