Analysis of electrostatic interactions in the denatured state ensemble of the N-terminal domain of L9 under native conditions

Proteins: Structure, Function and Bioinformatics

Volumn 79, Issue 12, 2011, Pages 3500-3510

  Meng, Wenli ^a   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

Author keywords

Denatured state ensemble; Electrostatic interactions; PK a; Protein stability; Ribosomal protein L9, pH titration; Unfolded state

Indexed keywords

ASPARAGINE; GLUTAMIC ACID; N TERMINAL DOMAIN OF L9; PROTEIN; UNCLASSIFIED DRUG; VALINE;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; DENATURED STATE ENSEMBLE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PKA; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON TRANSPORT; STATIC ELECTRICITY;

AMINO ACID SEQUENCE; AMINO ACIDS; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; PROTONS; RIBOSOMAL PROTEINS; STATIC ELECTRICITY; THERMODYNAMICS;

EID: 81055156798     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.23145     Document Type: Article

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