Properties and crystal structure of a (beta)-barrel folding mutant

Properties and crystal structure of a (beta)-barrel folding mutant

A mutant of a beta-barrel protein, rat intestinal fatty acid binding protein, was predicted to be more stable than the wild-type protein due to a novel hydrogen bond. Equilibrium denaturation studies indicated the opposite: the V60N mutant protein was less stable.

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Bibliographische Detailangaben
Veröffentlicht in:Biophysical journal 2000-03, Vol.78 (3), p.1551
Hauptverfasser: Ropson, Ira J, Yowler, Brian C, Dalessio, Paul M, Banaszak, Leonard, Thompson, James
Format: Artikel
Sprache:eng
Schlagworte:
Biochemistry
Fatty acids
Molecular biology
Mutation
Proteins
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Zusammenfassung:A mutant of a beta-barrel protein, rat intestinal fatty acid binding protein, was predicted to be more stable than the wild-type protein due to a novel hydrogen bond. Equilibrium denaturation studies indicated the opposite: the V60N mutant protein was less stable.
ISSN:0006-3495
1542-0086