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Contribution of Non-Canonical Interactions to the Stability of Sm/LSm Oligomeric Assemblies

Authorized Users Only
2011
Authors
Stojanović, Srđan
Isenovic, Esma R.
Zarić, Božidarka
Article (Published version)
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Abstract
The distinguishing property of Sm/LSm protein assemblies is their high stability. In order to better understand the nature of Sm/LSm protein oligomers in this study we have analyzed the contribution of non-canonical interactions to the stability of assemblies. The predominant types of non-canonical interactions at Sm/LSm protein interfaces are CH center dot center dot center dot O, and CH center dot center dot center dot N interactions represented at interfaces. Our results show low percentages of XH-pi and non-canonical interactions involving sulfur atoms, while the backbone groups were less frequently involved. The data show a high percentage of non-canonical interactions in interfaces formed by charged residues with Lys and Arg, these being the major charged donors. The main chain non-canonical interactions might be slightly more linear than the side chain interactions, and they have somewhat shorter median distances. Comparing the stabilizing amino acid residues with amino acids wh...ich build non-canonical interactions at interfaces shows that certain amino acids like Phe, Pro, His and Tyr are involved with a high percentage. The high conservation score of amino acids that are involved in non-canonical interactions in protein interfaces is an additional strong argument for their importance in the stabilization of Sm/LSm protein assemblies.

Keywords:
Computational chemistry / Interfaces / Noncovalent interactions / Proteins / Stabilization centers
Source:
Molecular Informatics, 2011, 30, 5, 430-442
Publisher:
  • Wiley-V C H Verlag Gmbh, Weinheim
Funding / projects:
  • The study of physicochemical and biochemical processes in living environment that have impacts on pollution and the investigation of possibilities for minimizing the consequences (RS-172001)
  • Hormonal regulation of expression and activity of the nitric oxide synthase and sodium-potassium pump in experimental models of insulin resistance, diabetes and cardiovascular disorders (RS-173033)

DOI: 10.1002/minf.201000176

ISSN: 1868-1743

PubMed: 27467089

WoS: 000291602600005

Scopus: 2-s2.0-79958792930
[ Google Scholar ]
5
3
URI
https://cer.ihtm.bg.ac.rs/handle/123456789/785
Collections
  • Radovi istraživača / Researchers' publications
Institution/Community
IHTM
TY  - JOUR
AU  - Stojanović, Srđan
AU  - Isenovic, Esma R.
AU  - Zarić, Božidarka
PY  - 2011
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/785
AB  - The distinguishing property of Sm/LSm protein assemblies is their high stability. In order to better understand the nature of Sm/LSm protein oligomers in this study we have analyzed the contribution of non-canonical interactions to the stability of assemblies. The predominant types of non-canonical interactions at Sm/LSm protein interfaces are CH center dot center dot center dot O, and CH center dot center dot center dot N interactions represented at interfaces. Our results show low percentages of XH-pi and non-canonical interactions involving sulfur atoms, while the backbone groups were less frequently involved. The data show a high percentage of non-canonical interactions in interfaces formed by charged residues with Lys and Arg, these being the major charged donors. The main chain non-canonical interactions might be slightly more linear than the side chain interactions, and they have somewhat shorter median distances. Comparing the stabilizing amino acid residues with amino acids which build non-canonical interactions at interfaces shows that certain amino acids like Phe, Pro, His and Tyr are involved with a high percentage. The high conservation score of amino acids that are involved in non-canonical interactions in protein interfaces is an additional strong argument for their importance in the stabilization of Sm/LSm protein assemblies.
PB  - Wiley-V C H Verlag Gmbh, Weinheim
T2  - Molecular Informatics
T1  - Contribution of Non-Canonical Interactions to the Stability of Sm/LSm Oligomeric Assemblies
VL  - 30
IS  - 5
SP  - 430
EP  - 442
DO  - 10.1002/minf.201000176
ER  - 
@article{
author = "Stojanović, Srđan and Isenovic, Esma R. and Zarić, Božidarka",
year = "2011",
abstract = "The distinguishing property of Sm/LSm protein assemblies is their high stability. In order to better understand the nature of Sm/LSm protein oligomers in this study we have analyzed the contribution of non-canonical interactions to the stability of assemblies. The predominant types of non-canonical interactions at Sm/LSm protein interfaces are CH center dot center dot center dot O, and CH center dot center dot center dot N interactions represented at interfaces. Our results show low percentages of XH-pi and non-canonical interactions involving sulfur atoms, while the backbone groups were less frequently involved. The data show a high percentage of non-canonical interactions in interfaces formed by charged residues with Lys and Arg, these being the major charged donors. The main chain non-canonical interactions might be slightly more linear than the side chain interactions, and they have somewhat shorter median distances. Comparing the stabilizing amino acid residues with amino acids which build non-canonical interactions at interfaces shows that certain amino acids like Phe, Pro, His and Tyr are involved with a high percentage. The high conservation score of amino acids that are involved in non-canonical interactions in protein interfaces is an additional strong argument for their importance in the stabilization of Sm/LSm protein assemblies.",
publisher = "Wiley-V C H Verlag Gmbh, Weinheim",
journal = "Molecular Informatics",
title = "Contribution of Non-Canonical Interactions to the Stability of Sm/LSm Oligomeric Assemblies",
volume = "30",
number = "5",
pages = "430-442",
doi = "10.1002/minf.201000176"
}
Stojanović, S., Isenovic, E. R.,& Zarić, B.. (2011). Contribution of Non-Canonical Interactions to the Stability of Sm/LSm Oligomeric Assemblies. in Molecular Informatics
Wiley-V C H Verlag Gmbh, Weinheim., 30(5), 430-442.
https://doi.org/10.1002/minf.201000176
Stojanović S, Isenovic ER, Zarić B. Contribution of Non-Canonical Interactions to the Stability of Sm/LSm Oligomeric Assemblies. in Molecular Informatics. 2011;30(5):430-442.
doi:10.1002/minf.201000176 .
Stojanović, Srđan, Isenovic, Esma R., Zarić, Božidarka, "Contribution of Non-Canonical Interactions to the Stability of Sm/LSm Oligomeric Assemblies" in Molecular Informatics, 30, no. 5 (2011):430-442,
https://doi.org/10.1002/minf.201000176 . .

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