Stabilisation of alpha-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding.

Taddei, N; Chiti, F; Fiaschi, T; Bucciantini, M; Capanni, C; Stefani, M; Serrano, L; Dobson, C M; Ramponi, G

Taddei, N; Chiti, F; Fiaschi, T; Bucciantini, M; Capanni, C; Stefani, M; Serrano, L; Dobson, C M; Ramponi, G.

Affiliation

Taddei N; Dipartimento di Scienze Biochimiche, Università di Firenze, Viale Morgagni 50, Firenze, 50134, Italy.

J Mol Biol ; 300(3): 633-47, 2000 Jul 14.

Article in En | MEDLINE | ID: mdl-10884358

Subject(s)

Acid Anhydride Hydrolases/chemistry; Acid Anhydride Hydrolases/metabolism; Mutagenesis, Site-Directed/genetics; Protein Folding; Acid Anhydride Hydrolases/genetics; Circular Dichroism; Dose-Response Relationship, Drug; Enzyme Stability; Humans; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Mutation/genetics; Peptide Fragments/chemistry; Peptide Fragments/genetics; Peptide Fragments/metabolism; Protein Denaturation/drug effects; Protein Structure, Secondary/drug effects; Thermodynamics; Trifluoroethanol/pharmacology; Urea/pharmacology; Acylphosphatase

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Collection: 01-internacional Database: MEDLINE Main subject: Mutagenesis, Site-Directed / Protein Folding / Acid Anhydride Hydrolases Limits: Humans Language: En Journal: J Mol Biol Year: 2000 Type: Article Affiliation country: Italy

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