Co-translational myristoylation alters the quaternary structure of HIV-1 Nef in solution

Proteins: Structure, Function and Genetics

Volumn 60, Issue 4, 2005, Pages 658-669

  Dennis, Caitríona A ^a,c   Baron, Andrew ^a   Grossmann, J Günter ^b   Mazaleyrat, Sabine ^a   Harris, Mark ^a   Jaeger, Joachim ^a,c  

^a UNIVERSITY OF LEEDS   (United Kingdom)

^b DARESBURY LABORATORY   (United Kingdom)

^c WADSWORTH CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCINE; MONOMER; MYRISTIC ACID; NEF PROTEIN; OLIGOMER; PROTEIN N MYRISTOYLTRANSFERASE; RECOMBINANT PROTEIN; REDUCING AGENT;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; CELL MEMBRANE; CENTRIFUGATION; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CYTOSOL; DISSOCIATION; DISSOLUTION; ESCHERICHIA COLI; HUMAN IMMUNODEFICIENCY VIRUS 1; HYDROPHOBICITY; LENTIVIRINAE; LIGHT SCATTERING; MYRISTYLATION; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN QUATERNARY STRUCTURE; RNA TRANSLATION; X RAY CRYSTALLOGRAPHY;

BASE SEQUENCE; BINDING SITES; GENE PRODUCTS, NEF; HIV-1; MOLECULAR SEQUENCE DATA; MYRISTIC ACIDS; POLYMERASE CHAIN REACTION; PROTEIN BIOSYNTHESIS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT PROTEINS; RESTRICTION MAPPING; SOLUTIONS;

ESCHERICHIA COLI; HUMAN IMMUNODEFICIENCY VIRUS 1; PRIMATES;

EID: 24644466459     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20544     Document Type: Article

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