Configurational entropy of native proteins

M. Karplus; T. Ichiye; B. M. Pettitt

doi:10.1016/S0006-3495(87)83303-9

Configurational entropy of native proteins

M. Karplus, T. Ichiye, B. M. Pettitt

Research output: Contribution to journal › Article › peer-review

165 Scopus citations

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 language	English (US)
Pages (from-to)	1083-1085
Number of pages	3
Journal	Biophysical journal
Volume	52
Issue number	6
DOIs	https://doi.org/10.1016/S0006-3495(87)83303-9
State	Published - 1987
Externally published	Yes

ASJC Scopus subject areas

Biophysics

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10.1016/S0006-3495(87)83303-9

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@article{89657ea302f94eb498712bc6779d1d16,

title = "Configurational entropy of native proteins",

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.",

author = "M. Karplus and T. Ichiye and Pettitt, {B. M.}",

note = "Funding Information: This work is supported in part by a grant from the National Institutes of Health. Received for publication 31 March 1987 and in final form 17 May 1987.",

year = "1987",

doi = "10.1016/S0006-3495(87)83303-9",

language = "English (US)",

volume = "52",

pages = "1083--1085",

journal = "Biophysical journal",

issn = "0006-3495",

publisher = "Elsevier B.V.",

number = "6",

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T1 - Configurational entropy of native proteins

AU - Karplus, M.

AU - Ichiye, T.

AU - Pettitt, B. M.

N1 - Funding Information: This work is supported in part by a grant from the National Institutes of Health. Received for publication 31 March 1987 and in final form 17 May 1987.

PY - 1987

Y1 - 1987

N2 - 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.

AB - 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.

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U2 - 10.1016/S0006-3495(87)83303-9

DO - 10.1016/S0006-3495(87)83303-9

M3 - Article

C2 - 3427197

AN - SCOPUS:0023475026

SN - 0006-3495

VL - 52

SP - 1083

EP - 1085

JO - Biophysical journal

JF - Biophysical journal

IS - 6

ER -

Configurational entropy of native proteins

Abstract

ASJC Scopus subject areas

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