DynDom is a fully automated program offering the determination of protein domains, hinge axes and amino acid residues that are involved in hinge bending.
The field of protein dynamics is concerned with the conformational changes that occur within proteins. Proteins, such as enzymes, adopt different conformations at different stages of the catalytic cycle, and understanding how proteins make transitions between conformations is an important part of understanding how they work. DynDom is a fully automated program offering the determination of protein domains, hinge axes and amino acid residues that are involved in hinge bending.
- Fully automated
- Determination of protein domains, hinge axes and hinge bends
- Easily understandable view of conformational changes
You can use DynDom if you have two conformations of the same protein, these may be two X-ray structures, or structures generated using simulation techniques, such as molecular dynamics or normal mode analysis. DynDom offers an easily understandable view of the conformational changes that take place. This change may be a complicated one but DynDom aids in visualising the movement of domains as quasi-rigid bodies.
Proteins 1997, 27(3), 425-437. doi:10.1002/(SICI)1097-0134(199703)27:3<425::AID-PROT10>3.0.CO;2-N
Team led by Dr Steven Hayward
Image sourced from: fizz.cmp.uea.ac.uk/dyndom/