Optimized variants of the cold shock protein from in vitro selection: structural basis of their high thermostability.

Max, Klaas E A; Wunderlich, Michael; Roske, Yvette; Schmid, Franz X; Heinemann, Udo

Max, Klaas E A; Wunderlich, Michael; Roske, Yvette; Schmid, Franz X; Heinemann, Udo.

Affiliation

Max KE; Makromolekulare Strukturen und Interaktionen, Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany.

J Mol Biol ; 369(4): 1087-97, 2007 Jun 15.

Article in En | MEDLINE | ID: mdl-17481655

Subject(s)

Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Cold Temperature; Genetic Variation; Protein Structure, Tertiary; Amino Acid Sequence; Bacterial Proteins/metabolism; Crystallography, X-Ray; Directed Molecular Evolution; Models, Molecular; Molecular Sequence Data; Mutation; Protein Denaturation; Sequence Alignment; Surface Properties

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Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Genetic Variation / Protein Structure, Tertiary / Cold Temperature Language: En Journal: J Mol Biol Year: 2007 Document type: Article Affiliation country: Germany

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