The FLG motif in the N-terminal region of glucoprotein 41 of human imnnunodeficiency virus type 1 adopts a type-I β turn in aqueous solution and serves as the initiation site for helix formation

European Journal of Biochemistry

Volumn 247, Issue 3, 1997, Pages 896-905

  Chang, Ding Kwo ^a,b   Chien, Wei Jyun ^a   Cheng, Shu Fang ^a  

^a INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

^b INSTITUTE OF CHEMISTRY   (Taiwan)

Author keywords

Hydrophobic interaction; Initiation site; Ring current shielding; Type I turn

Indexed keywords

VIRUS ENVELOPE PROTEIN;

AMINO ACID SEQUENCE; AQUEOUS SOLUTION; ARTICLE; CIRCULAR DICHROISM; HUMAN IMMUNODEFICIENCY VIRUS 1; HYDROPHOBICITY; IN VITRO STUDY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE;

HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 0030839258     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00896.x     Document Type: Article

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