| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2030032 | Structure | 2007 | 11 Pages |
Abstract
SummaryThe deformation patterns of a large set of representative proteins determined by essential dynamics extracted from atomistic simulations and coarse-grained normal mode analysis are compared. Our analysis shows that the deformational space obtained with both approaches is quite similar when taking into account a representative number of modes. The results provide not only a comprehensive validation of the use of a low-frequency modal spectrum to describe protein flexibility, but also a complete picture of normal mode limitations.
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Authors
Manuel Rueda, Pablo Chacón, Modesto Orozco,