BioMThermDB 1.0: Thermophysical Database of Proteins in Solutions

We present here a freely available web-based database, called BioMThermDB 1.0, of thermophysical and dynamic properties of various proteins and their aqueous solutions. It contains the hydrodynamic radius, electrophoretic mobility, zeta potential, self-diffusion coefficient, solution viscosity, and...

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Detalles Bibliográficos
Autores principales: Nikolić, Mina, Brudar, Sandi, Coutsias, Evangelos, Dill, Ken A., Lukšič, Miha, Simmerling, Carlos, Hribar-Lee, Barbara
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9741033/
https://www.ncbi.nlm.nih.gov/pubmed/36499696
http://dx.doi.org/10.3390/ijms232315371
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author Nikolić, Mina
Brudar, Sandi
Coutsias, Evangelos
Dill, Ken A.
Lukšič, Miha
Simmerling, Carlos
Hribar-Lee, Barbara
author_facet Nikolić, Mina
Brudar, Sandi
Coutsias, Evangelos
Dill, Ken A.
Lukšič, Miha
Simmerling, Carlos
Hribar-Lee, Barbara
author_sort Nikolić, Mina
collection PubMed
description We present here a freely available web-based database, called BioMThermDB 1.0, of thermophysical and dynamic properties of various proteins and their aqueous solutions. It contains the hydrodynamic radius, electrophoretic mobility, zeta potential, self-diffusion coefficient, solution viscosity, and cloud-point temperature, as well as the conditions for those determinations and details of the experimental method. It can facilitate the meta-analysis and visualization of data, can enable comparisons, and may be useful for comparing theoretical model predictions with experiments.
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spelling pubmed-97410332022-12-11 BioMThermDB 1.0: Thermophysical Database of Proteins in Solutions Nikolić, Mina Brudar, Sandi Coutsias, Evangelos Dill, Ken A. Lukšič, Miha Simmerling, Carlos Hribar-Lee, Barbara Int J Mol Sci Article We present here a freely available web-based database, called BioMThermDB 1.0, of thermophysical and dynamic properties of various proteins and their aqueous solutions. It contains the hydrodynamic radius, electrophoretic mobility, zeta potential, self-diffusion coefficient, solution viscosity, and cloud-point temperature, as well as the conditions for those determinations and details of the experimental method. It can facilitate the meta-analysis and visualization of data, can enable comparisons, and may be useful for comparing theoretical model predictions with experiments. MDPI 2022-12-06 /pmc/articles/PMC9741033/ /pubmed/36499696 http://dx.doi.org/10.3390/ijms232315371 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Nikolić, Mina
Brudar, Sandi
Coutsias, Evangelos
Dill, Ken A.
Lukšič, Miha
Simmerling, Carlos
Hribar-Lee, Barbara
BioMThermDB 1.0: Thermophysical Database of Proteins in Solutions
title BioMThermDB 1.0: Thermophysical Database of Proteins in Solutions
title_full BioMThermDB 1.0: Thermophysical Database of Proteins in Solutions
title_fullStr BioMThermDB 1.0: Thermophysical Database of Proteins in Solutions
title_full_unstemmed BioMThermDB 1.0: Thermophysical Database of Proteins in Solutions
title_short BioMThermDB 1.0: Thermophysical Database of Proteins in Solutions
title_sort biomthermdb 1.0: thermophysical database of proteins in solutions
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9741033/
https://www.ncbi.nlm.nih.gov/pubmed/36499696
http://dx.doi.org/10.3390/ijms232315371
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