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Volumn 321, Issue 1, 2002, Pages 1-6
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A buried polar residue in the hydrophobic interface of the coiled-coil peptide, GCN4-p1, plays a thermodynamic, not a kinetic role in folding
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Author keywords
Buried polar residues; Circular dichroism spectroscopy; Leucine zipper peptides; Protein folding kinetics
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Indexed keywords
ALANINE;
DIMER;
LEUCINE ZIPPER PROTEIN;
M PROTEIN;
PEPTIDE DERIVATIVE;
VALINE;
ARTICLE;
DISSOCIATION;
HYDROPHOBICITY;
KINETICS;
MUTATION;
PRIORITY JOURNAL;
PROTEIN ASSEMBLY;
PROTEIN FOLDING;
THERMODYNAMICS;
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EID: 0036353719
PISSN: 00222836
EISSN: None
Source Type: Journal
DOI: 10.1016/S0022-2836(02)00592-2 Document Type: Article |
Times cited : (28)
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References (21)
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