Stabilization of an isolated helical capping box in solution by hydrophobic interactions: evidence from the NMR study of bioactive peptides from the C-terminus of human C5a anaphylatoxin

Biopolymers

Volumn 38, Issue 1, 1996, Pages 31-41

  Ni, Feng ^a   Carpenter, K A ^a   Ripoll, Daniel R ^a   Sanderson, Sam D ^b   Hugli, Tony E ^c  

^a NATIONAL RESEARCH COUNCIL CANADA   (Canada)

^b UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

^c SCRIPPS CLINIC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANAPHYLATOXIN; COMPLEMENT COMPONENT C5A; COMPLEMENT RECEPTOR;

ARTICLE; CARBOXY TERMINAL SEQUENCE; HUMAN; HYDROPHOBICITY; MOLECULAR INTERACTION; NUCLEAR MAGNETIC RESONANCE; PROTEIN CONFORMATION;

AMINO ACID SEQUENCE; ANTIGENS, CD; COMPLEMENT C5A; HUMANS; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECEPTOR, ANAPHYLATOXIN C5A; RECEPTORS, COMPLEMENT; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0030021595     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0282(199601)38:1<31::AID-BIP3>3.0.CO;2-X     Document Type: Article

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