Triosephosphate Isomerase: 15N and 13C Chemical Shift Assignments and Conformational Change upon Ligand Binding by Magic-Angle Spinning Solid-State NMR Spectroscopy

Journal of Molecular Biology

Volumn 397, Issue 1, 2010, Pages 233-248

  Xu, Yimin ^a   Lorieau, Justin ^b   McDermott, Ann E ^a  

^a Howard Hughes Medical Institute   (United States)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

conformational change; crystal packing; sequential assignment; solid state NMR; triosephosphate isomerase

Indexed keywords

ALANINE; CARBON 13; GLUTAMINE; GLYCINE; NITROGEN 15; TRIOSEPHOSPHATE ISOMERASE; APOPROTEIN; CARBON; GLYCEROPHOSPHATE; LIGAND; NITROGEN;

AQUEOUS SOLUTION; ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; INTERMETHOD COMPARISON; LIGAND BINDING; MICROCRYSTALLINE SUSPENSION; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTON NUCLEAR MAGNETIC RESONANCE; RESIDUE ANALYSIS; SOLID STATE; STRUCTURE ANALYSIS; X RAY; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; CHICKEN; ENZYME SPECIFICITY; ENZYMOLOGY; METABOLISM; METHODOLOGY; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; SOLUTION AND SOLUBILITY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANIMALS; APOPROTEINS; CARBON ISOTOPES; CATALYTIC DOMAIN; CHICKENS; CRYSTALLOGRAPHY, X-RAY; GLYCEROPHOSPHATES; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; NITROGEN ISOTOPES; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; SOLUTIONS; SUBSTRATE SPECIFICITY; TRIOSE-PHOSPHATE ISOMERASE;

EID: 77249138171     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.10.043     Document Type: Article

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