Anion-pi interactions in protein-porphyrin complexes
Апстракт
In this work, we have analyzed the influence of anion-pi interactions on the stability of high resolution protein-porphyrin complex crystal structures. The anion-pi interactions are distance and orientation dependent. Results of ab initio calculations of stabilization energies showed that they lie mostly in the range from -2 to -4 kcal mol(-1) with some of the anion-pi interactions having stabilization energies of up to -16 kcal mol(-1). In the anionic group, the numbers of anion-pi interactions involving Asp and Glu are similar, while His is more often involved in these interactions than other aromatic residues. Furthermore, our study showed that in the dataset used about 70% of the investigated anion-pi interactions are in fact multiple anion-pi interactions. Our results suggest that interacting residues are predominantly located in buried and partially buried regions. The secondary structure of the anion-pi interaction involving residues shows that most of the interacting residues p...referred to be in helix conformations. Significant numbers of aromatic residues involved in anion-pi interactions have one or more stabilization centers, providing additional stability to the protein-porphyrin complexes. The conservation patterns indicate that more than half of the residues involved in these interactions are evolutionarily conserved, indicating that the contribution of the anion-pi interaction is an important factor for the structural stability of the investigated protein-porphyrin complexes.
Извор:
RSC Advances, 2015, 5, 48, 38361-38372Издавач:
- Royal Soc Chemistry, Cambridge
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)
- Синтеза аминохинолина и њихових деривата као антималарика и инхибитора ботулинум неуротоксина А (RS-MESTD-Basic Research (BR or ON)-172008)
DOI: 10.1039/c5ra03373j
ISSN: 2046-2069
WoS: 000353960800051
Scopus: 2-s2.0-84928914352
Институција/група
IHTMTY - JOUR AU - Zlatović, Mario AU - Borozan, Sunčica AU - Nikolić, Milan AU - Stojanović, Srđan PY - 2015 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/1811 AB - In this work, we have analyzed the influence of anion-pi interactions on the stability of high resolution protein-porphyrin complex crystal structures. The anion-pi interactions are distance and orientation dependent. Results of ab initio calculations of stabilization energies showed that they lie mostly in the range from -2 to -4 kcal mol(-1) with some of the anion-pi interactions having stabilization energies of up to -16 kcal mol(-1). In the anionic group, the numbers of anion-pi interactions involving Asp and Glu are similar, while His is more often involved in these interactions than other aromatic residues. Furthermore, our study showed that in the dataset used about 70% of the investigated anion-pi interactions are in fact multiple anion-pi interactions. Our results suggest that interacting residues are predominantly located in buried and partially buried regions. The secondary structure of the anion-pi interaction involving residues shows that most of the interacting residues preferred to be in helix conformations. Significant numbers of aromatic residues involved in anion-pi interactions have one or more stabilization centers, providing additional stability to the protein-porphyrin complexes. The conservation patterns indicate that more than half of the residues involved in these interactions are evolutionarily conserved, indicating that the contribution of the anion-pi interaction is an important factor for the structural stability of the investigated protein-porphyrin complexes. PB - Royal Soc Chemistry, Cambridge T2 - RSC Advances T1 - Anion-pi interactions in protein-porphyrin complexes VL - 5 IS - 48 SP - 38361 EP - 38372 DO - 10.1039/c5ra03373j ER -
@article{ author = "Zlatović, Mario and Borozan, Sunčica and Nikolić, Milan and Stojanović, Srđan", year = "2015", abstract = "In this work, we have analyzed the influence of anion-pi interactions on the stability of high resolution protein-porphyrin complex crystal structures. The anion-pi interactions are distance and orientation dependent. Results of ab initio calculations of stabilization energies showed that they lie mostly in the range from -2 to -4 kcal mol(-1) with some of the anion-pi interactions having stabilization energies of up to -16 kcal mol(-1). In the anionic group, the numbers of anion-pi interactions involving Asp and Glu are similar, while His is more often involved in these interactions than other aromatic residues. Furthermore, our study showed that in the dataset used about 70% of the investigated anion-pi interactions are in fact multiple anion-pi interactions. Our results suggest that interacting residues are predominantly located in buried and partially buried regions. The secondary structure of the anion-pi interaction involving residues shows that most of the interacting residues preferred to be in helix conformations. Significant numbers of aromatic residues involved in anion-pi interactions have one or more stabilization centers, providing additional stability to the protein-porphyrin complexes. The conservation patterns indicate that more than half of the residues involved in these interactions are evolutionarily conserved, indicating that the contribution of the anion-pi interaction is an important factor for the structural stability of the investigated protein-porphyrin complexes.", publisher = "Royal Soc Chemistry, Cambridge", journal = "RSC Advances", title = "Anion-pi interactions in protein-porphyrin complexes", volume = "5", number = "48", pages = "38361-38372", doi = "10.1039/c5ra03373j" }
Zlatović, M., Borozan, S., Nikolić, M.,& Stojanović, S.. (2015). Anion-pi interactions in protein-porphyrin complexes. in RSC Advances Royal Soc Chemistry, Cambridge., 5(48), 38361-38372. https://doi.org/10.1039/c5ra03373j
Zlatović M, Borozan S, Nikolić M, Stojanović S. Anion-pi interactions in protein-porphyrin complexes. in RSC Advances. 2015;5(48):38361-38372. doi:10.1039/c5ra03373j .
Zlatović, Mario, Borozan, Sunčica, Nikolić, Milan, Stojanović, Srđan, "Anion-pi interactions in protein-porphyrin complexes" in RSC Advances, 5, no. 48 (2015):38361-38372, https://doi.org/10.1039/c5ra03373j . .