The unfolded state of the C-terminal domain of the ribosomal protein L9 contains both native and non-native structure

Biochemistry

Volumn 48, Issue 22, 2009, Pages 4707-4719

  Shan, Bing ^a   Eliezer, David ^b   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

^b WEILL CORNELL MEDICAL COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE PROTON; C-TERMINAL DOMAINS; CONFORMATIONAL STATE; DYNAMIC PROPERTY; FOLDING KINETICS; HELICAL STRUCTURES; IDENTICAL CONDITIONS; MISFOLDING; NATIVE STATE; NEUTRAL PH; NON-NATIVE; RELAXATION RATES; RESIDUAL STRUCTURE; RIBOSOMAL PROTEINS; SIDE-CHAIN; STRAND STRUCTURE; TWO-STATE MODEL; UNFOLDED PROTEINS;

AMIDES; UREA;

PROTEIN FOLDING;

GLOBULAR PROTEIN; RIBOSOMAL PROTEIN L9; RIBOSOME PROTEIN; UNCLASSIFIED DRUG; UREA;

ALPHA HELIX; ARTICLE; BETA SHEET; CARBON NUCLEAR MAGNETIC RESONANCE; CARBOXY TERMINAL SEQUENCE; MOLECULAR DYNAMICS; MOLECULAR MODEL; NITROGEN NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE;

AMINO ACID SEQUENCE; CARBON ISOTOPES; HYDROGEN; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RIBOSOMAL PROTEINS;

EID: 66749176784     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802299j     Document Type: Article

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