The denatured state ensemble contains significant local and long-range structure under native conditions: Analysis of the N-terminal domain of ribosomal protein L9

Biochemistry

Volumn 52, Issue 15, 2013, Pages 2662-2671

  Meng, Wenli ^a   Luan, Bowu ^a   Lyle, Nicholas ^b   Pappu, Rohit V ^b   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

^b WASHINGTON UNIVERSITY IN ST LOUIS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LONG RANGE INTERACTIONS; LONG-RANGE STRUCTURES; N-TERMINAL DOMAINS; PARAMAGNETIC RELAXATION ENHANCEMENTS; PROTEIN STABILITY; RESIDUAL STRUCTURE; RIBOSOMAL PROTEINS; SECONDARY STRUCTURES;

EXPERIMENTS; METABOLISM; PARAMAGNETISM; PROTEIN FOLDING; UREA;

PROTEINS;

BUFFER; CARBON 13; HYDROGEN; PROTEIN; RIBOSOMAL PROTEIN L9; RIBOSOME PROTEIN; UNCLASSIFIED DRUG; UREA;

AMINO TERMINAL SEQUENCE; ARTICLE; MAGNETISM; MUTANT; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE;

BUFFERS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MODELS, MOLECULAR; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RIBOSOMAL PROTEINS; SCATTERING, SMALL ANGLE; UREA; X-RAY DIFFRACTION;

EID: 84876220105     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301667u     Document Type: Article

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