scholarly journals Structure-based prediction of the stability of transmembrane helix-helix interactions: The sequence dependence of glycophorin A dimerization

1998 ◽  
Vol 95 (7) ◽  
pp. 3583-3590 ◽  
Author(s):  
K. R. MacKenzie ◽  
D. M. Engelman
Keyword(s):  
Transmembrane Helix ◽  
Glycophorin A ◽  
Sequence Dependence ◽  
The Stability ◽  
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

Modulation of glycophorin A transmembrane helix interactions by lipid bilayers: molecular dynamics calculations

2000 ◽  
Vol 302 (3) ◽  
pp. 727-746 ◽  
Author(s):  
Horia I Petrache ◽  
Alan Grossfield ◽  
Kevin R MacKenzie ◽  
Donald M Engelman ◽  
Thomas B Woolf
Keyword(s):  
Molecular Dynamics ◽  
Lipid Bilayers ◽  
Transmembrane Helix ◽  
Glycophorin A ◽  
Molecular Dynamics Calculations ◽  
Helix Interactions

scholarly journals Detergent Properties Influence the Stability of the Glycophorin A Transmembrane Helix Dimer in Lysophosphatidylcholine Micelles

2012 ◽  
Vol 103 (12) ◽  
pp. 2455-2464 ◽  
Author(s):  
Michael Stangl ◽  
Anbazhagan Veerappan ◽  
Anja Kroeger ◽  
Peter Vogel ◽  
Dirk Schneider
Keyword(s):  
Transmembrane Helix ◽  
Glycophorin A ◽  
The Stability

The Stability of Transmembrane Helix Interactions Measured in a Biological Membrane

2006 ◽  
Vol 358 (5) ◽  
pp. 1221-1228 ◽  
Author(s):  
Carmen Finger ◽  
Thomas Volkmer ◽  
Alexander Prodöhl ◽  
Daniel E. Otzen ◽  
Donald M. Engelman ◽  
...  
Keyword(s):  
Biological Membrane ◽  
Transmembrane Helix ◽  
The Stability ◽  
Helix Interactions

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.

Sequence Dependence of the Stability of RNA Hairpin Molecules with Six Nucleotide Loops†

Biochemistry ◽  
2006 ◽  
Vol 45 (5) ◽  
pp. 1400-1407 ◽  
Author(s):  
Christopher J. Vecenie ◽  
Catherine V. Morrow ◽  
Allison Zyra ◽  
Martin J. Serra
Keyword(s):  
Sequence Dependence ◽  
The Stability ◽  
Rna Hairpin

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
Sign in / Sign up

Export Citation Format

Share Document