Statistical mechanical theory of protein conformation and its transition

Yukio Kobayashi, Hiroshi Wako, Nobuhiko Saitô

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The statistical mechanical theory of the structural transitions of proteins is developed in accordance with the island model by considering the hydrophobic interactions and the entropy factors while connecting the two hydrophobic residues. The proteins treated here are apo-α-lactalbumin (1B9O), lysozyme (1LZ1), ferrocytochrome c (1CYC), cytochrome c (isozyme 1) (1YCC), chymotrypsin inhibitor 2 (2CI2), and ubiquitin (1UBQ). Among them, according to the experiments, 2CI2 and 1UBQ do not exhibit intermediate structures (two-state model), but others do exhibit intermediate structures that are sometimes termed molten globules (three-state model). The theory related to these facts is given in terms of the island model, specifically 1B9O and 1LZ1. The stability or instability of the intermediate structures is explained by the effects of entropy during folding and the amino acid sequence. The intermediate structure is composed of several stable islands, which become unstable during unfolding.

Original languageEnglish
Article number074802
JournalJournal of the Physical Society of Japan
Volume76
Issue number7
DOIs
Publication statusPublished - 2007 Jul

Fingerprint

proteins
entropy
globules
cytochromes
lysozyme
inhibitors
folding
amino acids
interactions

Keywords

  • Entropy factor
  • Intermediate state
  • Island model
  • Specific hydrophobic interaction
  • Two-state and three-state models

ASJC Scopus subject areas

  • Physics and Astronomy(all)

Cite this

Statistical mechanical theory of protein conformation and its transition. / Kobayashi, Yukio; Wako, Hiroshi; Saitô, Nobuhiko.

In: Journal of the Physical Society of Japan, Vol. 76, No. 7, 074802, 07.2007.

Research output: Contribution to journalArticle

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