Version 1
: Received: 26 November 2019 / Approved: 27 November 2019 / Online: 27 November 2019 (09:35:09 CET)
How to cite:
Domino, K.; Bełdowski, D.; Mazurkiewicz, A.; Musiał, J.; Słomion, M.; Dobosz, R. Analysis of Protein Intramolecular and Solvent Bonding on Example of Major Synovial Fluid Component. Preprints2019, 2019110339. https://doi.org/10.20944/preprints201911.0339.v1
Domino, K.; Bełdowski, D.; Mazurkiewicz, A.; Musiał, J.; Słomion, M.; Dobosz, R. Analysis of Protein Intramolecular and Solvent Bonding on Example of Major Synovial Fluid Component. Preprints 2019, 2019110339. https://doi.org/10.20944/preprints201911.0339.v1
Domino, K.; Bełdowski, D.; Mazurkiewicz, A.; Musiał, J.; Słomion, M.; Dobosz, R. Analysis of Protein Intramolecular and Solvent Bonding on Example of Major Synovial Fluid Component. Preprints2019, 2019110339. https://doi.org/10.20944/preprints201911.0339.v1
APA Style
Domino, K., Bełdowski, D., Mazurkiewicz, A., Musiał, J., Słomion, M., & Dobosz, R. (2019). Analysis of Protein Intramolecular and Solvent Bonding on Example of Major Synovial Fluid Component. Preprints. https://doi.org/10.20944/preprints201911.0339.v1
Chicago/Turabian Style
Domino, K., Małgorzata Słomion and Robert Dobosz. 2019 "Analysis of Protein Intramolecular and Solvent Bonding on Example of Major Synovial Fluid Component" Preprints. https://doi.org/10.20944/preprints201911.0339.v1
Abstract
In this paper we review dynamics and roughness of bonds in proteins on example of albumin, that is important from the physiological point of view. We have performed computer simulations of albumin chain. Statistics were collected by performing many simulations realizations for each experimental setting. We concentrate on hydrogen bonds, cation-π and π- π interactions and NP contacts. Histograms of hydrogen bonds length are positively skewed in contrary to histograms of interactions and HP contacts that are negatively skewed. Scaling exponents of power spectra of energies of bonds / interactions /contacts are in range -0.2 to -0.5 and significantly differ between various hydrogen bonds or interactions. Varying scaling of such spectra can be used to classify between distinct bonds or contacts. Concerning particular amino-acids, largest amount of HBO H20 bonds are between Glutamate (GLU) amino-acids and water particle, while large amount of HBO bonds are formed with Lysine (LYS). For HP contacts the mayor role plays Phenylalanine (PHE) and Leucine (LEU) amino-acids. From decay curves HBO H2O bonds decays in fastest rate, while HBO bonds and HP contacts at slowest rate. We present as well decay curves of bonds formed by particular amino-acids, that gives interesting results.
Keywords
human albumin; hydrogen bonds; hp contacts; π- π / cation-π interactions; bonds roughness; decay curve; power spectrum; interaction between amino-acids
Subject
Chemistry and Materials Science, Medicinal Chemistry
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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