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Volumn 17, Issue 6, 2015, Pages 4220-4230
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Nature of aryl-tyrosine interactions contribute to β-hairpin scaffold stability: NMR evidence for alternate ring geometry
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Author keywords
[No Author keywords available]
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Indexed keywords
OLIGOPEPTIDE;
SOLUTION AND SOLUBILITY;
TYROSINE;
CHEMICAL STRUCTURE;
CHEMISTRY;
HEAT;
NUCLEAR MAGNETIC RESONANCE;
PROTEIN FOLDING;
PROTEIN SECONDARY STRUCTURE;
SOLUTION AND SOLUBILITY;
CHEMISTRY;
HOT TEMPERATURE;
MODELS, MOLECULAR;
NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR;
OLIGOPEPTIDES;
PROTEIN FOLDING;
PROTEIN STRUCTURE, SECONDARY;
SOLUTIONS;
TYROSINE;
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EID: 84964253128
PISSN: 14639076
EISSN: None
Source Type: Journal
DOI: 10.1039/c4cp04991h Document Type: Article |
Times cited : (4)
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References (69)
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