The energetic cost of domain reorientation in maltose-binding protein as studied by NMR and fluorescence spectroscopy

Proceedings of the National Academy of Sciences of the United States of America

Volumn 100, Issue 22, 2003, Pages 12700-12705

  Millet, Oscar ^a   Hudson, Rhea P ^b   Kay, Lewis E ^a  

^a UNIVERSITY OF TORONTO   (Canada)

^b HOSPITAL FOR SICK CHILDREN   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

APOPROTEIN; LIGAND; MALTOSE; MALTOSE BINDING PROTEIN; MALTOSE OLIGOSACCHARIDE; MALTOTRIOSE; MUTANT PROTEIN; OLIGOSACCHARIDE; SOLVENT; UNCLASSIFIED DRUG;

ARTICLE; CONFORMATIONAL TRANSITION; CORRELATION COEFFICIENT; ENERGY TRANSFER; FLUORESCENCE SPECTROSCOPY; HYDROPHOBICITY; LIGAND BINDING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN VARIANT; QUANTITATIVE STRUCTURE PROPERTY RELATION; ROTATION; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; WILD TYPE;

BINDING SITES; CARRIER PROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; MALTOSE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SENSITIVITY AND SPECIFICITY; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS;

EID: 0242331659     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.2134311100     Document Type: Article

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