The N-terminal part of Binder of SPerm 5 (BSP5), which promotes sperm capacitation in bovine species is intrinsically disordered

Biochemical and Biophysical Research Communications

Volumn 394, Issue 4, 2010, Pages 1036-1041

  Jois, Prashanth Sirigeri ^a   Manjunath, Puttaswamy ^a,b  

^a UNIVERSITY OF MONTREAL   (Canada)

^b UNIVERSITÉ DE MONTRÉAL   (Canada)

Author keywords

Binder of SPerm protein; Glycosylation; Intrinsic disorder; N terminal part; Protease sensitive; Thermostable

Indexed keywords

BINDER OF SPERM 5 PROTEIN; FIBRONECTIN; PROTEIN DERIVATIVE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANIMAL EXPERIMENT; ARTICLE; BIOINFORMATICS; CELL MIGRATION; CIRCULAR DICHROISM; CLONE; CONTROLLED STUDY; COW; CYTOLYSIS; ESCHERICHIA COLI; GENE EXPRESSION; HORSE; MALE; MASS SPECTROMETRY; MOLECULAR WEIGHT; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; SPERM; SPERMATOZOON CAPACITATION; THERMOSTABILITY;

AMINO ACID SEQUENCE; ANIMALS; CATTLE; CONSERVED SEQUENCE; MALE; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; RABBITS; SEMINAL VESICLE SECRETORY PROTEINS; SPERM CAPACITATION; SPERMATOZOA;

BOVINAE; EQUIDAE; ESCHERICHIA COLI; ORYCTOLAGUS CUNICULUS;

EID: 77950860747     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.03.118     Document Type: Article

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