Protein folding kinetics provides a context-independent assessment of beta-strand propensity in the Fyn SH3 domain.
Zarrine-Afsar, Arash
Protein folding kinetics provides a context-independent assessment of beta-strand propensity in the Fyn SH3 domain. [electronic resource] - Journal of molecular biology Oct 2007 - 764-74 p. digital
Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
0022-2836
10.1016/j.jmb.2007.07.059 doi
Amino Acid Substitution
Humans
Kinetics
Models, Molecular
Mutagenesis, Site-Directed
Protein Folding
Protein Structure, Secondary
Proto-Oncogene Proteins c-fyn--chemistry
Thermodynamics
src Homology Domains
Protein folding kinetics provides a context-independent assessment of beta-strand propensity in the Fyn SH3 domain. [electronic resource] - Journal of molecular biology Oct 2007 - 764-74 p. digital
Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
0022-2836
10.1016/j.jmb.2007.07.059 doi
Amino Acid Substitution
Humans
Kinetics
Models, Molecular
Mutagenesis, Site-Directed
Protein Folding
Protein Structure, Secondary
Proto-Oncogene Proteins c-fyn--chemistry
Thermodynamics
src Homology Domains