Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
170822 | Comptes Rendus Chimie | 2009 | 6 Pages |
Abstract
Human Odorant Binding Protein (OBPIIa) has a strong affinity for odorants belonging to the family of aldehydes. After having built the initial structures based on the protein sequence, we have performed molecular dynamics simulations on human OBP, free and bound to citral and undecanal to examine the reasons for this affinity from a dynamic point of view. The formation of a Schiff base between a Lysine residue and the aldehyde function could be responsible for this strong affinity.
Keywords
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Chemical Engineering (General)
Authors
Landry Charlier, Daniel Cabrol-Bass, Jérome Golebiowski,