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Automated protein NMR structure determination in solution

Gronwald, Wolfram and Kalbitzer, Hans Robert (2010) Automated protein NMR structure determination in solution. Methods in molecular biology 673, pp. 95-127.

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Abstract

The main drawback of protein NMR spectroscopy today is still the extensive amount of time required for solving a single structure. The main bottleneck in this respect is the manual evaluation of the experimental spectra. A clear solution to this challenge is the development of automated methods for this purpose. At the current stage of development, this goal has been almost or in a few cases ...

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Item type:Article
Date:2010
Additional Information (public):Book Title: Computational Biology (978-1-60761-842-3)
Institutions:Medicine > Institut für Funktionelle Genomik > Lehrstuhl für Funktionelle Genomik (Prof. Oefner)
Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
20835795PubMed ID
10.1007/978-1-60761-842-3_7DOI
Classification:
NotationType
AlgorithmsMESH
ArtifactsMESH
AutomationMESH
Computer SimulationMESH
Databases, ProteinMESH
HumansMESH
Magnetic Resonance Spectroscopy/methodsMESH
Models, MolecularMESH
Proteins/chemistryMESH
Reproducibility of ResultsMESH
SolutionsMESH
Structural Homology, ProteinMESH
Dewey Decimal Classification:500 Science > 500 Natural sciences & mathematics
500 Science > 570 Life sciences
600 Technology > 610 Medical sciences Medicine
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:30635
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