Letter to the editor: Solution structure of the hypothetical protein YpgF from Escherichia coli reveals an RNAse H fold [1]

Journal of Biomolecular NMR

Volumn 27, Issue 4, 2003, Pages 389-392

  Liu, Dingjiang ^a   Wang, Yu Sen ^a   Wyss, Daniel F ^a  

^a MERCK RESEARCH LABORATORIES   (United States)

Author keywords

Heteronuclear NMR; Holliday junction resolvase; Structural genomics

Indexed keywords

ESCHERICHIA COLI PROTEIN; HISTIDINE; RIBONUCLEASE; DEOXYRIBONUCLEASE; RIBONUCLEASE H; YQGF PROTEIN, E COLI;

AMINO ACID SEQUENCE; BACTERIAL GROWTH; CONTROLLED STUDY; GENETIC CODE; HOLLIDAY JUNCTION; ISOTOPE LABELING; LETTER; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STRUCTURE; CHEMISTRY; ISOLATION AND PURIFICATION; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE; PROTEIN CONFORMATION; SOLUTION AND SOLUBILITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

AMINO ACID SEQUENCE; ENDODEOXYRIBONUCLEASES; ESCHERICHIA COLI PROTEINS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; RIBONUCLEASE H, CALF THYMUS; SOLUTIONS;

EID: 0142180091     PISSN: 09252738     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1025840121177     Document Type: Letter

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