The three-dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1H nuclear magnetic resonance

Proteins: Structure, Function and Genetics

Volumn 37, Issue 3, 1999, Pages 388-403

  Fant, Franky ^a   Vranken, Wim F ^a   Borremans, Frans A M ^a  

^a GHENT UNIVERSITY   (Belgium)

Author keywords

thionin; Ah AMP1; Cysteine stabilized motif; Plant defensin; Rs AFP1

Indexed keywords

AMINO ACID; ANTIMICROBIAL PROTEIN 1; DEFENSIN; UNCLASSIFIED DRUG;

AESCULUS HIPPOCASTANUM; AMINO ACID SEQUENCE; ANTIFUNGAL ACTIVITY; ARTICLE; CONTROLLED STUDY; DRUG ACTIVITY; DRUG STRUCTURE; ELECTRIC POTENTIAL; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; DEFENSINS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PLANT PROTEINS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEINS; ROSALES; SEQUENCE ALIGNMENT; SOLUTIONS;

AESCULUS HIPPOCASTANUM; EQUUS CABALLUS; FUNGI; HIPPOCASTANUM;

EID: 0032707644     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19991115)37:3<388::AID-PROT7>3.0.CO;2-F     Document Type: Article

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