Overcoming the problems associated with poor spectra quality of the protein kinase Byr2 using residual dipolar couplings | Zendy

Gronwald Wolfram | Zendy; Brunner Eike | Zendy; Huber Fritz | Zendy; Wenzler Michael | Zendy; Herrmann Christian | Zendy; Kalbitzer Hans Robert | Zendy

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Overcoming the problems associated with poor spectra quality of the protein kinase Byr2 using residual dipolar couplings

Author(s) -

Gronwald Wolfram,

Brunner Eike,

Huber Fritz,

Wenzler Michael,

Herrmann Christian,

Kalbitzer Hans Robert

Publication year - 2001

Publication title -

protein science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.353

H-Index - 175

eISSN - 1469-896X

pISSN - 0961-8368

DOI - 10.1110/ps.43201

Subject(s) - residual , dipole , residual dipolar coupling , spectral line , quality (philosophy) , physics , chemistry , chemical physics , biological system , computational chemistry , molecular physics , statistical physics , computer science , algorithm , biology , quantum mechanics

For the Ras‐binding domain of the protein kinase Byr2, only a limited number of NOE contacts could be initially assigned unambiguously, as the quality of the NOESY spectra was too poor. However, the use of residual 1 H– 15 N dipolar couplings in the beginning of the structure determination process allows to overcome this problem. We used a three‐step recipe for this procedure. A previously unknown structure could be calculated reasonably well with only a limited number of unambiguously assigned NOE contacts.

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