Conformation Changes in E. coli Rho Monitored by Hydrogen/Deuterium Exchange and Mass Spectrometry: Response to Ligand Binding

Journal of Molecular Biology

Volumn 402, Issue 5, 2010, Pages 813-824

  Stitt, Barbara L ^a   Xiao, Hui ^b  

^a TEMPLE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

Helicase; Hydrogen deuterium exchange; Mass spectrometry; Rho; Transcription termination

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE MAGNESIUM; HELICASE; OLIGOMER; POLYCYTIDYLIC ACID; RHO FACTOR; BACTERIAL RNA; DEUTERIUM; ESCHERICHIA COLI PROTEIN; HYDROGEN; MESSENGER RNA; PROTEIN BINDING; RHO PROTEIN, E COLI;

AMINO TERMINAL SEQUENCE; ANALYTIC METHOD; ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DEUTERIUM HYDROGEN EXCHANGE; ENZYME ACTIVE SITE; ESCHERICHIA COLI; HYDROLYSIS; LIGAND BINDING; MASS SPECTROMETRY; MONITORING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN RNA BINDING; RNA SYNTHESIS; AMINO ACID SEQUENCE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; PROCEDURES; PROTEIN QUATERNARY STRUCTURE;

ESCHERICHIA COLI;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; DEUTERIUM; ESCHERICHIA COLI PROTEINS; HYDROGEN; MASS SPECTROMETRY; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; RNA, BACTERIAL; RNA, MESSENGER;

EID: 77957220498     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.08.004     Document Type: Article

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