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Application of NMR in structural proteomics: Screening for proteins amenable to structural analysis

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78552

Rehm,  T.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78142

Huber,  R.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78123

Holak,  T. A.
Holak, Tad / NMR Spectroscopy, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Rehm, T., Huber, R., & Holak, T. A. (2002). Application of NMR in structural proteomics: Screening for proteins amenable to structural analysis. Structure, 10(12), 1613-1618.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6DC2-2
Abstract
In the time of structural proteomics when protein structures are targeted on a genome-wide scale, the detection of "well- behaved" proteins that would yield good quality NMR spectra or X-ray images is the key to high-throughput structure determination. Already, simple one-dimensional proton NMR spectra provide enough information for assessing the folding properties of proteins. Heteronuclear two-dimensional spectra are routinely used for screenings that reveal structural, as well as binding, properties of proteins. NMR can thus provide important information for optimizing conditions for protein constructs that are amenable to structural studies.