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NMR studies of structure and dynamics of isotope enriched proteins
Author(s) -
Wagner Gerhard,
Thanabal V.,
Stockman Brian J.,
Peng Jeffrey W.,
Nirmala N. R.,
Hyberts Sven G.,
Goldberg Matthew S.,
Detlefsen David J.,
Clubb Robert T.,
Adler Marc
Publication year - 1992
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360320414
Subject(s) - chemistry , dynamics (music) , isotope , computational biology , computational chemistry , biophysics , nuclear physics , physics , acoustics , biology
Structural studies of globular proteins by nmr can be enhanced by the use of isotope enrichment. We have been working with proteins enriched with 15 N, and with both 15 N and 13 C. Due to the isotope enrichment we could assign several large proteins with up to 186 residues and could address structural questions. Furthermore, we can accurately measure heteronuclear and homonuclear vicinal coupling constants. This involves in part multidimensional multiple resonance experiments. This is important for characterization of minor conformational changes caused by mutations. We have also made use of isotope enrichment to study the internal mobility of proteins. We also have developed novel methods for measuring accurately 15 N relaxation parameters, in particular transverse relaxation rates. This has led us toward a method for directly mapping spectral density functions of the rotational motions of N–H bond vectors in proteins. The protein systems that are discussed include the unlabeled proteins kistrin and cytochrome c551, and the labeled proteins eglin c, a flavodoxin, and human dihydrofolate reductase.