Molecular dynamics as a tool to detect protein foldability. A mutant of domain B1 of protein G with non-native secondary structure propensities
Author:
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Reference43 articles.
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2. Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2: Why small proteins tend to have high denaturation temperatures;Alexander;Biochemistry,1992a
3. Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal protein G;Alexander;Biochemistry,1992b
4. Role of a non-native interaction in the folding of the protein G B1 domain as inferred from the conformational analysis of the alpha-helix fragment;Blanco;Fold Des,1997
5. A short linear peptide that folds into a native stable beta-hairpin in aqueous solution;Blanco;Nat Struct Biol,1994
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