Contribution of cation-pi interactions to the stability of Sm/LSm oligomeric assemblies
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2015
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In this work, we have analyzed the influence of cation-pi interactions to the stability of Sm/LSm assemblies and their environmental preferences. The number of interactions formed by arginine is higher than lysine in the cationic group, while histidine is comparatively higher than phenylalanine and tyrosine in the pi group. Arg-Tyr interactions are predominant among the various pairs analyzed. The furcation level of multiple cation-pi interactions is much higher than that of single cation-pi interactions in Sm/LSm interfaces. We have found hot spot residues forming cation-pi interactions, and hot spot composition is similar for all aromatic residues. The Arg-Phe pair has the strongest interaction energy of -8.81 kcal mol(-1) among all the possible pairs of amino acids. The extent of burial of the residue side-chain correlates with the Delta Delta G of binding for residues in the core and also for hot spot residues cation-pi bonded across the interface. Secondary structure of the cation...-pi residues shows that Arg and Lys preferred to be in strand. Among the pi residues, His prefers to be in helix, Phe prefers to be in turn, and Tyr prefers to be in strand. Stabilization centers for these proteins showed that all the five residues found in cation-pi interactions are important in locating one or more of such centers. More than 50 % of the cation-pi interacting residues are highly conserved. It is likely that the cation-pi interactions contribute significantly to the overall stability of Sm/LSm proteins.
Ključne reči:
Cation-pi interactions / Sm/LSm proteins / Interfaces / Stabilization centers / Binding free energyIzvor:
Protoplasma, 2015, 252, 4, 947-958Izdavač:
- Springer Wien, Wien
Finansiranje / projekti:
- Proučavanje fizičkohemijskih i biohemijskih procesa u životnoj sredini koji utiču na zagađenje i istraživanje mogućnosti za minimiziranje posledica (RS-MESTD-Basic Research (BR or ON)-172001)
- Racionalni dizajn i sinteza biološki aktivnih i koordinacionih jedinjenja i funkcionalnih materijala, relevantnih u (bio)nanotehnologiji (RS-MESTD-Basic Research (BR or ON)-172035)
DOI: 10.1007/s00709-014-0727-8
ISSN: 0033-183X
PubMed: 25408427
WoS: 000357469700003
Scopus: 2-s2.0-84943364810
Institucija/grupa
IHTMTY - JOUR AU - Mucic, Ivana D AU - Nikolić, Milan AU - Stojanović, Srđan PY - 2015 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/1630 AB - In this work, we have analyzed the influence of cation-pi interactions to the stability of Sm/LSm assemblies and their environmental preferences. The number of interactions formed by arginine is higher than lysine in the cationic group, while histidine is comparatively higher than phenylalanine and tyrosine in the pi group. Arg-Tyr interactions are predominant among the various pairs analyzed. The furcation level of multiple cation-pi interactions is much higher than that of single cation-pi interactions in Sm/LSm interfaces. We have found hot spot residues forming cation-pi interactions, and hot spot composition is similar for all aromatic residues. The Arg-Phe pair has the strongest interaction energy of -8.81 kcal mol(-1) among all the possible pairs of amino acids. The extent of burial of the residue side-chain correlates with the Delta Delta G of binding for residues in the core and also for hot spot residues cation-pi bonded across the interface. Secondary structure of the cation-pi residues shows that Arg and Lys preferred to be in strand. Among the pi residues, His prefers to be in helix, Phe prefers to be in turn, and Tyr prefers to be in strand. Stabilization centers for these proteins showed that all the five residues found in cation-pi interactions are important in locating one or more of such centers. More than 50 % of the cation-pi interacting residues are highly conserved. It is likely that the cation-pi interactions contribute significantly to the overall stability of Sm/LSm proteins. PB - Springer Wien, Wien T2 - Protoplasma T1 - Contribution of cation-pi interactions to the stability of Sm/LSm oligomeric assemblies VL - 252 IS - 4 SP - 947 EP - 958 DO - 10.1007/s00709-014-0727-8 ER -
@article{ author = "Mucic, Ivana D and Nikolić, Milan and Stojanović, Srđan", year = "2015", abstract = "In this work, we have analyzed the influence of cation-pi interactions to the stability of Sm/LSm assemblies and their environmental preferences. The number of interactions formed by arginine is higher than lysine in the cationic group, while histidine is comparatively higher than phenylalanine and tyrosine in the pi group. Arg-Tyr interactions are predominant among the various pairs analyzed. The furcation level of multiple cation-pi interactions is much higher than that of single cation-pi interactions in Sm/LSm interfaces. We have found hot spot residues forming cation-pi interactions, and hot spot composition is similar for all aromatic residues. The Arg-Phe pair has the strongest interaction energy of -8.81 kcal mol(-1) among all the possible pairs of amino acids. The extent of burial of the residue side-chain correlates with the Delta Delta G of binding for residues in the core and also for hot spot residues cation-pi bonded across the interface. Secondary structure of the cation-pi residues shows that Arg and Lys preferred to be in strand. Among the pi residues, His prefers to be in helix, Phe prefers to be in turn, and Tyr prefers to be in strand. Stabilization centers for these proteins showed that all the five residues found in cation-pi interactions are important in locating one or more of such centers. More than 50 % of the cation-pi interacting residues are highly conserved. It is likely that the cation-pi interactions contribute significantly to the overall stability of Sm/LSm proteins.", publisher = "Springer Wien, Wien", journal = "Protoplasma", title = "Contribution of cation-pi interactions to the stability of Sm/LSm oligomeric assemblies", volume = "252", number = "4", pages = "947-958", doi = "10.1007/s00709-014-0727-8" }
Mucic, I. D., Nikolić, M.,& Stojanović, S.. (2015). Contribution of cation-pi interactions to the stability of Sm/LSm oligomeric assemblies. in Protoplasma Springer Wien, Wien., 252(4), 947-958. https://doi.org/10.1007/s00709-014-0727-8
Mucic ID, Nikolić M, Stojanović S. Contribution of cation-pi interactions to the stability of Sm/LSm oligomeric assemblies. in Protoplasma. 2015;252(4):947-958. doi:10.1007/s00709-014-0727-8 .
Mucic, Ivana D, Nikolić, Milan, Stojanović, Srđan, "Contribution of cation-pi interactions to the stability of Sm/LSm oligomeric assemblies" in Protoplasma, 252, no. 4 (2015):947-958, https://doi.org/10.1007/s00709-014-0727-8 . .