Mars – robust automatic backbone assignment of proteins
| Venue: | Journal of Biomolecular NMR |
| Citations: | 13 - 1 self |
BibTeX
@ARTICLE{Jung_mars–,
author = {Young-sang Jung and Markus Zweckstetter},
title = {Mars – robust automatic backbone assignment of proteins},
journal = {Journal of Biomolecular NMR},
year = {},
pages = {2004}
}
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Abstract
MARS a program for robust automatic backbone assignment of 13 C / 15 N labeled proteins is presented. MARS does not require tight thresholds for establishing sequential connectivity or detailed adjustment of these thresholds and it can work with a wide variety of NMR experiments. Using only 13 C α / 13 C β connectivity information, MARS allows automatic, error-free assignment of 96 % of the 370-residue maltose-binding protein. MARS can successfully be used when data are missing for a substantial portion of residues or for proteins with very high chemical shift degeneracy such as partially or fully unfolded proteins. Other sources of information, such as residue specific information or known assignments from a homologues protein, can be included into the assignment process. MARS exports its result in SPARKY format. This allows visual validation and integration of automated and manual assignment.
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