The scaffold protein IscU retains a structured conformation in the Fe-S cluster assembly complex

ChemBioChem

Volumn 15, Issue 11, 2014, Pages 1682-1686

  Yan, Robert ^a,b   Kelly, Geoff ^a   Pastore, Annalisa ^b  

^a NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

^b KING'S COLLEGE LONDON   (United Kingdom)

Author keywords

iron sulfur clusters; methyl TROSY; NMR spectroscopy; protein protein interactions

Indexed keywords

DEUTERIUM; FERRIC ION; ISCU PROTEIN; ISOLEUCINE; LEUCINE; SCAFFOLD PROTEIN; SULFUR; TIOCONAZOLE; TRYPTOPHAN; UNCLASSIFIED DRUG; VALINE; CYSTATHIONINE GAMMA LYASE; ESCHERICHIA COLI PROTEIN; IRON SULFUR PROTEIN; ISCU PROTEIN, E COLI; LYASE;

ARTICLE; CRYSTAL STRUCTURE; HETERONUCLEAR MULTIPLE QUANTUM COHERENCE; HETERONUCLEAR SINGLE QUANTUM COHERENCE; ISOMERIZATION; MOLECULAR WEIGHT; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE; SIGNAL NOISE RATIO; TITRIMETRY; CHEMISTRY; ESCHERICHIA COLI; HUMAN; METABOLISM;

CARBON-SULFUR LYASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HUMANS; IRON-SULFUR PROTEINS; PROTEIN CONFORMATION;

EID: 84904699765     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.201402211     Document Type: Article

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