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A knowledge‐based potential highlights unique features of membrane α‐helical and β‐barrel protein insertion and folding
Author(s) -
Hsieh Daniel,
Davis Alexander,
Nanda Vikas
Publication year - 2012
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.758
Subject(s) - barrel (horology) , folding (dsp implementation) , membrane protein , protein folding , biophysics , chemistry , bacterial outer membrane , membrane , peripheral membrane protein , protein secondary structure , crystallography , biology , biochemistry , integral membrane protein , materials science , escherichia coli , gene , electrical engineering , composite material , engineering
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, E z , 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.