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The use of selective deuteration for the sequence specific 1 H NMR assignment of larger proteins
Author(s) -
Arrowsmith Cheryl H.,
TreatClemons Lynda,
Szilágyi László,
Pachter Ruth,
Jardetzky Oleg
Publication year - 1990
Publication title -
makromolekulare chemie. macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 0258-0322
DOI - 10.1002/masy.19900340104
Subject(s) - sequence (biology) , chemistry , nmr spectra database , nuclear magnetic resonance spectroscopy , isotopic labeling , spectral line , stereochemistry , biochemistry , physics , organic chemistry , astronomy
The possibility of extending NMR methods for structure determination to larger proteins (MW > 10 kD) depends on the development of isotopic labeling protocols for the simplification of their NMR spectra (isotopic spectral editing). We describe here the successful use of selective deuteration to obtain sequence specific assignments for (thus far) more than 50% of the residues of the trp repressor protein (25 kD). This is the largest protein for which detailed sequence specific assignments have been attempted to‐date.