Contribution of anion- π interactions to the stability of Sm/LSm proteins
| LEADER | caa a22 4500 | ||
|---|---|---|---|
| 001 | 605507333 | ||
| 003 | CHVBK | ||
| 005 | 20210128100631.0 | ||
| 007 | cr unu---uuuuu | ||
| 008 | 210128e20150401xx s 000 0 eng | ||
| 024 | 7 | 0 | |a 10.1007/s00775-014-1227-1 |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00775-014-1227-1 | ||
| 245 | 0 | 0 | |a Contribution of anion- π interactions to the stability of Sm/LSm proteins |h [Elektronische Daten] |c [Luka Breberina, Miloš Milčić, Milan Nikolić, Srđan Stojanović] |
| 520 | 3 | |a 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: | |
| 540 | |a SBIC, 2014 | ||
| 690 | 7 | |a Anion- π interactions |2 nationallicence | |
| 690 | 7 | |a Sm/LSm proteins |2 nationallicence | |
| 690 | 7 | |a Interfaces |2 nationallicence | |
| 690 | 7 | |a Stabilization centers |2 nationallicence | |
| 690 | 7 | |a Interaction energy |2 nationallicence | |
| 700 | 1 | |a Breberina |D Luka |u Faculty of Chemistry, University of Belgrade, Belgrade, Serbia |4 aut | |
| 700 | 1 | |a Milčić |D Miloš |u Faculty of Chemistry, University of Belgrade, Belgrade, Serbia |4 aut | |
| 700 | 1 | |a Nikolić |D Milan |u Faculty of Chemistry, University of Belgrade, Belgrade, Serbia |4 aut | |
| 700 | 1 | |a Stojanović |D Srđan |u Department of Chemistry, ICTM, University of Belgrade, Belgrade, Serbia |4 aut | |
| 773 | 0 | |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/3(2015-04-01), 475-485 |x 0949-8257 |q 20:3<475 |1 2015 |2 20 |o 775 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00775-014-1227-1 |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a research-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00775-014-1227-1 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Breberina |D Luka |u Faculty of Chemistry, University of Belgrade, Belgrade, Serbia |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Milčić |D Miloš |u Faculty of Chemistry, University of Belgrade, Belgrade, Serbia |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Nikolić |D Milan |u Faculty of Chemistry, University of Belgrade, Belgrade, Serbia |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Stojanović |D Srđan |u Department of Chemistry, ICTM, University of Belgrade, Belgrade, Serbia |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/3(2015-04-01), 475-485 |x 0949-8257 |q 20:3<475 |1 2015 |2 20 |o 775 | ||