Strong and weak hydrogen bonds in sm/lsm oligomeric assemblies: a comparison of intra- and interchain interaction
Само за регистроване кориснике
2013
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
The Sm and Sm-like (LSm) proteins are a widespread protein family with members in all kingdoms of life. Sm proteins form complexes engaging in various RNA-processing events. Sm proteins do form and act as oligomeric assemblies whose characteristic is their exceptional stability. This study compares strong and weak hydrogen bonds in the interior of monomers and at interfaces of Sm/LSm proteins in order to better understand the stability of oligomers. According to our results, the stability of oligomeric assemblies is achieved by CH center dot center dot center dot O, NH center dot center dot center dot O and CH center dot center dot center dot N interactions including, NH center dot center dot center dot N, OH center dot center dot center dot O, XH center dot center dot center dot pi interactions present in small percentages. Intrachain hydrogen bonds behave in respect to geometry, distances and angles, like interchain hydrogen bonds. It is also shown that amino acids Arg and Lys partic...ipate significantly as donors or acceptors in some of the strong or weak interactions at interfaces to a higher extent than in the monomers. There is a trend for most polar amino acids to cross into more solvent exposed position in interfaces, which is not the case for nonpolar or charged amino acids. There is no exclusive preference for particular secondary structure both for intrachains and for interfaces.
Кључне речи:
Sm/LSm proteins / Hydrogen bonds / Secondary structure preferences / Solvent accessibilityИзвор:
Digest Journal of Nanomaterials and Biostructures, 2013, 8, 2, 639-654Издавач:
- Inst Materials Physics, Bucharest
Финансирање / 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)
Институција/група
IHTMTY - JOUR AU - Zarić, Božidarka AU - Bukorović, Milica AU - Stojanović, Srđan PY - 2013 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/1210 AB - The Sm and Sm-like (LSm) proteins are a widespread protein family with members in all kingdoms of life. Sm proteins form complexes engaging in various RNA-processing events. Sm proteins do form and act as oligomeric assemblies whose characteristic is their exceptional stability. This study compares strong and weak hydrogen bonds in the interior of monomers and at interfaces of Sm/LSm proteins in order to better understand the stability of oligomers. According to our results, the stability of oligomeric assemblies is achieved by CH center dot center dot center dot O, NH center dot center dot center dot O and CH center dot center dot center dot N interactions including, NH center dot center dot center dot N, OH center dot center dot center dot O, XH center dot center dot center dot pi interactions present in small percentages. Intrachain hydrogen bonds behave in respect to geometry, distances and angles, like interchain hydrogen bonds. It is also shown that amino acids Arg and Lys participate significantly as donors or acceptors in some of the strong or weak interactions at interfaces to a higher extent than in the monomers. There is a trend for most polar amino acids to cross into more solvent exposed position in interfaces, which is not the case for nonpolar or charged amino acids. There is no exclusive preference for particular secondary structure both for intrachains and for interfaces. PB - Inst Materials Physics, Bucharest T2 - Digest Journal of Nanomaterials and Biostructures T1 - Strong and weak hydrogen bonds in sm/lsm oligomeric assemblies: a comparison of intra- and interchain interaction VL - 8 IS - 2 SP - 639 EP - 654 UR - https://hdl.handle.net/21.15107/rcub_cer_1210 ER -
@article{ author = "Zarić, Božidarka and Bukorović, Milica and Stojanović, Srđan", year = "2013", abstract = "The Sm and Sm-like (LSm) proteins are a widespread protein family with members in all kingdoms of life. Sm proteins form complexes engaging in various RNA-processing events. Sm proteins do form and act as oligomeric assemblies whose characteristic is their exceptional stability. This study compares strong and weak hydrogen bonds in the interior of monomers and at interfaces of Sm/LSm proteins in order to better understand the stability of oligomers. According to our results, the stability of oligomeric assemblies is achieved by CH center dot center dot center dot O, NH center dot center dot center dot O and CH center dot center dot center dot N interactions including, NH center dot center dot center dot N, OH center dot center dot center dot O, XH center dot center dot center dot pi interactions present in small percentages. Intrachain hydrogen bonds behave in respect to geometry, distances and angles, like interchain hydrogen bonds. It is also shown that amino acids Arg and Lys participate significantly as donors or acceptors in some of the strong or weak interactions at interfaces to a higher extent than in the monomers. There is a trend for most polar amino acids to cross into more solvent exposed position in interfaces, which is not the case for nonpolar or charged amino acids. There is no exclusive preference for particular secondary structure both for intrachains and for interfaces.", publisher = "Inst Materials Physics, Bucharest", journal = "Digest Journal of Nanomaterials and Biostructures", title = "Strong and weak hydrogen bonds in sm/lsm oligomeric assemblies: a comparison of intra- and interchain interaction", volume = "8", number = "2", pages = "639-654", url = "https://hdl.handle.net/21.15107/rcub_cer_1210" }
Zarić, B., Bukorović, M.,& Stojanović, S.. (2013). Strong and weak hydrogen bonds in sm/lsm oligomeric assemblies: a comparison of intra- and interchain interaction. in Digest Journal of Nanomaterials and Biostructures Inst Materials Physics, Bucharest., 8(2), 639-654. https://hdl.handle.net/21.15107/rcub_cer_1210
Zarić B, Bukorović M, Stojanović S. Strong and weak hydrogen bonds in sm/lsm oligomeric assemblies: a comparison of intra- and interchain interaction. in Digest Journal of Nanomaterials and Biostructures. 2013;8(2):639-654. https://hdl.handle.net/21.15107/rcub_cer_1210 .
Zarić, Božidarka, Bukorović, Milica, Stojanović, Srđan, "Strong and weak hydrogen bonds in sm/lsm oligomeric assemblies: a comparison of intra- and interchain interaction" in Digest Journal of Nanomaterials and Biostructures, 8, no. 2 (2013):639-654, https://hdl.handle.net/21.15107/rcub_cer_1210 .