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Article
A knowledge-based potential highlights unique features of membrane α-helical and β-barrel protein insertion and folding
Article first published online: 23 NOV 2011
DOI: 10.1002/pro.758
Copyright © 2011 The Protein Society
Additional Information
How to Cite
Hsieh, D., Davis, A. and Nanda, V. (2012), A knowledge-based potential highlights unique features of membrane α-helical and β-barrel protein insertion and folding. Protein Science, 21: 50–62. doi: 10.1002/pro.758
Publication History
- Issue published online: 15 DEC 2011
- Article first published online: 23 NOV 2011
- Accepted manuscript online: 26 OCT 2011 08:28AM EST
- Manuscript Accepted: 19 OCT 2011
- Manuscript Revised: 6 SEP 2011
- Manuscript Received: 8 JUN 2011
Funded by
- National Institutes of Health. Grant Number: R01 GM089949-01A1
Keywords:
- outer membrane proteins;
- protein folding;
- hydrophobicity scale;
- secondary structure;
- statistical potentials;
- protein–protein interactions
Abstract
Outer membrane β-barrel proteins differ from α-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, Ez, was derived for α-helical inner membrane proteins. We have generated an equivalent potential for TM β-barrel proteins. The similarities and differences between these two potentials provide insight into unique aspects of the folding and insertion of β-barrel membrane proteins. This potential can predict orientation within the membrane and identify functional residues involved in intermolecular interactions.