SCOPUS 정보 검색 플랫폼

Volumn 9, Issue 2, 1997, Pages 181-200

Triple-resonance NOESY-based experiments with improved spectral resolution: Applications to structural characterization of unfolded, partially folded and folded proteins

(4) Zhang, Ouwen a,b,c Forman Kay, Julie D b,c Shortle, David d Kay, Lewis E a

a UNIVERSITY OF TORONTO (Canada)

b HOSPITAL FOR SICK CHILDREN (Canada)

c UNIVERSITY OF TORONTO (Canada)

d JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE (United States)

Author keywords

Heteronuclear; Multidimensional NMR; NOE; Unfolded or partially folded proteins

Indexed keywords

CARBON; MICROCOCCAL NUCLEASE; NITROGEN; PEPTIDE FRAGMENT; PROTEIN; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BIOSYNTHESIS; CHEMISTRY; ESCHERICHIA COLI; METABOLISM; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SENSITIVITY AND SPECIFICITY; SRC HOMOLOGY DOMAIN;

AMINO ACID SEQUENCE; CARBON ISOTOPES; ESCHERICHIA COLI; MAGNETIC RESONANCE SPECTROSCOPY; MICROCOCCAL NUCLEASE; NITROGEN ISOTOPES; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS; RECOMBINANT PROTEINS; SENSITIVITY AND SPECIFICITY; SRC HOMOLOGY DOMAINS;

EID: 0031064317 PISSN: 09252738 EISSN: None Source Type: Journal
DOI: 10.1023/A:1018658305040 Document Type: Article

Times cited : (87)

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