A knowledge-based potential highlights unique features of membrane alpha-helical and beta-barrel protein insertion and folding

作者：Hsieh Daniel; Davis Alexander; Nanda Vikas^*

来源：Protein Science, 2012, 21(1): 50-62.

DOI：10.1002/pro.758

• outer membrane proteins
• protein folding
• hydrophobicity scale
• secondary structure
• statistical potentials
• protein-protein interactions

Outer membrane beta-barrel proteins differ from a-helical inner membrane proteins in lipid environment, secondary structure, and the proposed processes of folding and insertion. It is reasonable to expect that outer membrane proteins may contain primary sequence information specific for their folding and insertion behavior. In previous work, a depth-dependent insertion potential, E-z, was derived for a-helical inner membrane proteins. We have generated an equivalent potential for TM beta-barrel proteins. The similarities and differences between these two potentials provide insight into unique aspects of the folding and insertion of beta-barrel membrane proteins. This potential can predict orientation within the membrane and identify functional residues involved in intermolecular interactions.

• 出版日期2012-1