Normal mode analysis of protein dynamics
β Scribed by Case, David A.
- Book ID
- 120067979
- Publisher
- Elsevier Science
- Year
- 1994
- Tongue
- English
- Weight
- 626 KB
- Volume
- 4
- Category
- Article
- ISSN
- 0959-440X
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T w o DNA binding proteins, Cro and the amino-terminal domain of the repressor of bacteriophage 434 (434 Cro and 434 repressor) that regulate gene expression and contain a helix-turn-helix (HTH) motif responsible for their site-specific DNA recognition adopt very similar three-dimensional structures
Model-free methods are introduced to determine quantities pertaining to protein domain motions from normal mode analyses and molecular dynamics simulations. For the normal mode analysis, the methods are based on the assumption that in low frequency modes, domain motions can be well approximated by m
Effects of different treatments of the degrees of freedom of bond length stretching and bond angle bending in computational analysis of conformational dynamics of proteins and polypeptides are assessed. More specifically, the normal mode analysis of conformational dynamics of a-helix of deca-alanine