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Biologistics—Diffusion coefficients for complete proteome of Escherichia coli

Motivation: Biologistics provides data for quantitative analysis of transport (diffusion) processes and their spatio-temporal correlations in cells. Mobility of proteins is one of the few parameters necessary to describe reaction rates for gene regulation. Although understanding of diffusion-limited...

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Autores principales: Kalwarczyk, Tomasz, Tabaka, Marcin, Holyst, Robert
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3496334/
https://www.ncbi.nlm.nih.gov/pubmed/22942021
http://dx.doi.org/10.1093/bioinformatics/bts537
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author Kalwarczyk, Tomasz
Tabaka, Marcin
Holyst, Robert
author_facet Kalwarczyk, Tomasz
Tabaka, Marcin
Holyst, Robert
author_sort Kalwarczyk, Tomasz
collection PubMed
description Motivation: Biologistics provides data for quantitative analysis of transport (diffusion) processes and their spatio-temporal correlations in cells. Mobility of proteins is one of the few parameters necessary to describe reaction rates for gene regulation. Although understanding of diffusion-limited biochemical reactions in vivo requires mobility data for the largest possible number of proteins in their native forms, currently, there is no database that would contain the complete information about the diffusion coefficients (DCs) of proteins in a given cell type. Results: We demonstrate a method for the determination of in vivo DCs for any molecule—regardless of its molecular weight, size and structure—in any type of cell. We exemplify the method with the database of in vivo DC for all proteins (4302 records) from the proteome of K12 strain of Escherichia coli, together with examples of DC of amino acids, sugars, RNA and DNA. The database follows from the scale-dependent viscosity reference curve (sdVRC). Construction of sdVRC for prokaryotic or eukaryotic cell requires ~20 in vivo measurements using techniques such as fluorescence correlation spectroscopy (FCS), fluorescence recovery after photobleaching (FRAP), nuclear magnetic resonance (NMR) or particle tracking. The shape of the sdVRC would be different for each organism, but the mathematical form of the curve remains the same. The presented method has a high predictive power, as the measurements of DCs of several inert, properly chosen probes in a single cell type allows to determine the DCs of thousands of proteins. Additionally, obtained mobility data allow quantitative study of biochemical interactions in vivo. Contact: rholyst@ichf.edu.pl Supplementary information: Supplementary data are available at Bioinformatics Online.
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spelling pubmed-34963342012-12-12 Biologistics—Diffusion coefficients for complete proteome of Escherichia coli Kalwarczyk, Tomasz Tabaka, Marcin Holyst, Robert Bioinformatics Original Papers Motivation: Biologistics provides data for quantitative analysis of transport (diffusion) processes and their spatio-temporal correlations in cells. Mobility of proteins is one of the few parameters necessary to describe reaction rates for gene regulation. Although understanding of diffusion-limited biochemical reactions in vivo requires mobility data for the largest possible number of proteins in their native forms, currently, there is no database that would contain the complete information about the diffusion coefficients (DCs) of proteins in a given cell type. Results: We demonstrate a method for the determination of in vivo DCs for any molecule—regardless of its molecular weight, size and structure—in any type of cell. We exemplify the method with the database of in vivo DC for all proteins (4302 records) from the proteome of K12 strain of Escherichia coli, together with examples of DC of amino acids, sugars, RNA and DNA. The database follows from the scale-dependent viscosity reference curve (sdVRC). Construction of sdVRC for prokaryotic or eukaryotic cell requires ~20 in vivo measurements using techniques such as fluorescence correlation spectroscopy (FCS), fluorescence recovery after photobleaching (FRAP), nuclear magnetic resonance (NMR) or particle tracking. The shape of the sdVRC would be different for each organism, but the mathematical form of the curve remains the same. The presented method has a high predictive power, as the measurements of DCs of several inert, properly chosen probes in a single cell type allows to determine the DCs of thousands of proteins. Additionally, obtained mobility data allow quantitative study of biochemical interactions in vivo. Contact: rholyst@ichf.edu.pl Supplementary information: Supplementary data are available at Bioinformatics Online. Oxford University Press 2012-11-15 2012-08-31 /pmc/articles/PMC3496334/ /pubmed/22942021 http://dx.doi.org/10.1093/bioinformatics/bts537 Text en © The Author 2012. Published by Oxford University Press. http://creativecommons.org/licenses/by/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Papers
Kalwarczyk, Tomasz
Tabaka, Marcin
Holyst, Robert
Biologistics—Diffusion coefficients for complete proteome of Escherichia coli
title Biologistics—Diffusion coefficients for complete proteome of Escherichia coli
title_full Biologistics—Diffusion coefficients for complete proteome of Escherichia coli
title_fullStr Biologistics—Diffusion coefficients for complete proteome of Escherichia coli
title_full_unstemmed Biologistics—Diffusion coefficients for complete proteome of Escherichia coli
title_short Biologistics—Diffusion coefficients for complete proteome of Escherichia coli
title_sort biologistics—diffusion coefficients for complete proteome of escherichia coli
topic Original Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3496334/
https://www.ncbi.nlm.nih.gov/pubmed/22942021
http://dx.doi.org/10.1093/bioinformatics/bts537
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