Automated analysis of nuclear magnetic resonance assignments for proteins
Recent developments in protein NMR technology provide spectral data that are highly amenable to analysis by computer software systems. Automated methods of analysis use constraint satisfaction, pseudoenergy minimization, directed search, neural net, simulated annealing, and/or genetic algorithms to...
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| Veröffentlicht in: | Current opinion in structural biology 1995-10, Vol.5 (5), p.664-673 |
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| container_end_page | 673 |
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| container_issue | 5 |
| container_start_page | 664 |
| container_title | Current opinion in structural biology |
| container_volume | 5 |
| creator | Zimmerman, Diane E Montelione, Gaetano T |
| description | Recent developments in protein NMR technology provide spectral data that are highly amenable to analysis by computer software systems. Automated methods of analysis use constraint satisfaction, pseudoenergy minimization, directed search, neural net, simulated annealing, and/or genetic algorithms to establish sequential links and sequence-specific assignments. The most advanced systems provide automated analysis of complete backbone and extensive side-chain resonance assignments for proteins of 50–150 amino acids. |
| doi_str_mv | 10.1016/0959-440X(95)80060-3 |
| format | Article |
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Automated methods of analysis use constraint satisfaction, pseudoenergy minimization, directed search, neural net, simulated annealing, and/or genetic algorithms to establish sequential links and sequence-specific assignments. 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| fulltext | fulltext |
| identifier | ISSN: 0959-440X |
| ispartof | Current opinion in structural biology, 1995-10, Vol.5 (5), p.664-673 |
| issn | 0959-440X 1879-033X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77781657 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amino Acid Sequence Amino Acids - chemistry Magnetic Resonance Spectroscopy - methods Molecular Conformation Protein Structure, Secondary Protein Structure, Tertiary Proteins - chemistry Software |
| title | Automated analysis of nuclear magnetic resonance assignments for proteins |
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