Crystallographic study on CH/O interactions of aromatic CH donors within proteins
Authors
Dragelj, J.Lj.Stanković, Ivana M.
Božinovski, D.M.
Meyer, T.
Veljković, Dušan
Medaković, Vesna B.
Knapp, Ernst Walter
Zarić, Snežana D.
Conference object (Published version)
Metadata
Show full item recordAbstract
CH/O interactions represent weak hydrogen bonds that stabilize protein structures
where they contribute up to 25% among the total number of detected
hydrogen bonds. Previously, we showed that CH/O interactions do not show
strong preference for linear contacts and that the energy of CH/O interactions
of aromatic CH donors depends on the type of atom or group in ortho-position to
the interacting CH group [1, 2]. In this work, CH/O interactions of aromatic CH
donors within proteins have been studied by analyzing the data in the Protein
Data Bank (PDB) and by quantum chemical calculations of electrostatic potentials.
The CH/O interactions were studied between three aromatic amino acids;
phenylalanine, tyrosine and tryptophan, with several acceptors.
The analysis of the distribution of the CHO angle in the crystal structures from
the PDB indicates no preference for linear CH/O interactions between aromatic
donors and acceptors in protein structures. Although there is no tendency... for
linear CH/O interactions, there is no significant number of bifurcated CH/O
interactions. The analyses also indicate an influence of simultaneous classical
hydrogen bonds. The influence is particularly observed in case of tyrosine. The
hydroxyl group of aromatic ring of tyrosine plays an important role by forming
a simultaneous classical hydrogen bond along with CH/O interaction in orthoposition
to the OH substituent. These investigations could help in future CH/O
interactions studies in proteins or other proteic systems.
Keywords:
Aromatic amino acids / CH/O interactions / Hydrogen bond / PDBSource:
Book of Abstracts - Belgrade BioInformatics Conference 2016, BelBI2016, 2016, 119-119Publisher:
- Belgrade : The Bioinformatics Research Group, University of Belgrade - Faculty of Mathematics
Note:
- Belgrade, Serbia, June 20-24, 2016
Collections
Institution/Community
IHTMTY - CONF AU - Dragelj, J.Lj. AU - Stanković, Ivana M. AU - Božinovski, D.M. AU - Meyer, T. AU - Veljković, Dušan AU - Medaković, Vesna B. AU - Knapp, Ernst Walter AU - Zarić, Snežana D. PY - 2016 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/4858 AB - CH/O interactions represent weak hydrogen bonds that stabilize protein structures where they contribute up to 25% among the total number of detected hydrogen bonds. Previously, we showed that CH/O interactions do not show strong preference for linear contacts and that the energy of CH/O interactions of aromatic CH donors depends on the type of atom or group in ortho-position to the interacting CH group [1, 2]. In this work, CH/O interactions of aromatic CH donors within proteins have been studied by analyzing the data in the Protein Data Bank (PDB) and by quantum chemical calculations of electrostatic potentials. The CH/O interactions were studied between three aromatic amino acids; phenylalanine, tyrosine and tryptophan, with several acceptors. The analysis of the distribution of the CHO angle in the crystal structures from the PDB indicates no preference for linear CH/O interactions between aromatic donors and acceptors in protein structures. Although there is no tendency for linear CH/O interactions, there is no significant number of bifurcated CH/O interactions. The analyses also indicate an influence of simultaneous classical hydrogen bonds. The influence is particularly observed in case of tyrosine. The hydroxyl group of aromatic ring of tyrosine plays an important role by forming a simultaneous classical hydrogen bond along with CH/O interaction in orthoposition to the OH substituent. These investigations could help in future CH/O interactions studies in proteins or other proteic systems. PB - Belgrade : The Bioinformatics Research Group, University of Belgrade - Faculty of Mathematics C3 - Book of Abstracts - Belgrade BioInformatics Conference 2016, BelBI2016 T1 - Crystallographic study on CH/O interactions of aromatic CH donors within proteins SP - 119 EP - 119 UR - https://hdl.handle.net/21.15107/rcub_cer_4858 ER -
@conference{ author = "Dragelj, J.Lj. and Stanković, Ivana M. and Božinovski, D.M. and Meyer, T. and Veljković, Dušan and Medaković, Vesna B. and Knapp, Ernst Walter and Zarić, Snežana D.", year = "2016", abstract = "CH/O interactions represent weak hydrogen bonds that stabilize protein structures where they contribute up to 25% among the total number of detected hydrogen bonds. Previously, we showed that CH/O interactions do not show strong preference for linear contacts and that the energy of CH/O interactions of aromatic CH donors depends on the type of atom or group in ortho-position to the interacting CH group [1, 2]. In this work, CH/O interactions of aromatic CH donors within proteins have been studied by analyzing the data in the Protein Data Bank (PDB) and by quantum chemical calculations of electrostatic potentials. The CH/O interactions were studied between three aromatic amino acids; phenylalanine, tyrosine and tryptophan, with several acceptors. The analysis of the distribution of the CHO angle in the crystal structures from the PDB indicates no preference for linear CH/O interactions between aromatic donors and acceptors in protein structures. Although there is no tendency for linear CH/O interactions, there is no significant number of bifurcated CH/O interactions. The analyses also indicate an influence of simultaneous classical hydrogen bonds. The influence is particularly observed in case of tyrosine. The hydroxyl group of aromatic ring of tyrosine plays an important role by forming a simultaneous classical hydrogen bond along with CH/O interaction in orthoposition to the OH substituent. These investigations could help in future CH/O interactions studies in proteins or other proteic systems.", publisher = "Belgrade : The Bioinformatics Research Group, University of Belgrade - Faculty of Mathematics", journal = "Book of Abstracts - Belgrade BioInformatics Conference 2016, BelBI2016", title = "Crystallographic study on CH/O interactions of aromatic CH donors within proteins", pages = "119-119", url = "https://hdl.handle.net/21.15107/rcub_cer_4858" }
Dragelj, J.Lj., Stanković, I. M., Božinovski, D.M., Meyer, T., Veljković, D., Medaković, V. B., Knapp, E. W.,& Zarić, S. D.. (2016). Crystallographic study on CH/O interactions of aromatic CH donors within proteins. in Book of Abstracts - Belgrade BioInformatics Conference 2016, BelBI2016 Belgrade : The Bioinformatics Research Group, University of Belgrade - Faculty of Mathematics., 119-119. https://hdl.handle.net/21.15107/rcub_cer_4858
Dragelj J, Stanković IM, Božinovski D, Meyer T, Veljković D, Medaković VB, Knapp EW, Zarić SD. Crystallographic study on CH/O interactions of aromatic CH donors within proteins. in Book of Abstracts - Belgrade BioInformatics Conference 2016, BelBI2016. 2016;:119-119. https://hdl.handle.net/21.15107/rcub_cer_4858 .
Dragelj, J.Lj., Stanković, Ivana M., Božinovski, D.M., Meyer, T., Veljković, Dušan, Medaković, Vesna B., Knapp, Ernst Walter, Zarić, Snežana D., "Crystallographic study on CH/O interactions of aromatic CH donors within proteins" in Book of Abstracts - Belgrade BioInformatics Conference 2016, BelBI2016 (2016):119-119, https://hdl.handle.net/21.15107/rcub_cer_4858 .