Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding

Matthews, B W; Nicholson, H; Becktel, W J

doi:10.1073/pnas.84.19.6663

Public

Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding.

Published in Proceedings of the National Academy of Sciences of the United States of America • Oct 1, 1987

NobleIDNI6P76W68R33S43

Authors:

B W Matthews

,

H Nicholson

,

W J Becktel

Abstract

It is proposed that the stability of a protein can be increased by selected amino acid substitutions that decrease the configurational entropy of unfolding. Two such substitutions, one of the form Xaa----Pro and the other of the form Gly----Xaa, were constructed in bacteriophage T4 lysozyme at sites...

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