scholarly journals Kinetics of Membrane Protein–Detergent Interactions Depend on Protein Electrostatics

2018 ◽  
Vol 122 (41) ◽  
pp. 9471-9481 ◽  
Author(s):  
Aaron J. Wolfe ◽  
Jack F. Gugel ◽  
Min Chen ◽  
Liviu Movileanu
Keyword(s):  
Membrane Protein ◽  
Protein Electrostatics ◽  
Kinetics Of ◽  
Detergent Interactions

scholarly journals Energetics and Kinetics of Membrane Protein-Detergent Interactions

2019 ◽  
Vol 116 (3) ◽  
pp. 513a
Author(s):  
Aaron Wolfe ◽  
Liviu Movileanu
Keyword(s):  
Membrane Protein ◽  
Kinetics Of ◽  
Detergent Interactions

Simulation studies of the interactions between membrane proteins and detergents

2005 ◽  
Vol 33 (5) ◽  
pp. 910-912 ◽  
Author(s):  
P.J. Bond ◽  
J. Cuthbertson ◽  
M.S.P. Sansom
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Self Assembly ◽  
Kinetic Mechanism ◽  
Coarse Grained ◽  
Simulation Studies ◽  
High Resolution Data ◽  
Biologically Relevant ◽  
Structure And Dynamics ◽  
Detergent Interactions

Interactions between membrane proteins and detergents are important in biophysical and structural studies and are also biologically relevant in the context of folding and transport. Despite a paucity of high-resolution data on protein–detergent interactions, novel methods and increased computational power enable simulations to provide a means of understanding such interactions in detail. Simulations have been used to compare the effect of lipid or detergent on the structure and dynamics of membrane proteins. Moreover, some of the longest and most complex simulations to date have been used to observe the spontaneous formation of membrane protein–detergent micelles. Common mechanistic steps in the micelle self-assembly process were identified for both α-helical and β-barrel membrane proteins, and a simple kinetic mechanism was proposed. Recently, simplified (i.e. coarse-grained) models have been utilized to follow long timescale transitions in membrane protein–detergent assemblies.

Comparison between Ca2+-induced scrambling of various fluorescently labelled lipid analogues in red blood cells

2002 ◽  
Vol 362 (3) ◽  
pp. 741-747 ◽  
Author(s):  
David W. C. DEKKERS ◽  
Paul COMFURIUS ◽  
Edouard M. BEVERS ◽  
Robert F. A. ZWAAL
Keyword(s):  
Plasma Membrane ◽  
Membrane Protein ◽  
Red Blood Cells ◽  
Phospholipase D ◽  
Blood Cells ◽  
Amino Group ◽  
Flip Flop ◽  
Putative Membrane Protein ◽  
Kinetics Of

Treatment of red blood cells with calcium and ionomycin causes activation of the lipid scramblase, a putative membrane protein catalysing flip-flop of (phospho)lipids. Various fluorescent 1-oleoyl-2-[6(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino] caproyl (C6-NBD) analogues were tested for transbilayer movement across the plasma membrane of red blood cells. Among these phospholipid analogues were phosphatidylgalactose, phosphatidylmaltose and phosphatidylmaltotriose, which were obtained from C6-NBD-phosphatidylcholine by phospholipase D-catalysed transphosphatidylation. The inward movement after the onset of scrambling was monitored by extraction of the non-internalized probe with BSA. We demonstrate that both the amino group and the size of the headgroup determine the kinetics of lipid scrambling, and that lipids with a ceramide backbone migrate much more slowly than glycerophospholipids with the same headgroup.

scholarly journals A growth arrest-specific (gas) gene codes for a membrane protein.

1990 ◽  
Vol 10 (6) ◽  
pp. 2924-2930 ◽  
Author(s):  
G Manfioletti ◽  
M E Ruaro ◽  
G Del Sal ◽  
L Philipson ◽  
C Schneider
Keyword(s):  
Nucleotide Sequence ◽  
Membrane Protein ◽  
Detailed Analysis ◽  
Growth Arrest ◽  
Protein Product ◽  
In Vitro Translation ◽  
Transcriptional Level ◽  
Transmembrane Glycoprotein ◽  
Kinetics Of

A set of growth arrest-specific (gas) genes whose expression is negatively regulated by serum has recently been identified. We report on the detailed analysis of one of these genes (gas3). The kinetics of regulation by the presence and absence of serum were investigated, and it was found that this gene is regulated at the post-transcriptional level. The encoded protein deduced from the nucleotide sequence showed some similarity to a mitochondrial oxyreductase, and in vitro translation established that the protein product is a transmembrane glycoprotein.

scholarly journals Dynamic membrane topology in an unassembled membrane protein

2019 ◽  
Author(s):  
Maximilian Seurig ◽  
Moira Ek ◽  
Gunnar von Heijne ◽  
Nir Fluman
Keyword(s):  
Membrane Protein ◽  
Transmembrane Helix ◽  
Membrane Topology ◽  
Topological Dynamics ◽  
Membrane Insertion ◽  
Dynamic Membrane ◽  
Membrane Protein Topology ◽  
Small Multidrug Resistance ◽  
Kinetics Of

AbstractHelical membrane proteins constitute roughly a quarter of all proteomes and perform diverse biological functions. To avoid aggregation, they undergo cotranslational membrane insertion and are typically assumed to attain stable transmembrane topologies immediately upon insertion. To what extent post-translational changes in topology are possible in-vivo and how they may affect biogenesis is incompletely understood. Here, we show that monomeric forms of Small Multidrug Resistance (SMR) proteins display topological dynamics, where the N-terminal transmembrane helix equilibrates between membrane-inserted and non-inserted states. We characterize the kinetics of the process and show how the composition of the helix regulates the topological dynamics. We further show that topological dynamics is a property of the unassembled monomeric protein, as the N-terminal helix becomes fixed in a transmembrane disposition upon dimerization. Membrane protein topology can thus remain dynamic long after cotranslational membrane insertion, and can be regulated by later assembly processes.

scholarly journals Kinetics of the incorporation of cytochrome b 5 , an integral membrane protein, into unilamellar dimyristoyllecithin liposomes

FEBS Letters ◽  
1978 ◽  
Vol 87 (2) ◽  
pp. 269-272 ◽  
Author(s):  
Winchil L.C. Vaz ◽  
Horst Vogel ◽  
Fritz Jähnig ◽  
Robert H. Austin
Keyword(s):  
Membrane Protein ◽  
Cytochrome B ◽  
Integral Membrane Protein ◽  
Kinetics Of

scholarly journals The oligomerization reaction of the Semliki Forest virus membrane protein subunits.

1995 ◽  
Vol 128 (3) ◽  
pp. 283-291 ◽  
Author(s):  
B U Barth ◽  
J M Wahlberg ◽  
H Garoff
Keyword(s):  
Endoplasmic Reticulum ◽  
Membrane Protein ◽  
Semliki Forest Virus ◽  
Mrna Translation ◽  
Translation Product ◽  
Protein Subunits ◽  
Anchor Sequence ◽  
In Cis ◽  
Kinetics Of ◽  
Oligomerization Reaction

The Semliki Forest virus (SFV) spike is composed of three copies of a membrane protein heterodimer. The two subunits of this heterodimer (p62 and E1) are synthesized sequentially from a common mRNA together with the capsid (C) in the order C-p62-E1. In this work heterodimerization of the spike proteins has been studied in BHK 21 cells. The results indicate that: (a) the polyprotein is cotranslationally cleaved into individual chains; (b) the two membrane protein subunits are initially not associated with each other in the endoplasmic reticulum (ER); (c) heterodimerization occurs predominantly between subunits that originate from the same translation product (heterodimerization in cis); (d) the kinetics of subunit association are very fast (t1/2 = 4 min); and (e) this heterodimerization is highly efficient. To explain the cis-directed heterodimerization reaction we suggest that the p62 protein, which is made before E1 during 26S mRNA translation, is retained at its translocation site until also the E1 chain has been synthesized and translocated at this same site. The mechanism for p62 retention could either be that the p62 anchor sequence cannot diffuse out from an "active" translocation site or that the p62 protein is complexed with a protein folding facilitating machinery that is physically linked to the translocation apparatus.

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