期刊
JOURNAL OF BIOMOLECULAR NMR
卷 18, 期 2, 页码 129-137出版社
SPRINGER
DOI: 10.1023/A:1008318805889
关键词
automated assignment; NMR assignment of proteins; program MAPPER; sequence-specific assignment; triple resonance experiments
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 C-13(alpha) and C-13(beta) 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 sequence-specific assignments were obtained for a 110 kDa homooctameric protein, 7,8-dihydroneopterin aldolase from Staphylococcus aureus.
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