Access the full text.
Sign up today, get DeepDyve free for 14 days.
Loading next page...
/lp/annual-reviews/collective-variable-description-of-native-protein-dynamics-LiCuSPi8uN
References
References for this paper are not available at this time. We will be adding them shortly, thank you for your patience.
- Publisher
- Annual Reviews
- Copyright
- Copyright 1995 Annual Reviews. All rights reserved
- Subject
- Review Articles
- ISSN
- 0066-426X
- eISSN
- 1545-1593
- DOI
- 10.1146/annurev.pc.46.100195.001255
- pmid
- 24329489
- Publisher site
- See Article on Publisher Site
Abstract
The importance of collective motions in proteins, such as hinge-bending motions or motions involving domains, has been recognized. Occurrence of such motions and their experimental and theoretical studies are reviewed. Normal-mode analysis and principal component analysis are powerful theoretical tools for studying such motions. The former is based on the assumption of harmonicity of the dynamics, while the latter is valid even when the dynamics is highly anharmonic. The results of the latter analysis indicate that most important conformational events are taking place in a conformational subspace spanned by a rather small number of principal modes, and this important subspace is also spanned by a small number of normal modes. The normal-mode refinement method of protein X-ray crystallography, which is developed based on the concept of the above important subspace, is discussed.
Journal
Annual Review of Physical Chemistry – Annual Reviews
Published: Oct 1, 1995
Keywords: normal-mode analysis; computer simulation; anharmonicity; X-ray refinement; solvent effects