scholarly journals 1P105 Measurement of thermodynamic parameters for self-association of a transmembrane helix in lipid bilayers containing cholesterol(Membrane proteins,Oral Presentations)

2007 ◽  
Vol 47 (supplement) ◽  
pp. S49
Author(s):  
Arisa Yamamoto ◽  
Yoshiaki Yano ◽  
Katsumi Matsuzaki
Keyword(s):  
Membrane Proteins ◽  
Thermodynamic Parameters ◽  
Lipid Bilayers ◽  
Transmembrane Helix ◽  
Self Association ◽  
Oral Presentations

Topological Stability and Self-Association of a Completely Hydrophobic Model Transmembrane Helix in Lipid Bilayers†

Biochemistry ◽  
2002 ◽  
Vol 41 (9) ◽  
pp. 3073-3080 ◽  
Author(s):  
Yoshiaki Yano ◽  
Tomokazu Takemoto ◽  
Satoe Kobayashi ◽  
Hiroyuki Yasui ◽  
Hiromu Sakurai ◽  
...  
Keyword(s):  
Lipid Bilayers ◽  
Transmembrane Helix ◽  
Topological Stability ◽  
Self Association

scholarly journals Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy

2020 ◽  
Author(s):  
Evan S. O’Brien ◽  
Brian Fuglestad ◽  
Henry J. Lessen ◽  
Matthew A. Stetz ◽  
Danny W. Lin ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Lipid Bilayers ◽  
Transmembrane Helix ◽  
Water Soluble ◽  
Side Chain ◽  
Side Chains ◽  
Amino Acid Side Chain ◽  
Relaxation Techniques ◽  
Conformational Entropy ◽  
Large Reservoir

AbstractFor a variety of reasons, the internal motions of integral membrane proteins have largely eluded comprehensive experiential characterization. Here, the fast side chain dynamics of the 7-transmembrane helix protein sensory rhodopsin II and the beta-barrel bacterial outer membrane channel protein W have been characterized in lipid bilayers and detergent micelles by solution NMR relaxation techniques. Though of quite different topologies, both proteins are found to have a similar and striking distribution of methyl-bearing amino acid side chain motion that is independent of membrane mimetic. The methyl-bearing side chains of both proteins, on average, are more dynamic in the ps-ns time regime than any soluble protein characterized to date. Approximately one third of methyl-bearing side chains exhibit extreme rotameric averaging on this timescale. Accordingly, both proteins retain an extraordinary residual conformational entropy in the folded state, which provides a counterbalance to the absence of the hydrophobic effect that normally stabilizes the folded state of water-soluble proteins. Furthermore, the large reservoir of conformational entropy that is observed provides the potential to greatly influence the thermodynamics underlying a plethora of membrane protein functions including ligand binding, allostery and signaling.

scholarly journals Lipid Transporters Beam Signals from Cell Membranes

Membranes ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 562
Author(s):  
Miliça Ristovski ◽  
Danny Farhat ◽  
Shelly Ellaine M. Bancud ◽  
Jyh-Yeuan Lee
Keyword(s):  
Membrane Proteins ◽  
Lipid Bilayers ◽  
Lipid Composition ◽  
Structural Integrity ◽  
Current Knowledge ◽  
Integral Membrane Proteins ◽  
Cellular Membranes ◽  
Cytoplasmic Proteins ◽  
Lipid Transporters

Lipid composition in cellular membranes plays an important role in maintaining the structural integrity of cells and in regulating cellular signaling that controls functions of both membrane-anchored and cytoplasmic proteins. ATP-dependent ABC and P4-ATPase lipid transporters, two integral membrane proteins, are known to contribute to lipid translocation across the lipid bilayers on the cellular membranes. In this review, we will highlight current knowledge about the role of cholesterol and phospholipids of cellular membranes in regulating cell signaling and how lipid transporters participate this process.

Specificity and promiscuity in membrane helix interactions

1994 ◽  
Vol 27 (2) ◽  
pp. 157-218 ◽  
Author(s):  
Mark A. Lemmon ◽  
Donald M. Engelman
Keyword(s):  
Membrane Proteins ◽  
Transmembrane Helix ◽  
Integral Membrane Proteins ◽  
Lipid Packing ◽  
Membrane Protein Folding ◽  
Membrane Spanning ◽  
Α Helix ◽  
Prosthetic Groups ◽  
Packing Effects ◽  
Helix Interactions

The membrane-spanning portions of many integral membrane proteins consist of one or a number of transmembrane α-helices, which are expected to be independently stable on thermodynamic grounds. Side-by-side interactions between these transmembrane α-helices are important in the folding and assembly of such integral membrane proteins and their complexes. In considering the contribution of these helix–helix interactions to membrane protein folding and oligomerization, a distinction between the energetics and specificity should be recognized. A number of contributions to the energetics of transmembrane helix association within the lipid bilayer will be relatively non-specific, including those resulting from charge–charge interactions and lipid–packing effects. Specificity (and part of the energy) in transmembrane α-helix association, however, appears to rely mainly upon a detailed stereochemical fit between sets of dynamically accessible states of particular helices. In some cases, these interactions are mediated in part by prosthetic groups.

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