scholarly journals Author Correction: Identifying ionic interactions within a membrane using BLaTM, a genetic tool to measure homo- and heterotypic transmembrane helix-helix interactions

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Christoph Schanzenbach ◽  
Fabian C. Schmidt ◽  
Patrick Breckner ◽  
Mark G. Teese ◽  
Dieter Langosch
Keyword(s):  
Transmembrane Helix ◽  
Ionic Interactions ◽  
Genetic Tool ◽  
Helix Interactions

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

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.

scholarly journals NMR-based approach to measure the free energy of transmembrane helix–helix interactions

2014 ◽  
Vol 1838 (1) ◽  
pp. 164-172 ◽  
Author(s):  
Konstantin S. Mineev ◽  
Dmitry M. Lesovoy ◽  
Dinara R. Usmanova ◽  
Sergey A. Goncharuk ◽  
Mikhail A. Shulepko ◽  
...  
Keyword(s):  
Free Energy ◽  
Transmembrane Helix ◽  
Helix Interactions

scholarly journals The Affinity of GXXXG Motifs in Transmembrane Helix-Helix Interactions Is Modulated by Long-range Communication

2004 ◽  
Vol 279 (16) ◽  
pp. 16591-16597 ◽  
Author(s):  
Roman A. Melnyk ◽  
Sanguk Kim ◽  
A. Rachael Curran ◽  
Donald M. Engelman ◽  
James U. Bowie ◽  
...  
Keyword(s):  
Long Range ◽  
Transmembrane Helix ◽  
Long Range Communication ◽  
Helix Interactions

scholarly journals Mapping the Energy Surface of Transmembrane Helix-Helix Interactions

2001 ◽  
Vol 81 (5) ◽  
pp. 2681-2692 ◽  
Author(s):  
Jaume Torres ◽  
Andreas Kukol ◽  
Isaiah T. Arkin
Keyword(s):  
Energy Surface ◽  
Transmembrane Helix ◽  
Helix Interactions

scholarly journals Solid-State NMR Investigations of Transmembrane Helix Interactions

2017 ◽  
Vol 112 (3) ◽  
pp. 528a
Author(s):  
Kelsey Knobbe ◽  
Venkatesan Rajagopalan ◽  
Ashley Martfeld ◽  
Denise Greathouse ◽  
Roger Koeppe
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Transmembrane Helix ◽  
Helix Interactions

Transmembrane Helix−Helix Interactions:  Comparative Simulations of the Glycophorin A Dimer†

Biochemistry ◽  
2006 ◽  
Vol 45 (48) ◽  
pp. 14298-14310 ◽  
Author(s):  
Jonathan M. Cuthbertson ◽  
Peter J. Bond ◽  
Mark S. P. Sansom
Keyword(s):  
Transmembrane Helix ◽  
Glycophorin A ◽  
Helix Interactions

A mutational study of transmembrane helix–helix interactions

Biochimie ◽  
2007 ◽  
Vol 89 (11) ◽  
pp. 1433-1437 ◽  
Author(s):  
Alexander Prodöhl ◽  
Mathias Weber ◽  
Carolin Dreher ◽  
Dirk Schneider
Keyword(s):  
Transmembrane Helix ◽  
Mutational Study ◽  
Helix Interactions
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