High-throughput backbone resonance assignment of small 13C, 15N-labeled proteins by a triple-resonance experiment with four sequential connectivity pathways using chemical shift-dependent, apparent 1J (1H,13C): HNCACBcodedHAHB

Journal of Magnetic Resonance

Volumn 165, Issue 2, 2003, Pages 315-319

  Pegan, Scott ^a   Kwiatkowski, Witek ^a   Choe, Senyon ^a   Riek, Roland ^a  

^a SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

Author keywords

Chemical shift coded experiment; High throughput resonance assignment; Multi dimensional experiment; NMR; Protein

Indexed keywords

DNA; ENZYMES; HYDROGEN; NUCLEAR MAGNETIC RESONANCE; VIRUSES;

CHEMICAL-SHIFT CODING;

BONE;

VACCINIA VIRUS;

AMINO ACID; CARBON; DNA TOPOISOMERASE; NITROGEN; PROTEIN;

ALGORITHM; AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; COMPARATIVE STUDY; CRYSTALLOGRAPHY; ENZYMOLOGY; EVALUATION; METHODOLOGY; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE ANALYSIS; SPIN LABELING; VACCINIA VIRUS; VALIDATION STUDY;

ALGORITHMS; AMINO ACID SEQUENCE; AMINO ACIDS; CARBON ISOTOPES; CRYSTALLOGRAPHY; DNA TOPOISOMERASES, TYPE I; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; NITROGEN ISOTOPES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; PROTEINS; SEQUENCE ANALYSIS, PROTEIN; SPIN LABELS; VACCINIA VIRUS;

EID: 0344033628     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmr.2003.08.012     Document Type: Article

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