1 H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus

Journal of Molecular Biology

Volumn 258, Issue 2, 1996, Pages 322-333

  Martins, José C ^a   Maes, Dominique ^a   Loris, Remy ^a   Pepermans, Henri A M ^b   Wyns, Lode ^a   Willem, Rudolph ^a   Verheyden, Patricia ^a  

^a VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

^b UNILEVER RESEARCH VLAARDINGEN   (Netherlands)

Author keywords

1H NMR; Amaranthus caudatus; Antimicrobial peptide; Conformation; Hevein domain

Indexed keywords

AMARANTHUS CAUDATUS; TRITICUM AESTIVUM;

AMP2 PROTEIN, AMARANTHUS CAUDATUS; ANTIFUNGAL AGENT; CARBOHYDRATE; DISULFIDE; VEGETABLE PROTEIN; ANTIINFECTIVE AGENT; CARBOHYDRATE BINDING PROTEIN; CHITIN; CYSTINE;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDE SEQUENCE; PLANT; PLANT SEED; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY; SOLUTION AND SOLUBILITY; DISULFIDE BOND; MOLECULAR DYNAMICS; MOLECULAR MODEL; NONHUMAN; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; STATISTICAL ANALYSIS;

AMINO ACID SEQUENCE; ANTIFUNGAL AGENTS; BASE SEQUENCE; CARBOHYDRATES; DISULFIDES; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PLANT PROTEINS; PLANTS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SEEDS; SEQUENCE HOMOLOGY, AMINO ACID; SOLUTIONS;

EID: 0029664883     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0253     Document Type: Article

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