Lipid Solvation Effects Contribute to the Affinity of Gly-xxx-Gly Motif-Mediated Helix−Helix Interactions†

Biochemistry ◽  
2006 ◽  
Vol 45 (28) ◽  
pp. 8507-8515 ◽  
Author(s):  
Rachel M. Johnson ◽  
Arianna Rath ◽  
Roman A. Melnyk ◽  
Charles M. Deber
Keyword(s):  
Solvation Effects ◽  
Helix Interactions

Interaction of heterocycles and nucleophiles. II. Sigma complexes formed from methoxide ion and Methoxy-3,5-dinitropyridines in dimethyl sulphoxide

1970 ◽  
Vol 23 (5) ◽  
pp. 957 ◽  
Author(s):  
MEC Biffin ◽  
J Miller ◽  
AG Moritz ◽  
DB Paul
Keyword(s):  
Dimethyl Sulphoxide ◽  
No Conversion ◽  
Solvation Effects ◽  
Sigma Complexes ◽  
Sigma Complex ◽  
Methoxide Ion ◽  
Rearrangement Reactions

Contrasting behaviour is observed when 2- and 4-methoxy-3,5-dinitropyridine interact with methoxide ion in dimethyl sulphoxide. The 4-methoxy compound affords both methine and acetal sigma complexes, the latter being thermodynamically more stable. The interconversion is catalysed by methanol. Labelling experiments have established that the sigma complex from the 2-methoxypyridine is formed by addition at C6; no conversion into the acetal could be effected. These observations are rationalized in terms of differential steric and solvation effects. Demethylation and rearrangement reactions of 4-methoxy-3,5-dinitropyridine are reported.

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.

Solvation effects and stabilization of multicharged ions: a case study of ArmBeOq+ complexes

2012 ◽  
Vol 14 (12) ◽  
pp. 4236 ◽  
Author(s):  
Roberto Linguerri ◽  
Najia Komiha ◽  
Majdi Hochlaf
Keyword(s):  
Solvation Effects

scholarly journals Assessing backbone solvation effects in the conformational propensities of amino acid residues in unfolded peptides

2015 ◽  
Vol 17 (38) ◽  
pp. 24917-24924 ◽  
Author(s):  
Niranjan V. Ilawe ◽  
Alexandra E. Raeber ◽  
Reinhard Schweitzer-Stenner ◽  
Siobhan E. Toal ◽  
Bryan M. Wong
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Solvation Effects ◽  
Self Energy ◽  
Polyproline Ii ◽  
Water Water Water

Large energetic contributions to the stabilization of polyproline II result from peptide–water, water–water interactions, and changes of the solvent self-energy.

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