ISSN:
1573-5001
Keywords:
automated assignment
;
NMR assignment of proteins
;
program Mapper
;
sequence-specific assignment
;
triple resonance experiments
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
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 13Cα and 13Cβ 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1008318805889
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