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

Gronwald, W. and Brunner, E. and Huber, F. and Wenzler, M. and Herrmann, C. and Kalbitzer, Hans Robert (2001) Overcoming the problems associated with poor spectra quality of the protein kinase Byr2 using residual dipolar couplings. Protein science 10 (6), pp. 1260-1263.

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Abstract

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 ...

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Item Type:Article
Date:2001
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
9353189PubMed ID
10.1110/ps.43201DOI
Classification:
NotationType
Biochemistry/methodsMESH
Fungal Proteins/chemistryMESH
MAP Kinase Kinase KinasesMESH
Magnetic Resonance Spectroscopy/methodsMESH
Mitogen-Activated Protein Kinases/chemistryMESH
Models, MolecularMESH
Protein ConformationMESH
Schizosaccharomyces/chemistryMESH
Schizosaccharomyces pombe ProteinsMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:15 Sep 2010 09:06
Last Modified:15 Sep 2010 09:06
Item ID:16576
Owner Only: item control page
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