Statistical analysis of the protein environment of N-glycosylation sites: Implications for occupancy, structure, and folding

Glycobiology

Volumn 14, Issue 2, 2004, Pages 103-114

  Petrescu, Andrei J ^a,b   Milac, Adina L ^b   Petrescu, Stefana M ^a,b   Dwek, Raymond A ^a   Wormald, Mark R ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b ACADEMY OF ROMANIAN SCIENTISTS   (Romania)

Author keywords

Glycan protein linkage; N glycosylation sites; Occupancy; Protein folding; X ray diffraction

Indexed keywords

AROMATIC AMINO ACID; ASPARAGINE; GLYCAN; GLYCOPROTEIN; THREONINE;

AMINO ACID COMPOSITION; AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CONTROLLED STUDY; CRYSTALLOGRAPHY; EVOLUTION; HYDROPHOBICITY; PRIORITY JOURNAL; PROBABILITY; PROTEIN BINDING; PROTEIN DATA BANK; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN GLYCOSYLATION; PROTEIN INTERACTION; PROTEIN MODIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; QUALITY CONTROL; STATISTICAL ANALYSIS; SURFACE PROPERTY;

AMINO ACIDS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DATABASES, PROTEIN; GLYCOPROTEINS; GLYCOSYLATION; MODELS, STATISTICAL; POLYSACCHARIDES; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; TORSION;

EID: 1342327544     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/cwh008     Document Type: Article

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