Hairpin folding of HIV gp41 abrogates lipid mixing function at physiologic pH and inhibits lipid mixing by exposed gp41 constructs

Biochemistry

Volumn 48, Issue 12, 2009, Pages 2714-2722

  Sackett, Kelly ^a   Nethercott, Matthew J ^a   Shai, Yechiel ^b   Weliky, David P ^a  

^a MICHIGAN STATE UNIVERSITY   (United States)

^b WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

BIOPHYSICAL STUDIES; CONFORMATIONAL CHANGES; FUSION MODELS; HAIRPIN CONFORMATIONS; HELIX BUNDLES; LIPID MIXING; LOW-ENERGY CONFORMATIONS; MEMBRANE DISRUPTIONS; MEMBRANE FUSIONS; MEMBRANE VESICLES; TARGET CELLS;

CONFORMATIONS; INTERNET; MEMBRANES;

CELL MEMBRANES;

GLYCOPROTEIN GP 41; VIRUS FUSION PROTEIN;

ANIMAL CELL; ARTICLE; CELL DISRUPTION; CELL MEMBRANE; CONTROLLED STUDY; ESCHERICHIA COLI; GENE CONSTRUCT; GROWTH INHIBITION; HUMAN IMMUNODEFICIENCY VIRUS; LIPID ANALYSIS; LIPID MIXING; MEMBRANE FUSION; MEMBRANE VESICLE; NONHUMAN; PH MEASUREMENT; PHYSIOLOGY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LIPID INTERACTION; PROTEIN STRUCTURE; TARGET CELL;

CIRCULAR DICHROISM; HIV ENVELOPE PROTEIN GP41; HYDROGEN-ION CONCENTRATION; LIPIDS; MEMBRANE FUSION; MODELS, BIOLOGICAL; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN FOLDING;

EID: 65249174493     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8019492     Document Type: Article

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