Difference between revisions of "M82L"
From Bioinformatikpedia
(→Hydrogen Bonding network) |
(→Hydrogen Bonding network) |
||
Line 4: | Line 4: | ||
scwrl wt energy? |
scwrl wt energy? |
||
+ | |||
+ | ==== Side chain properties ==== |
||
+ | |||
+ | |||
+ | {|class="centered" |
||
+ | |[[File:Wildtype1_BCKDHAMinimise.png|thumb|Figure 2: Structure of methionine on position 82 in the wildtype protein]] |
||
+ | |[[File:Mutation1_BCKDHAMinimise.png|thumb|Figure 3: Structure of Leucine on position 82 in the mutated protein]] |
||
+ | |} |
||
==== Hydrogen Bonding network ==== |
==== Hydrogen Bonding network ==== |
||
Line 10: | Line 18: | ||
{|class="centered" |
{|class="centered" |
||
− | |[[File:BCKDHA_Wt37.png|thumb|150px|Figure |
+ | |[[File:BCKDHA_Wt37.png|thumb|150px|Figure 4: Hydrogen Bonds for methionine on pos 82 in the wild type structure]] |
− | |[[File:BCKDHA_Mut37.png|thumb|150px|Figure |
+ | |[[File:BCKDHA_Mut37.png|thumb|150px|Figure 5: Hydrogen Bonds for leucine on pos 82 in the mutated type structure]] |
|} |
|} |
||
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. |
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. |
Revision as of 09:36, 11 August 2011
Contents
Structure-based Mutation Analysis
Mapping onto crystal structure
SCWRL
scwrl wt energy?
Side chain properties
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.
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 comparison
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 |