Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6487144 | Computational Biology and Chemistry | 2013 | 44 Pages |
Abstract
- Molecular dynamic analysis of open to close conformation for two LolA derivatives, LolA(R43L) and MsL43R.
- In silico point mutation of Leu43 to Arg43 induced conformational changes leading complete closed conformation of protein.
- Conformational changes from open to close observed for the first time in absence of lipoprotein of LolA.
- In addition to Arg43, residue Asn45 identified to play a central role in stability of protein by hydrogen bond formation.
- Closure of hydrophobic cavity takes place at two levels: closing of lid at the interface and loops at the entrance.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Priyadarshini Murahari, Sharmila Anishetty, Gautam Pennathur,