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Volumn 41, Issue 6, 2002, Pages 1759-1766
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Characterization of the tertiary structure of soluble CD4 bound to glycosylated full-length HIVgp120 by chemical modification of arginine residues and mass spectrometric analysis
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Author keywords
[No Author keywords available]
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Indexed keywords
TERTIARY STRUCTURES;
BLOOD;
DESORPTION;
IONIZATION;
MASS SPECTROMETRY;
PROTEINS;
BIOCHEMISTRY;
CD4 ANTIGEN;
GLYCOPROTEIN GP 120;
VIRUS ENVELOPE PROTEIN;
AMINO ACID SEQUENCE;
ARTICLE;
CHEMICAL MODIFICATION;
COVALENT BOND;
CRYSTAL STRUCTURE;
DERIVATIZATION;
ENZYME ACTIVE SITE;
GLYCOSYLATION;
HUMAN IMMUNODEFICIENCY VIRUS;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN INTERACTION;
PROTEIN PROCESSING;
PROTEIN PURIFICATION;
PROTEIN STRUCTURE;
PROTEIN TERTIARY STRUCTURE;
SPECTROMETRY;
AMINO ACID SEQUENCE;
ANTIGENS, CD4;
ARGININE;
BINDING SITES;
GLYCOSYLATION;
HIV ENVELOPE PROTEIN GP120;
HUMANS;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
PROTEIN BINDING;
PROTEIN STRUCTURE, TERTIARY;
RECOMBINANT PROTEINS;
SOLUBILITY;
SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;
SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;
HUMAN IMMUNODEFICIENCY VIRUS;
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EID: 0037065723
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi011626k Document Type: Article |
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Times cited : (34)
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References (37)
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