Dipolar \Waves\ as \NMR\ maps of helices in proteins
M. Mesleh, und S. Opella. J. Magn. Reson., 163 (2):
288--299(August 2003)
Zusammenfassung
Dipolar Waves describe the periodic variation in the magnitudes of dipolar couplings in the backbone of a protein as a function of residue number. They provide a direct link between experimental measurements of dipolar couplings in aligned samples and the periodicity inherent in regular secondary structure elements. It is possible to identify the residues in a helix and the type of helix, deviations from ideality, and to orient the helices relative to an external axis in completely aligned samples and relative to each other in a common frame in weakly aligned samples with Dipolar Waves. They provide a tool for accurately describing helices and a step towards high throughput structure determination of proteins.
%0 Journal Article
%1 mesleh_dipolar_2003-1
%A Mesleh, Michael F
%A Opella, Stanley J
%D 2003
%J J. Magn. Reson.
%K Algorithms,Crystallography,Magnetic Conformation,Protein Isotopes,Periodicity,Protein Labels Resonance Spectroscopy,Magnetics,Nitrogen Structure,Proteins,Protons,Secondary,Spin
%N 2
%P 288--299
%T Dipolar \Waves\ as \NMR\ maps of helices in proteins
%V 163
%X Dipolar Waves describe the periodic variation in the magnitudes of dipolar couplings in the backbone of a protein as a function of residue number. They provide a direct link between experimental measurements of dipolar couplings in aligned samples and the periodicity inherent in regular secondary structure elements. It is possible to identify the residues in a helix and the type of helix, deviations from ideality, and to orient the helices relative to an external axis in completely aligned samples and relative to each other in a common frame in weakly aligned samples with Dipolar Waves. They provide a tool for accurately describing helices and a step towards high throughput structure determination of proteins.
@article{mesleh_dipolar_2003-1,
abstract = {Dipolar Waves describe the periodic variation in the magnitudes of dipolar couplings in the backbone of a protein as a function of residue number. They provide a direct link between experimental measurements of dipolar couplings in aligned samples and the periodicity inherent in regular secondary structure elements. It is possible to identify the residues in a helix and the type of helix, deviations from ideality, and to orient the helices relative to an external axis in completely aligned samples and relative to each other in a common frame in weakly aligned samples with Dipolar Waves. They provide a tool for accurately describing helices and a step towards high throughput structure determination of proteins.},
added-at = {2017-03-14T02:48:56.000+0100},
author = {Mesleh, Michael F and Opella, Stanley J},
biburl = {https://www.bibsonomy.org/bibtex/23f82dd8861077f4bebc38b43d17b00f2/nmrresource},
interhash = {0acea848ce7f640f35ac158480a02c26},
intrahash = {3f82dd8861077f4bebc38b43d17b00f2},
issn = {1090-7807},
journal = {J. Magn. Reson.},
keywords = {Algorithms,Crystallography,Magnetic Conformation,Protein Isotopes,Periodicity,Protein Labels Resonance Spectroscopy,Magnetics,Nitrogen Structure,Proteins,Protons,Secondary,Spin},
month = aug,
number = 2,
pages = {288--299},
pmid = {12914844},
timestamp = {2017-03-14T02:49:21.000+0100},
title = {{Dipolar {\{}Waves{\}} as {\{}NMR{\}} maps of helices in proteins}},
volume = 163,
year = 2003
}