Difference between revisions of "M82L"
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Revision as of 09:12, 11 August 2011
Contents
Structure-based Mutation Analysis
Mapping onto crystal structure
SCWRL
scwrl wt energy?
Hydrogen Bonding network
The following figures show the hydrogen bonds between the wildtype residue and its environment compared to the formation of hydrogen bonds when the corresponding residue is mutated.
- M82L
Comparing the figures 2 and 3 for the wildtype and the mutated amino acid on position 82, no change in the hydrogen bonding network can be observed. This is due to the similar physiochemical properties of these two amino acids. No atom which could serve as additional hydrogen-bond donor or acceptor was introduced or removed.
foldX Energy Comparison
| wildtype energy | total energy of mutated protein | difference |
|---|---|---|
| 401.00 | 437.88 | 36.88 |
minimise Energy Comparison
| wildtype energy | total energy of mutated protein | difference |
|---|---|---|
| -2485.452755 | -4253.174790 | -1767.722015 |
gromacs
| Energy | Average | Err.Est | RMSD | Tot-Drift (kJ/mol) |
|---|---|---|---|---|
| Bond | 2518.71 | 1700 | 6337.97 | -10023.3 |
| Angle | 3642.41 | 270 | 638.624 | -1479.34 |
| Potential | 5.16e+06 | 5.1e+06 | 7.47e+07 | -3.13e+07 |
