SCOPUS 정보 검색 플랫폼

Volumn 10, Issue 17, 2009, Pages 2736-2739

A cost-effective labeling strategy for the NMR study of large proteins: Selective 15N-labeling of the tryptophan side chains of prolyl oligopeptidase

(6) Tarragó, Teresa a Claasen, Birgit a Kichik, Nessim a Rodriguez Mias, Ricard A c Gairí, Margarida b Giralt, Ernest a,b

a INSTITUTE FOR RESEARCH IN BIOMEDICINE (Spain)

b UNIVERSITY OF BARCELONA (Spain)

c HARVARD MEDICAL SCHOOL (United States)

Author keywords

Indole; NMR spectroscopy; Prolyl oligopeptidase; Proteins; Selective labeling

Indexed keywords

NITROGEN 15; PHENYLALANINE; PROLYL ENDOPEPTIDASE; SERINE PROTEINASE; TRYPTOPHAN;

AMINO ACID METABOLISM; AMINO ACID SUBSTITUTION; ANISOTROPY; ARTICLE; BINDING AFFINITY; CHEMICAL LABELING; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; COST EFFECTIVENESS ANALYSIS; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME BINDING; ENZYME STRUCTURE; HETERONUCLEAR SINGLE QUANTUM COHERENCE; HYDROPHOBICITY; INCUBATION TIME; MASS SPECTROMETRY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTON NUCLEAR MAGNETIC RESONANCE; SIGNAL NOISE RATIO; SITE DIRECTED MUTAGENESIS; WILD TYPE;

ANIMALS; MODELS, MOLECULAR; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, TERTIARY; PROTEINS; RESEARCH; SERINE ENDOPEPTIDASES; TRYPTOPHAN;

EID: 73149085987 PISSN: 14394227 EISSN: 14397633 Source Type: Journal
DOI: 10.1002/cbic.200900575 Document Type: Article

Times cited : (13)

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