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Title: Organization, Structure and Activity of Proteins in Monolayers

Abstract

Many different processes take place at the cell membrane interface. Indeed, for instance, ligands bind membrane proteins which in turn activate peripheral membrane proteins, some of which are enzymes whose action is also located at the membrane interface. Native cell membranes are difficult to use to gain information on the activity of individual proteins at the membrane interface because of the large number of different proteins involved in membranous processes. Model membrane systems, such as monolayers at the air-water interface, have thus been extensively used during the last 50 years to reconstitute proteins and to gain information on their organization, structure and activity in membranes. In the present paper, we review the recent work we have performed with membrane and peripheral proteins as well as enzymes in monolayers at the air-water interface. We show that the structure and orientation of gramicidin has been determined by combining different methods. Furthermore, we demonstrate that the secondary structure of rhodopsin and bacteriorhodopsin is indistinguishable from that in native membranes when appropriate conditions are used. We also show that the kinetics and extent of monolayer binding of myristoylated recoverin is much faster than that of the nonmyristoylated form and that this binding is highlymore » favored by the presence polyunsaturated phospholipids. Moreover, we show that the use of fragments of RPE65 allow determine which region of this protein is most likely involved in membrane binding. Monomolecular films were also used to further understand the hydrolysis of organized phospholipids by phospholipases A2 and C.« less

Authors:
; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
929797
Report Number(s):
BNL-80344-2008-JA
TRN: US200822%%1016
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Colloids and Surfaces B: Biointerfaces; Journal Volume: 58; Journal Issue: 2
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; CELL MEMBRANES; ENZYMES; KINETICS; LIGANDS; MEMBRANE PROTEINS; MEMBRANES; ORIENTATION; PHOSPHOLIPIDS; PROTEINS; RHODOPSIN; national synchrotron light source

Citation Formats

Boucher,J., Trudel, E., Methot, M., Desmeules, P., and Salesse, C. Organization, Structure and Activity of Proteins in Monolayers. United States: N. p., 2007. Web. doi:10.1016/j.colsurfb.2007.03.019.
Boucher,J., Trudel, E., Methot, M., Desmeules, P., & Salesse, C. Organization, Structure and Activity of Proteins in Monolayers. United States. doi:10.1016/j.colsurfb.2007.03.019.
Boucher,J., Trudel, E., Methot, M., Desmeules, P., and Salesse, C. Mon . "Organization, Structure and Activity of Proteins in Monolayers". United States. doi:10.1016/j.colsurfb.2007.03.019.
@article{osti_929797,
title = {Organization, Structure and Activity of Proteins in Monolayers},
author = {Boucher,J. and Trudel, E. and Methot, M. and Desmeules, P. and Salesse, C.},
abstractNote = {Many different processes take place at the cell membrane interface. Indeed, for instance, ligands bind membrane proteins which in turn activate peripheral membrane proteins, some of which are enzymes whose action is also located at the membrane interface. Native cell membranes are difficult to use to gain information on the activity of individual proteins at the membrane interface because of the large number of different proteins involved in membranous processes. Model membrane systems, such as monolayers at the air-water interface, have thus been extensively used during the last 50 years to reconstitute proteins and to gain information on their organization, structure and activity in membranes. In the present paper, we review the recent work we have performed with membrane and peripheral proteins as well as enzymes in monolayers at the air-water interface. We show that the structure and orientation of gramicidin has been determined by combining different methods. Furthermore, we demonstrate that the secondary structure of rhodopsin and bacteriorhodopsin is indistinguishable from that in native membranes when appropriate conditions are used. We also show that the kinetics and extent of monolayer binding of myristoylated recoverin is much faster than that of the nonmyristoylated form and that this binding is highly favored by the presence polyunsaturated phospholipids. Moreover, we show that the use of fragments of RPE65 allow determine which region of this protein is most likely involved in membrane binding. Monomolecular films were also used to further understand the hydrolysis of organized phospholipids by phospholipases A2 and C.},
doi = {10.1016/j.colsurfb.2007.03.019},
journal = {Colloids and Surfaces B: Biointerfaces},
number = 2,
volume = 58,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}