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Volumn 92, Issue 6, 2009, Pages 502-507
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The structure of well-folded beta-hairpin peptides promotes resistance to peptidase degradation.
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Author keywords
[No Author keywords available]
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Indexed keywords
ALPHA-CHYMOTRYPSIN;
CHYMOTRYPSIN;
CHYMOTRYPSIN A;
PEPTIDE;
PRONASE;
ANIMAL;
ARTICLE;
CATTLE;
CHEMISTRY;
PROTEIN FOLDING;
PROTEIN SECONDARY STRUCTURE;
SYNTHESIS;
ANIMALS;
CATTLE;
CHYMOTRYPSIN;
PEPTIDES;
PRONASE;
PROTEIN FOLDING;
PROTEIN STRUCTURE, SECONDARY;
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EID: 75649141318
PISSN: 00063525
EISSN: None
Source Type: Journal
DOI: 10.1002/bip.21266 Document Type: Article |
Times cited : (31)
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References (0)
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