C-H/O Interactions of Aromatic CH Donors within Proteins: A Crystallographic Study
Само за регистроване кориснике
2016
Аутори
Dragelj, Jovan Lj.Stanković, Ivana M.
Božinovski, Dragana M.
Meyer, Tim
Veljković, Dušan Ž.
Medaković, Vesna
Knapp, Ernst-Walter
Zarić, Snežana D.
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
C-H/O interactions of aromatic C-H donors within proteins have been studied by analyzing the data in the Protein Data Bank (PDB). The C-H/O interactions were studied between aromatic donors; phenylalanine, tyrosine, and tryptophan and the acceptors; alcohol, backbone amide, and side-chain amide groups. The analysis of the C-H-O angle indicates that protein C-H donors do not show a preference for linear contacts. Although there is no tendency for linear C-H/O interactions, there are only around 3% of bifurcated C-H/O interactions. Furthermore, the analyses of the C-H/O interactions indicate an influence of simultaneous classical hydrogen bonds, especially for the tyrosine systems. The calculated electrostatic potential maps for model systems can explain the results of the crystallographic analysis. These results can be important for recognizing the C-H/O interaction of aromatic rings in the crystal structures of proteic systems.
Извор:
Crystal Growth and Design, 2016, 16, 4, 1948-1957Издавач:
- Amer Chemical Soc, Washington
Финансирање / пројекти:
- Нековалентне интеракције pi-система и њихова улога у молекулском препознавању (RS-MESTD-Basic Research (BR or ON)-172065)
- DAAD
Напомена:
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3393
DOI: 10.1021/acs.cgd.5b01543
ISSN: 1528-7483
WoS: 000373747700022
Scopus: 2-s2.0-84964663599
Колекције
Институција/група
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Dragelj, Jovan Lj. AU - Stanković, Ivana M. AU - Božinovski, Dragana M. AU - Meyer, Tim AU - Veljković, Dušan Ž. AU - Medaković, Vesna AU - Knapp, Ernst-Walter AU - Zarić, Snežana D. PY - 2016 UR - https://cherry.chem.bg.ac.rs/handle/123456789/1910 AB - C-H/O interactions of aromatic C-H donors within proteins have been studied by analyzing the data in the Protein Data Bank (PDB). The C-H/O interactions were studied between aromatic donors; phenylalanine, tyrosine, and tryptophan and the acceptors; alcohol, backbone amide, and side-chain amide groups. The analysis of the C-H-O angle indicates that protein C-H donors do not show a preference for linear contacts. Although there is no tendency for linear C-H/O interactions, there are only around 3% of bifurcated C-H/O interactions. Furthermore, the analyses of the C-H/O interactions indicate an influence of simultaneous classical hydrogen bonds, especially for the tyrosine systems. The calculated electrostatic potential maps for model systems can explain the results of the crystallographic analysis. These results can be important for recognizing the C-H/O interaction of aromatic rings in the crystal structures of proteic systems. PB - Amer Chemical Soc, Washington T2 - Crystal Growth and Design T1 - C-H/O Interactions of Aromatic CH Donors within Proteins: A Crystallographic Study VL - 16 IS - 4 SP - 1948 EP - 1957 DO - 10.1021/acs.cgd.5b01543 ER -
@article{ author = "Dragelj, Jovan Lj. and Stanković, Ivana M. and Božinovski, Dragana M. and Meyer, Tim and Veljković, Dušan Ž. and Medaković, Vesna and Knapp, Ernst-Walter and Zarić, Snežana D.", year = "2016", abstract = "C-H/O interactions of aromatic C-H donors within proteins have been studied by analyzing the data in the Protein Data Bank (PDB). The C-H/O interactions were studied between aromatic donors; phenylalanine, tyrosine, and tryptophan and the acceptors; alcohol, backbone amide, and side-chain amide groups. The analysis of the C-H-O angle indicates that protein C-H donors do not show a preference for linear contacts. Although there is no tendency for linear C-H/O interactions, there are only around 3% of bifurcated C-H/O interactions. Furthermore, the analyses of the C-H/O interactions indicate an influence of simultaneous classical hydrogen bonds, especially for the tyrosine systems. The calculated electrostatic potential maps for model systems can explain the results of the crystallographic analysis. These results can be important for recognizing the C-H/O interaction of aromatic rings in the crystal structures of proteic systems.", publisher = "Amer Chemical Soc, Washington", journal = "Crystal Growth and Design", title = "C-H/O Interactions of Aromatic CH Donors within Proteins: A Crystallographic Study", volume = "16", number = "4", pages = "1948-1957", doi = "10.1021/acs.cgd.5b01543" }
Dragelj, J. Lj., Stanković, I. M., Božinovski, D. M., Meyer, T., Veljković, D. Ž., Medaković, V., Knapp, E.,& Zarić, S. D.. (2016). C-H/O Interactions of Aromatic CH Donors within Proteins: A Crystallographic Study. in Crystal Growth and Design Amer Chemical Soc, Washington., 16(4), 1948-1957. https://doi.org/10.1021/acs.cgd.5b01543
Dragelj JL, Stanković IM, Božinovski DM, Meyer T, Veljković DŽ, Medaković V, Knapp E, Zarić SD. C-H/O Interactions of Aromatic CH Donors within Proteins: A Crystallographic Study. in Crystal Growth and Design. 2016;16(4):1948-1957. doi:10.1021/acs.cgd.5b01543 .
Dragelj, Jovan Lj., Stanković, Ivana M., Božinovski, Dragana M., Meyer, Tim, Veljković, Dušan Ž., Medaković, Vesna, Knapp, Ernst-Walter, Zarić, Snežana D., "C-H/O Interactions of Aromatic CH Donors within Proteins: A Crystallographic Study" in Crystal Growth and Design, 16, no. 4 (2016):1948-1957, https://doi.org/10.1021/acs.cgd.5b01543 . .