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Title: The interactions of peripheral membrane proteins with biological membranes

Abstract

The interactions of peripheral proteins with membrane surfaces are critical to many biological processes, including signaling, recognition, membrane trafficking, cell division and cell structure. On a molecular level, peripheral membrane proteins can modulate lipid composition, membrane dynamics and protein-protein interactions. Biochemical and biophysical studies have shown that these interactions are in fact highly complex, dominated by several different types of interactions, and have an interdependent effect on both the protein and membrane. Here we examine three major mechanisms underlying the interactions between peripheral membrane proteins and membranes: electrostatic interactions, hydrophobic interactions, and fatty acid modification of proteins. While experimental approaches continue to provide critical insights into specific interaction mechanisms, emerging bioinformatics resources and tools contribute to a systems-level picture of protein-lipid interactions. Through these recent advances, we begin to understand the pivotal role of protein-lipid interactions underlying complex biological functions at membrane interfaces.

Authors:
 [1];  [1]
  1. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Publication Date:
Research Org.:
Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1286884
Alternate Identifier(s):
OSTI ID: 1247815
Grant/Contract Number:  
AC05-00OR22725
Resource Type:
Accepted Manuscript
Journal Name:
Chemistry and Physics of Lipids
Additional Journal Information:
Journal Volume: 192; Journal ID: ISSN 0009-3084
Publisher:
Elsevier
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; protein-lipid interaction; biomembrane; phospholipid; peripheral membrane protein; membrane protein

Citation Formats

Johs, Alexander, and Whited, A. M.. The interactions of peripheral membrane proteins with biological membranes. United States: N. p., 2015. Web. doi:10.1016/j.chemphyslip.2015.07.015.
Johs, Alexander, & Whited, A. M.. The interactions of peripheral membrane proteins with biological membranes. United States. https://doi.org/10.1016/j.chemphyslip.2015.07.015
Johs, Alexander, and Whited, A. M.. Wed . "The interactions of peripheral membrane proteins with biological membranes". United States. https://doi.org/10.1016/j.chemphyslip.2015.07.015. https://www.osti.gov/servlets/purl/1286884.
@article{osti_1286884,
title = {The interactions of peripheral membrane proteins with biological membranes},
author = {Johs, Alexander and Whited, A. M.},
abstractNote = {The interactions of peripheral proteins with membrane surfaces are critical to many biological processes, including signaling, recognition, membrane trafficking, cell division and cell structure. On a molecular level, peripheral membrane proteins can modulate lipid composition, membrane dynamics and protein-protein interactions. Biochemical and biophysical studies have shown that these interactions are in fact highly complex, dominated by several different types of interactions, and have an interdependent effect on both the protein and membrane. Here we examine three major mechanisms underlying the interactions between peripheral membrane proteins and membranes: electrostatic interactions, hydrophobic interactions, and fatty acid modification of proteins. While experimental approaches continue to provide critical insights into specific interaction mechanisms, emerging bioinformatics resources and tools contribute to a systems-level picture of protein-lipid interactions. Through these recent advances, we begin to understand the pivotal role of protein-lipid interactions underlying complex biological functions at membrane interfaces.},
doi = {10.1016/j.chemphyslip.2015.07.015},
journal = {Chemistry and Physics of Lipids},
number = ,
volume = 192,
place = {United States},
year = {Wed Jul 29 00:00:00 EDT 2015},
month = {Wed Jul 29 00:00:00 EDT 2015}
}

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Cited by: 54 works
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