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.
Keywords:
Non-covalent interactions / Protein Data Bank (PDB) / C-H/O interactions / phenylalanine / tyrosine / tryptophan / alcohol / amide / electrostatic potential maps / aromatic rings
TY - JOUR
AU - Dragelj, Jovan Lj
AU - Stanković, Ivana
AU - Bozinovski, Dragana M
AU - Meyer, Tim
AU - Veljković, Dušan
AU - Medaković, Vesna
AU - Knapp, Ernst-Walter
AU - Zarić, Snežana D.
PY - 2016
UR - https://cer.ihtm.bg.ac.rs/handle/123456789/2035
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 - American Chemical Society (ACS)
T2 - Crystal Growth & 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 and Bozinovski, Dragana M and Meyer, Tim and Veljković, Dušan 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 = "American Chemical Society (ACS)",
journal = "Crystal Growth & 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. L., Stanković, I., Bozinovski, D. M., Meyer, T., Veljković, D., Medaković, V., Knapp, E.,& Zarić, S. D.. (2016). C-H/O Interactions of Aromatic CH Donors within Proteins: A Crystallographic Study. in Crystal Growth & Design
American Chemical Society (ACS)., 16(4), 1948-1957.
https://doi.org/10.1021/acs.cgd.5b01543
Dragelj JL, Stanković I, Bozinovski DM, Meyer T, Veljković D, Medaković V, Knapp E, Zarić SD. C-H/O Interactions of Aromatic CH Donors within Proteins: A Crystallographic Study. in Crystal Growth & Design. 2016;16(4):1948-1957.
doi:10.1021/acs.cgd.5b01543 .
Dragelj, Jovan Lj, Stanković, Ivana, Bozinovski, Dragana M, Meyer, Tim, Veljković, Dušan, Medaković, Vesna, Knapp, Ernst-Walter, Zarić, Snežana D., "C-H/O Interactions of Aromatic CH Donors within Proteins: A Crystallographic Study" in Crystal Growth & Design, 16, no. 4 (2016):1948-1957,
https://doi.org/10.1021/acs.cgd.5b01543 . .
