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- Andrea Cavalli
- Department of Chemistry, Cambridge University, Cambridge CB2 1EW, United Kingdom
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- Xavier Salvatella
- Department of Chemistry, Cambridge University, Cambridge CB2 1EW, United Kingdom
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- Christopher M. Dobson
- Department of Chemistry, Cambridge University, Cambridge CB2 1EW, United Kingdom
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- Michele Vendruscolo
- Department of Chemistry, Cambridge University, Cambridge CB2 1EW, United Kingdom
書誌事項
- 公開日
- 2007-06-05
- DOI
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- 10.1073/pnas.0610313104
- 公開者
- Proceedings of the National Academy of Sciences
この論文をさがす
説明
<jats:p>NMR spectroscopy plays a major role in the determination of the structures and dynamics of proteins and other biological macromolecules. Chemical shifts are the most readily and accurately measurable NMR parameters, and they reflect with great specificity the conformations of native and nonnative states of proteins. We show, using 11 examples of proteins representative of the major structural classes and containing up to 123 residues, that it is possible to use chemical shifts as structural restraints in combination with a conventional molecular mechanics force field to determine the conformations of proteins at a resolution of 2 Å or better. This strategy should be widely applicable and, subject to further development, will enable quantitative structural analysis to be carried out to address a range of complex biological problems not accessible to current structural techniques.</jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 104 (23), 9615-9620, 2007-06-05
Proceedings of the National Academy of Sciences
