X-ray diffraction reveals the intrinsic difference in the physical properties of membrane and soluble proteins.

ABSTRACT: Membrane proteins are distinguished from soluble proteins by their insertion into biological membranes. This insertion is achieved via a noticeable arrangement of hydrophobic amino acids that are exposed at the surface of the protein, and renders the interaction with the aliphatic tails of lipids more energetically favorable. This important difference between these two categories of proteins is the source of the need for a specific handling of membrane proteins, which transpired in the creation of new tools for their recombinant expression, purification and even crystallization. Following this line, we show here that crystals of membrane proteins display systematically higher diffraction anisotropy than those of soluble proteins. This phenomenon dramatically hampers structure solution and

SUBMITTER: Robert X 

PROVIDER: S-EPMC5717104 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature