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Mechanism of protein kinetic stabilization by engineered disulfide crosslinks

Abstract:

The impact of disulfide bonds on protein stability goes beyond simple equilibrium thermodynamics effects associated with the conformational entropy of the unfolded state. Indeed, disulfide crosslinks may play a role in the prevention of dysfunctional association and strongly affect the rates of irreversible enzyme inactivation, highly relevant in biotechnological applications. While these kinetic-stability effects remain poorly understood, by analogy with proposed mechanisms for processes of ...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1371/journal.pone.0070013

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Institution:
University of Oxford
Division:
MSD
Department:
Pathology Dunn School
Role:
Author
Publisher:
Public Library of Science
Journal:
PLoS One More from this journal
Volume:
8
Issue:
7
Pages:
e70013
Publication date:
2013-07-30
Acceptance date:
2013-06-14
DOI:
EISSN:
1932-6203
Language:
English
Keywords:
Pubs id:
pubs:659849
UUID:
uuid:2e046fe4-870a-49d6-aed9-94c15fc726ca
Local pid:
pubs:659849
Source identifiers:
659849
Deposit date:
2016-12-13

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