Biophysical characterisation reveals structural disorder in the nucleolar protein, Dribble

Biochemical and Biophysical Research Communications

Volumn 343, Issue 1, 2006, Pages 311-318

  Yiu, C P Benny ^a   Beavil, Rebecca L ^b   Chan, H Y Edwin ^a  

^a CHINESE UNIVERSITY OF HONG KONG   (Hong Kong)

^b KING'S COLLEGE LONDON   (United Kingdom)

Author keywords

HRB2; Intrinsically disordered protein; Intrinsically unfolded proteins; K homology; Krr1p; Pfg27; RNA binding

Indexed keywords

NUCLEAR PROTEIN; PROTEIN DRIBBLE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BIOINFORMATICS; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; IN VITRO STUDY; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN STRUCTURE; RNA BINDING; SPECTROSCOPY;

AMINO ACID SEQUENCE; ANIMALS; BIOPHYSICS; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; MOLECULAR SEQUENCE DATA; NUCLEAR PROTEINS; PROTEIN CONFORMATION; RNA; RNA-BINDING PROTEINS; SOLVENTS;

ESCHERICHIA COLI;

EID: 33645098224     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.02.153     Document Type: Article

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