Unknown

Dataset Information

0

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

ABSTRACT: Outer membrane ?-barrel proteins differ from ?-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 ?-helical inner membrane proteins. We have generated an equivalent potential for TM ?-barrel proteins. The similarities and differences between these two potentials provide insight into unique aspects of the folding and insertion of ?-barrel membrane proteins. This potential can predict orientation within the membrane and identify functional residues involved in intermolecular interactions.

SUBMITTER: Hsieh D 

PROVIDER: S-EPMC3323780 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

A knowledge-based potential highlights unique features of membrane α-helical and β-barrel protein insertion and folding.

Hsieh Daniel D   Davis Alexander A   Nanda Vikas V  

Protein science : a publication of the Protein Society 20111123 1

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 prot  ...[more]

Similar Datasets

Unknown Membrane defects accelerate outer membrane ?-barrel protein folding.
| S-EPMC4303321 | biostudies-literature
Unknown Statistically derived asymmetric membrane potentials from ?-helical and ?-barrel membrane proteins.
| S-EPMC5849751 | biostudies-literature
Unknown Membrane protein insertion through a mitochondrial ?-barrel gate.
| S-EPMC5959003 | biostudies-literature
Unknown Folding of the ?-Barrel Membrane Protein OmpA into Nanodiscs.
| S-EPMC6976806 | biostudies-literature
Unknown Outer Membrane Protein Insertion by the β-barrel Assembly Machine.
| S-EPMC6419762 | biostudies-literature
Unknown Physical determinants of ?-barrel membrane protein folding in lipid vesicles.
| S-EPMC3149260 | biostudies-literature
Unknown Mechanisms of integral membrane protein insertion and folding.
| S-EPMC4339636 | biostudies-literature
Unknown Membrane elastic fluctuations and the insertion and tilt of beta-barrel proteins.
| S-EPMC1479067 | biostudies-literature
Unknown A predictor of membrane class: Discriminating alpha-helical and beta-barrel membrane proteins from non-membranous proteins.
| S-EPMC1891694 | biostudies-literature
Unknown Stable folding core in the folding transition state of an alpha-helical integral membrane protein.
| S-EPMC3161581 | biostudies-literature