Comparing proteins by their internal dynamics: Exploring structure-function relationships beyond static structural alignments
Abstract
The growing interest for comparing protein internal dynamics owes much to the realisation that protein function can be accompanied or assisted by structural fluctuations and conformational changes. Analogously to the case of functional structural elements, those aspects of protein flexibility and dynamics that are functionally oriented should be subject to evolutionary conservation. Accordingly, dynamics-based protein comparisons or alignments could be used to detect protein relationships that are more elusive to sequence and structural alignments. Here we provide an account of the progress that has been made in recent years towards developing and applying general methods for comparing proteins in terms of their internal dynamics and advance the understanding of the structure-function relationship.
- Publication:
-
Physics of Life Reviews
- Pub Date:
- March 2013
- DOI:
- 10.1016/j.plrev.2012.10.009
- arXiv:
- arXiv:1212.4161
- Bibcode:
- 2013PhLRv..10....1M
- Keywords:
-
- Quantitative Biology - Biomolecules;
- Condensed Matter - Soft Condensed Matter
- E-Print:
- Review article, 24 pages, 10 figures. Journal article in "Physics of Life Reviews" available at http://dx.doi.org/10.1016/j.plrev.2012.10.009 along with several commentaries