The leucine zipper motif of the envelope glycoprotein ectodomain of human immunodeficiency virus type 1 contains conformationally flexible regions as revealed by NMR and circular dichroism studies in different media

Journal of Peptide Research

Volumn 57, Issue 3, 2001, Pages 234-239

  Chang, D Kwo ^a   Trivedi, V D ^a   Cheng, S F ^a   Francis, S ^a  

^a INSTITUTE OF CHEMISTRY   (Taiwan)

Author keywords

Coiled coil; Conformational change; Oligomerization; Secondary structure

Indexed keywords

GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 41; LEUCINE ZIPPER PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CIRCULAR DICHROISM; DISSOCIATION; HUMAN IMMUNODEFICIENCY VIRUS 1; LIGHT SCATTERING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; RECEPTOR BINDING;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; HIV ENVELOPE PROTEIN GP120; HIV ENVELOPE PROTEIN GP41; HIV-1; LEUCINE ZIPPERS; MAGNETIC RESONANCE SPECTROSCOPY; METHANOL; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN CONFORMATION; REPETITIVE SEQUENCES, AMINO ACID; SCATTERING, RADIATION; SOLVENTS;

HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 0035078486     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1397-002X.2000.00831.x     Document Type: Article

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