Direct characterization of the folded, unfolded and urea-denatured states of the C-terminal domain of the ribosomal protein L9

Journal of Molecular Biology

Volumn 349, Issue 4, 2005, Pages 839-846

  Li, Ying ^a   Picart, Francis ^a   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

Author keywords

C terminal domain of L9; NMR; Protein folding; Radius of hydration; Unfolded state

Indexed keywords

RIBOSOME PROTEIN; RIBOSOME PROTEIN L9; UNCLASSIFIED DRUG; UREA;

ARTICLE; CARBOXY TERMINAL SEQUENCE; DIFFUSION COEFFICIENT; HYDRODYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; PULSED FIELD GEL ELECTROPHORESIS; STRUCTURAL PROTEOMICS;

EID: 19544369340     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.04.017     Document Type: Article

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