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Bioinformatic method for protein thermal stabilization by structural entropy optimization.


ABSTRACT: Engineering proteins for higher thermal stability is an important and difficult challenge. We describe a bioinformatic method incorporating sequence alignments to redesign proteins to be more stable through optimization of local structural entropy. Using this method, improved configurational entropy (ICE), we were able to design more stable variants of a mesophilic adenylate kinase with only the sequence information of one psychrophilic homologue. The redesigned proteins display considerable increases in their thermal stabilities while still retaining catalytic activity. ICE does not require a three-dimensional structure or a large number of homologous sequences, indicating a broad applicability of this method. Our results also highlight the importance of entropy in the stability of protein structures.

SUBMITTER: Bae E 

PROVIDER: S-EPMC2474475 | biostudies-literature | 2008 Jul

REPOSITORIES: biostudies-literature

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Bioinformatic method for protein thermal stabilization by structural entropy optimization.

Bae Euiyoung E   Bannen Ryan M RM   Phillips George N GN  

Proceedings of the National Academy of Sciences of the United States of America 20080708 28


Engineering proteins for higher thermal stability is an important and difficult challenge. We describe a bioinformatic method incorporating sequence alignments to redesign proteins to be more stable through optimization of local structural entropy. Using this method, improved configurational entropy (ICE), we were able to design more stable variants of a mesophilic adenylate kinase with only the sequence information of one psychrophilic homologue. The redesigned proteins display considerable inc  ...[more]

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