Bringing dynamic molecular machines into focus by methyl-TROSY NMR

Annual Review of Biochemistry

Volumn 83, Issue , 2014, Pages 291-315

  Rosenzweig, Rina ^a,b   Kay, Lewis E ^a,b,c  

^a Departments of Biochemistry   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c HOSPITAL FOR SICK CHILDREN   (Canada)

Author keywords

allostery; deuteration; highmolecular weight complexes; methyl labeling; protein NMR; proteinsubstrate interactions

Indexed keywords

3,4 METHYLENEDIOXYAMPHETAMINE; CHAPERONE; HEAT SHOCK PROTEIN 70; HIGH MOBILITY GROUP N2 PROTEIN; POTASSIUM CHANNEL; PROTEASOME; BACTERIAL PROTEIN; HEAT SHOCK PROTEIN; MACROMOLECULE; NUCLEOSOME; PROKARYOTIC POTASSIUM CHANNEL; PROTEIN;

ALLOSTERISM; ARTICLE; BIOCHEMISTRY; CELL FUNCTION; CHEMICAL LABELING; CHEMICAL STRUCTURE; CHROMATIN STRUCTURE; ELECTRON MICROSCOPY; HUMAN; MACHINE; MEDICAL RESEARCH; METHYL TRANSVERSE RELAXATION OPTIMIZED SPECTROSCOPY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR DYNAMICS; MOLECULAR MECHANICS; MOLECULAR WEIGHT; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOSOME; PLASTICITY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN INTERACTION; SYNAPSE VESICLE; X RAY DIFFRACTION; ANIMAL; BINDING SITE; CHEMISTRY; ENZYME ACTIVE SITE; EXOSOME; MACROMOLECULE; PH; PROCEDURES; PROTEIN CONFORMATION;

ALLOSTERIC SITE; ANIMALS; BACTERIAL PROTEINS; CATALYTIC DOMAIN; EXOSOMES; HEAT-SHOCK PROTEINS; HMGN2 PROTEIN; HUMANS; HYDROGEN-ION CONCENTRATION; MACROMOLECULAR SUBSTANCES; MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOSOMES; POTASSIUM CHANNELS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN CONFORMATION; PROTEINS;

EID: 84902209981     PISSN: 00664154     EISSN: 15454509     Source Type: Book Series    
DOI: 10.1146/annurev-biochem-060713-035829     Document Type: Article

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