caa a22 4500 605507333 CHVBK 20210128100631.0 cr unu---uuuuu 210128e20150401xx s 000 0 eng 10.1007/s00775-014-1227-1 doi (NATIONALLICENCE)springer-10.1007/s00775-014-1227-1 Contribution of anion- π interactions to the stability of Sm/LSm proteins [Elektronische Daten] [Luka Breberina, Miloš Milčić, Milan Nikolić, Srđan Stojanović] 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 −15kcalmol−1, and most of them have energy in the range −2 to −9kcalmol−1. 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: SBIC, 2014 Anion- π interactions nationallicence Sm/LSm proteins nationallicence Interfaces nationallicence Stabilization centers nationallicence Interaction energy nationallicence Breberina Luka Faculty of Chemistry, University of Belgrade, Belgrade, Serbia aut Milčić Miloš Faculty of Chemistry, University of Belgrade, Belgrade, Serbia aut Nikolić Milan Faculty of Chemistry, University of Belgrade, Belgrade, Serbia aut Stojanović Srđan Department of Chemistry, ICTM, University of Belgrade, Belgrade, Serbia aut JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/3(2015-04-01), 475-485 0949-8257 20:3<475 2015 20 775 https://doi.org/10.1007/s00775-014-1227-1 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00775-014-1227-1 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Breberina Luka Faculty of Chemistry, University of Belgrade, Belgrade, Serbia aut NATIONALLICENCE 700 1- Milčić Miloš Faculty of Chemistry, University of Belgrade, Belgrade, Serbia aut NATIONALLICENCE 700 1- Nikolić Milan Faculty of Chemistry, University of Belgrade, Belgrade, Serbia aut NATIONALLICENCE 700 1- Stojanović Srđan Department of Chemistry, ICTM, University of Belgrade, Belgrade, Serbia aut NATIONALLICENCE 773 0- JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/3(2015-04-01), 475-485 0949-8257 20:3<475 2015 20 775