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  Measuring the chi(1) torsion angle in protein by CH-CH cross-correlated relaxation: A new resolution-optimised experiment

Carlomagno, T., Bermel, W., & Griesinger, C. (2003). Measuring the chi(1) torsion angle in protein by CH-CH cross-correlated relaxation: A new resolution-optimised experiment. Journal of Biomolecular NMR, 27(2), 151-157. Retrieved from http://www.springerlink.com/content/n667816u1776834m/fulltext.pdf.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0012-F013-B Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0028-DD30-D
Genre: Journal Article

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Carlomagno, T.1, Author           
Bermel, W., Author
Griesinger, C.2, Author           
Affiliations:
1Research Group of Liquid NMR Spectroscopy, MPI for biophysical chemistry, Max Planck Society, ou_578572              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: CH dipole; cross-correlated relaxation; dynamics; side-chain conformation; ubiquitin
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Language(s): eng - English
 Dates: 2003-10
 Publication Status: Issued
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 Identifiers: eDoc: 124263
URI: http://www.springerlink.com/content/n667816u1776834m/fulltext.pdf
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Title: Journal of Biomolecular NMR
Source Genre: Journal
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Pages: - Volume / Issue: 27 (2) Sequence Number: - Start / End Page: 151 - 157 Identifier: -