Conformational analysis of a set of peptides corresponding to the entire primary sequence of the N-terminal domain of the ribosomal protein L9: Evidence for stable native-like secondary structure in the unfolded state

Journal of Molecular Biology

Volumn 287, Issue 2, 1999, Pages 395-407

  Luisi, Donna L ^a   Wu, Wen Jin ^a   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

Author keywords

Denatured state; Peptide structure; Protein folding; Ribosomal protein L9; helix

Indexed keywords

PROLINE; RIBOSOME PROTEIN; THREONINE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; IONIC STRENGTH; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTON NUCLEAR MAGNETIC RESONANCE;

EID: 0033605920     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2595     Document Type: Article

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