Analysing structural properties of human alcohol dehydrogenase class V
||Analysing structural properties of human alcohol dehydrogenase class V|
||Bengt Persson <firstname.lastname@example.org>|
||Uppsala universitet, Karolinska Institutet|
||2014-03-01 – 2014-09-01|
Alcohol dehydrogenase (ADH) is a family of enzymes involved in the breakdown of alcohols to aldehydes. In humans, the family has seven members, divided into five classes, ADH classes I--V (ADH1--5). The human class I--IV enzymes have been isolated and characterized, but all attempts to purify the class V enzyme have failed. The indications from in vitro experiments are that the ADH5 protein is unstable.
The purpose of our experiments is to compare the sequence and structure of ADH5 with those of the other ADH classes with known function. In order to do so, we have been using a dual sequence analysis and molecular dynamics approach.
We have earlier created multiple homology models of human ADH5 and simulated their behaviour using molecular dynamics. This (in combination with the aforementioned sequence analysis methods) allowed us to identify multiple regions that may cause structural instability in the enzyme.
What remains for us is to narrow down these regions in order to (hopefully) give us more distinct answers about the ADH5 enzymes and their apparent instability. In order to this, we need more computer time to perform multiple molecular dynamics simulations of modified ("mutated") versions of the human ADH5 protein to study the increase/decrease in stability.