scholarly journals 1P104 Design of a soluble transmembrane helix for measurement of water-membrane partitioning(Membrane proteins,Oral Presentations)

2007 ◽  
Vol 47 (supplement) ◽  
pp. S49
Author(s):  
Norie Shimai ◽  
Yoshiaki Yano ◽  
Katsumi Matsuzaki
1994 ◽  
Vol 27 (2) ◽  
pp. 157-218 ◽  
Author(s):  
Mark A. Lemmon ◽  
Donald M. Engelman

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.


2011 ◽  
Vol 09 (supp01) ◽  
pp. 37-50 ◽  
Author(s):  
YUTAKA UENO ◽  
KAZUNORI KAWASAKI ◽  
OSAMU SAITO ◽  
MASAFUMI ARAI ◽  
MAKIKO SUWA

Structure prediction of membrane proteins could be constrained and thereby improved by introducing data of the observed molecular shape. We studied a coarse-grained molecular model that relied on residue-based dummy atoms to fold the transmembrane helices of a protein in the observed molecular shape. Based on the inter-residue potential, the α-helices were folded to contact each other in a simulated annealing protocol to search optimized conformation. Fitting the model into a three-dimensional volume was tested for proteins with known structures and resulted in a fairly reasonable arrangement of helices. In addition, the constraint to the packing transmembrane helix with the two-dimensional region was tested and found to work as a very similar folding guide. The obtained models nicely represented α-helices with the desired slight bend. Our structure prediction method for membrane proteins well demonstrated reasonable folding results using a low-resolution structural constraint introduced from recent cell-surface imaging techniques.


2007 ◽  
Vol 47 (supplement) ◽  
pp. S52
Author(s):  
Motoyuki Hattori ◽  
Yoshiki Tanaka ◽  
Shuya Fukai ◽  
Ryuichiro Ishitani ◽  
Osamu Nureki

2009 ◽  
Vol 96 (3) ◽  
pp. 336a
Author(s):  
Yoshiaki Yano ◽  
Norie Shimai ◽  
Katsumi Matsuzaki

2007 ◽  
Vol 47 (supplement) ◽  
pp. S51
Author(s):  
Satoko Amano ◽  
Masakazu Moriyama ◽  
Yumiko Nakashima ◽  
Kyoko Shinzawa-Itoh ◽  
Christoph Gerle ◽  
...  

1999 ◽  
Vol 77 (3) ◽  
pp. 1609-1618 ◽  
Author(s):  
Maryam M. Javadpour ◽  
Markus Eilers ◽  
Michel Groesbeek ◽  
Steven O. Smith

2021 ◽  
pp. 166909
Author(s):  
Benjamin C. McIlwain ◽  
Amanda L. Erwin ◽  
Alexander R. Davis ◽  
B. Ben Koff ◽  
Louise Chang ◽  
...  

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