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Sequence-specific NMR assignment of proteins by global fragment mapping with the program MAPPER (2000)
| Venue: | J. Biomol. NMR |
| Citations: | 30 - 0 self |
BibTeX
@ARTICLE{Güntert00sequence-specificnmr,
author = {Peter Güntert and Michael Salzmann and Daniel Braun and Kurt Wüthrich},
title = {Sequence-specific NMR assignment of proteins by global fragment mapping with the program MAPPER},
journal = {J. Biomol. NMR},
year = {2000},
volume = {17},
pages = {129--137}
}
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Abstract
A new program, MAPPER, for semiautomatic sequence-specific NMR assignment in proteins is introduced. The program uses an input of short fragments of sequentially neighboring residues, which have been assembled based on sequential NMR connectivities and for which either the 13 C # and 13 C # chemical shifts or data on the amino acid type from other sources are known. MAPPER then performs an exhaustive search for self-consistent simultaneous mappings of all these fragments onto the protein sequence. Compared to using only the individual mappings of the spectroscopically connected fragments, the global mapping adds a powerful new constraint, which results in resolving many otherwise intractable ambiguities. In an initial application, virtually complete sequencespecific assignments were obtained for a 110 kDa homooctameric protein, 7,8-dihydroneopterin aldolase from Staphylococcus aureus.
Keyphrases
sequence-specific nmr assignment program mapper global fragment mapping kda homooctameric protein exhaustive search short fragment powerful new constraint global mapping staphylococcus aureus connected fragment 8-dihydroneopterin aldolase intractable ambiguity semiautomatic sequence-specific nmr assignment self-consistent simultaneous mapping complete sequencespecific assignment sequential nmr connectivity individual mapping protein sequence chemical shift new program initial application
