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- Title
Contribution of anion- π interactions to the stability of Sm/LSm proteins.
- Authors
Breberina, Luka; Milčić, Miloš; Nikolić, Milan; Stojanović, Srđan
- Abstract
We have analyzed the influence of anion- π interactions to the stability of Sm/LSm assemblies. The side chain of Glu is more likely to be in anion- π interactions than Asp. Phe has the highest occurrence in these interactions than the other two π residues. Among the anion- π residue pairs, Glu-Phe residue pair showed the maximum number of anion- π. We have found hot-spot residues forming anion- π interactions, and Glu-Phe is the most common hot-spot interacting pair. The significant numbers of anion- π interacting residues identified in the dataset were involved in the formation of multiple anion- π interactions. More than half of the residues involved in these interactions are evolutionarily conserved. The anion- π interaction energies are distance and orientation dependent. It was found that anion- π interactions showed energy less than −15 kcal mol, and most of them have energy in the range −2 to −9 kcal mol. Solvent accessibility pattern of Sm/LSm proteins reveals that all of the interacting residues are preferred to be in buried regions. Most of the interacting residues preferred to be in strand. A significant percentage of anion- π interacting residues are located as stabilization centers and thus might provide additional stability to these proteins. The simultaneous interaction of anions and cations on different faces of the same π-system has been observed. On the whole, the results presented in this work will be very useful for understanding the contribution of anion- π interaction to the stability of Sm/LSm proteins. Graphical Abstract: [Figure not available: see fulltext.]
- Subjects
ANION analysis; CARRIER proteins; PROTEIN stability; PROTEIN-protein interactions; SUBSTITUENTS (Chemistry)
- Publication
Journal of Biological Inorganic Chemistry (JBIC), 2015, Vol 20, Issue 3, p475
- ISSN
0949-8257
- Publication type
Article
- DOI
10.1007/s00775-014-1227-1