Modulating Transmembrane α-Helix Interactions through pH-Sensitive Boundary Residues

Biochemistry ◽  
2016 ◽  
Vol 55 (31) ◽  
pp. 4306-4315 ◽  
Author(s):  
Derek P. Ng ◽  
Charles M. Deber
Keyword(s):  
Ph Sensitive ◽  
Α Helix ◽  
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.

Transmembrane α-Helix Interactions are Required for the Functional Assembly of theEscherichia coliTol Complex

1995 ◽  
Vol 246 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Jean Claude Lazzaroni ◽  
Anne Vianney ◽  
Jean Luc Popot ◽  
Hélène Bénédetti ◽  
Fadel Samatey ◽  
...  
Keyword(s):  
Α Helix ◽  
Helix Interactions

scholarly journals Role of E270 in pH- and metal-sensitivities of firefly luciferases

2020 ◽  
Vol 19 (11) ◽  
pp. 1548-1558
Author(s):  
V. R. Viviani ◽  
G. F. Pelentir ◽  
G. Oliveira ◽  
A. Tomazini ◽  
V. R. Bevilaqua
Keyword(s):  
Active Site ◽  
Ph Sensitive ◽  
Ph Sensitivity ◽  
Decreasing Ph ◽  
Α Helix ◽  
Conserved Residue ◽  
Active Site Conformation

The substitutions of the conserved residue E270 at the N-terminal of α-helix 10 in pH-sensitive firefly luciferases stabilize a green emitting active site conformation, decreasing pH-sensitivity.

scholarly journals Modulating Transmembrane α-Helix Interactions through pH

2012 ◽  
Vol 102 (3) ◽  
pp. 490a
Author(s):  
Derek P. Ng ◽  
Charles M. Deber
Keyword(s):  
Α Helix ◽  
Helix Interactions

A Mechanism for Reversibly Pausing a Self-Immolation Cascade in Response to pH Changes

2019 ◽  
Author(s):  
Derrick Roberts ◽  
Ben S. Pilgrim ◽  
Tristan Dell ◽  
Molly Stevens
Keyword(s):  
Local Environment ◽  
Chemical Signals ◽  
Ph Sensitive ◽  
First Report ◽  
Ph Changes ◽  
Self Immolation

We describe the first report of a self-immolation cascade that can be reversibly paused and reactivated in response to pH changes. This system employs a triazole-based self-immolative linker, which expresses a pH-sensitive intermediate during its elimination sequence. This allows the system to respond to pH cues within its local environment, thus establishing a new way to gate self-immolative release using fluctuating or transient chemical signals.<br>

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