Contribution of Non-Canonical Interactions to the Stability of Sm/LSm Oligomeric Assemblies
Апстракт
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.
Кључне речи:
Computational chemistry / Interfaces / Noncovalent interactions / Proteins / Stabilization centersИзвор:
Molecular Informatics, 2011, 30, 5, 430-442Финансирање / пројекти:
- Проучавање физичкохемијских и биохемијских процеса у животној средини који утичу на загађење и истраживање могућности за минимизирање последица (RS-MESTD-Basic Research (BR or ON)-172001)
- Хормонска регулација експресије и активности азот оксид синтазе и натријум-калијумове пумпе у експерименталним моделима инсулинске резистенције, дијабетеса и кардиоваскуларних поремећаја (RS-MESTD-Basic Research (BR or ON)-173033)
DOI: 10.1002/minf.201000176
ISSN: 1868-1743; 1868-1751
PubMed: 27467089
WoS: 000291602600005
Scopus: 2-s2.0-79958792930
Колекције
Институција/група
VinčaTY - JOUR AU - Stojanovic, Srdan D. AU - Isenović, Esma R. AU - Zarić, Božidarka PY - 2011 UR - https://vinar.vin.bg.ac.rs/handle/123456789/4381 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. 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 = "Stojanovic, Srdan D. and Isenović, 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.", 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" }
Stojanovic, S. D., Isenović, E. R.,& Zarić, B.. (2011). Contribution of Non-Canonical Interactions to the Stability of Sm/LSm Oligomeric Assemblies. in Molecular Informatics, 30(5), 430-442. https://doi.org/10.1002/minf.201000176
Stojanovic SD, Isenović 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 .
Stojanovic, Srdan D., Isenović, 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 . .