Lipid exposure prediction enhances the inference of rotational angles of transmembrane helices.

ABSTRACT:

Background

Since membrane protein structures are challenging to crystallize, computational approaches are essential for elucidating the sequence-to-structure relationships. Structural modeling of membrane proteins requires a multidimensional approach, and one critical geometric parameter is the rotational angle of transmembrane helices. Rotational angles of transmembrane helices are characterized by their folded structures and could be inferred by the hydrophobic moment; however, the folding mechanism of membrane proteins is not yet fully understood. The rotational angle of a transmembrane helix is related to the exposed surface of a transmembrane helix, since lipid exposure gives the degree of accessibility of each residue in lipid environment. To the best of our knowledge, there

SUBMITTER: Lai JS 

PROVIDER: S-EPMC3854514 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature