Polymeric Aspects of Protein Folding: a Brief Overview

Authors: Tcherkasskaya O.; Uversky V.N.

Source: Protein and Peptide Letters, Volume 10, Number 3, June 2003 , pp. 239-245(7)

Publisher: Bentham Science Publishers

Abstract:

Regardless of the differences in primary amino acid sequences, protein molecules in a number of conformational states behave as polymer homologues, allowing speculations as to the volume interactions being a driving force in formation of equilibrium structures. For instance, both native and molten globules exhibit key features of polymer globules, where the fluctuations of the molecular density are expected to be much less than the molecular density itself. Protein molecules in the compact denatured (pre-molten globule) states possess properties of squeezed coils. In fact, even high concentrations of strong denaturants (e.g., urea and GdmCl) more likely constitute bad solvents for protein chains. Thus, globular proteins are probably never random coils without positional correlations and biological polypeptide chains represent the macromolecular coils below a critical point even under harsh denaturing conditions. Several implications of these findings to protein folding are discussed.

Keywords: protein folding; equilibrium structures; polymer globules; pre-molten globule; squeezed coils; globular proteins; polymer homologues

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866033478988

Publication date: 2003-06-01

• Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

• In this: publication
• By this: publisher
• In this Subject: Anatomy & Physiology
• By this author: Tcherkasskaya O. ;  Uversky V.N.

Website © Publishing Technology. Article copyright remains with the publisher, society or author(s) as specified within the article.

• Terms and conditions
• Privacy policy
• Information for advertisers