Configurational entropy of native proteins.

M. Karplus, T. Ichiye, Bernard Pettitt

Research output: Contribution to journalArticle

158 Citations (Scopus)

Abstract

Simulations of the residual configurational entropy of a protein in the native state suggest that it is nearly an order of magnitude larger than the entropy of denaturation. The implications of this result are discussed.

Original languageEnglish (US)
Pages (from-to)1083-1085
Number of pages3
JournalBiophysical Journal
Volume52
Issue number6
StatePublished - Dec 1987
Externally publishedYes

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Entropy
Proteins

ASJC Scopus subject areas

  • Biophysics

Cite this

Karplus, M., Ichiye, T., & Pettitt, B. (1987). Configurational entropy of native proteins. Biophysical Journal, 52(6), 1083-1085.

Configurational entropy of native proteins. / Karplus, M.; Ichiye, T.; Pettitt, Bernard.

In: Biophysical Journal, Vol. 52, No. 6, 12.1987, p. 1083-1085.

Research output: Contribution to journalArticle

Karplus, M, Ichiye, T & Pettitt, B 1987, 'Configurational entropy of native proteins.', Biophysical Journal, vol. 52, no. 6, pp. 1083-1085.
Karplus M, Ichiye T, Pettitt B. Configurational entropy of native proteins. Biophysical Journal. 1987 Dec;52(6):1083-1085.
Karplus, M. ; Ichiye, T. ; Pettitt, Bernard. / Configurational entropy of native proteins. In: Biophysical Journal. 1987 ; Vol. 52, No. 6. pp. 1083-1085.
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