Non-covalent interactions across subunit interfaces in Sm proteins
Само за регистроване кориснике
2011
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
The distinguishing property of Sm protein associations is their high stability. In order to understand this property, we analyzed the interface non-covalent interactions and compared the properties of the Sm protein interfaces with those of a test set, Binding Interface Database (BID). The comparison revealed that the main differences between interfaces of Sm proteins and those of the BID set are the content of charged residues, hydrogen bonds, salt bridges, and conservation scores of interface residues. In Sm proteins, the interfaces have more hydrophobic and fewer charged residues than the surface, which is also the case for the BID test set and other proteins. However, in the interfaces, the content of charged residues in Sm proteins (26%) is substantially larger than that in the BID set (22%). Both interfaces of Sm proteins and of test set have a similar number of hydrophobic interactions per 100 angstrom(2). The interfaces of Sm proteins have substantially more hydrogen bonds than... the interfaces in test set. The results show clearly that the interfaces of Sm proteins form more salt bridges compared with test set. On average, there are about 16 salt bridges per interface. The high conservation score of amino acids that are involved in non-covalent interactions in protein interfaces is an additional strong argument for their importance. The overriding conclusion from this study is that the non-covalent interactions in Sm protein interfaces considerably contribute to stability of higher order structures.
Кључне речи:
Interface / Sm proteins / Hydrogen bonds / Hydrophobic interactions / Salt bridgesИзвор:
Journal of Theoretical Biology, 2011, 271, 1, 18-26Издавач:
- Academic Press Ltd- Elsevier Science Ltd, London
Финансирање / пројекти:
- Проучавање односа реактивности, нековалентних интеракција и структуре молекула и моделовање хемијских система (RS-MESTD-MPN2006-2010-142037)
- Испитивање структуре и функције биолошки важних макромолекула у физиолошким и патолошким стањима (RS-MESTD-MPN2006-2010-142020)
DOI: 10.1016/j.jtbi.2010.11.025
ISSN: 0022-5193
PubMed: 21095194
WoS: 000286492100003
Scopus: 2-s2.0-78649761217
Институција/група
IHTMTY - JOUR AU - Zarić, Božidarka AU - Jovanović, Vesna B. AU - Stojanović, Srđan PY - 2011 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/924 AB - The distinguishing property of Sm protein associations is their high stability. In order to understand this property, we analyzed the interface non-covalent interactions and compared the properties of the Sm protein interfaces with those of a test set, Binding Interface Database (BID). The comparison revealed that the main differences between interfaces of Sm proteins and those of the BID set are the content of charged residues, hydrogen bonds, salt bridges, and conservation scores of interface residues. In Sm proteins, the interfaces have more hydrophobic and fewer charged residues than the surface, which is also the case for the BID test set and other proteins. However, in the interfaces, the content of charged residues in Sm proteins (26%) is substantially larger than that in the BID set (22%). Both interfaces of Sm proteins and of test set have a similar number of hydrophobic interactions per 100 angstrom(2). The interfaces of Sm proteins have substantially more hydrogen bonds than the interfaces in test set. The results show clearly that the interfaces of Sm proteins form more salt bridges compared with test set. On average, there are about 16 salt bridges per interface. The high conservation score of amino acids that are involved in non-covalent interactions in protein interfaces is an additional strong argument for their importance. The overriding conclusion from this study is that the non-covalent interactions in Sm protein interfaces considerably contribute to stability of higher order structures. PB - Academic Press Ltd- Elsevier Science Ltd, London T2 - Journal of Theoretical Biology T1 - Non-covalent interactions across subunit interfaces in Sm proteins VL - 271 IS - 1 SP - 18 EP - 26 DO - 10.1016/j.jtbi.2010.11.025 ER -
@article{ author = "Zarić, Božidarka and Jovanović, Vesna B. and Stojanović, Srđan", year = "2011", abstract = "The distinguishing property of Sm protein associations is their high stability. In order to understand this property, we analyzed the interface non-covalent interactions and compared the properties of the Sm protein interfaces with those of a test set, Binding Interface Database (BID). The comparison revealed that the main differences between interfaces of Sm proteins and those of the BID set are the content of charged residues, hydrogen bonds, salt bridges, and conservation scores of interface residues. In Sm proteins, the interfaces have more hydrophobic and fewer charged residues than the surface, which is also the case for the BID test set and other proteins. However, in the interfaces, the content of charged residues in Sm proteins (26%) is substantially larger than that in the BID set (22%). Both interfaces of Sm proteins and of test set have a similar number of hydrophobic interactions per 100 angstrom(2). The interfaces of Sm proteins have substantially more hydrogen bonds than the interfaces in test set. The results show clearly that the interfaces of Sm proteins form more salt bridges compared with test set. On average, there are about 16 salt bridges per interface. The high conservation score of amino acids that are involved in non-covalent interactions in protein interfaces is an additional strong argument for their importance. The overriding conclusion from this study is that the non-covalent interactions in Sm protein interfaces considerably contribute to stability of higher order structures.", publisher = "Academic Press Ltd- Elsevier Science Ltd, London", journal = "Journal of Theoretical Biology", title = "Non-covalent interactions across subunit interfaces in Sm proteins", volume = "271", number = "1", pages = "18-26", doi = "10.1016/j.jtbi.2010.11.025" }
Zarić, B., Jovanović, V. B.,& Stojanović, S.. (2011). Non-covalent interactions across subunit interfaces in Sm proteins. in Journal of Theoretical Biology Academic Press Ltd- Elsevier Science Ltd, London., 271(1), 18-26. https://doi.org/10.1016/j.jtbi.2010.11.025
Zarić B, Jovanović VB, Stojanović S. Non-covalent interactions across subunit interfaces in Sm proteins. in Journal of Theoretical Biology. 2011;271(1):18-26. doi:10.1016/j.jtbi.2010.11.025 .
Zarić, Božidarka, Jovanović, Vesna B., Stojanović, Srđan, "Non-covalent interactions across subunit interfaces in Sm proteins" in Journal of Theoretical Biology, 271, no. 1 (2011):18-26, https://doi.org/10.1016/j.jtbi.2010.11.025 . .