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Water Dynamics in Highly Concentrated Protein Systems—Insight from Nuclear Magnetic Resonance Relaxometry
(1)H spin-lattice relaxation experiments have been performed for water–Bovine Serum Albumin (BSA) mixtures, including 20%wt and 40%wt of BSA. The experiments have been carried out in a frequency range encompassing three orders of magnitude, from 10 kHz to 10 MHz, versus temperature. The relaxation d...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9963861/ https://www.ncbi.nlm.nih.gov/pubmed/36835511 http://dx.doi.org/10.3390/ijms24044093 |
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author | Kruk, Danuta Kasparek, Adam Masiewicz, Elzbieta Kolodziejski, Karol Cybulski, Radoslaw Nowak, Bartosz |
author_facet | Kruk, Danuta Kasparek, Adam Masiewicz, Elzbieta Kolodziejski, Karol Cybulski, Radoslaw Nowak, Bartosz |
author_sort | Kruk, Danuta |
collection | PubMed |
description | (1)H spin-lattice relaxation experiments have been performed for water–Bovine Serum Albumin (BSA) mixtures, including 20%wt and 40%wt of BSA. The experiments have been carried out in a frequency range encompassing three orders of magnitude, from 10 kHz to 10 MHz, versus temperature. The relaxation data have been thoroughly analyzed in terms of several relaxation models with the purpose of revealing the mechanisms of water motion. For this purpose, four relaxation models have been used: the data have been decomposed into relaxation contributions expressed in terms of Lorentzian spectral densities, then three-dimensional translation diffusion has been assumed, next two-dimensional surface diffusion has been considered, and eventually, a model of surface diffusion mediated by acts of adsorption to the surface has been employed. In this way, it has been demonstrated that the last concept is the most plausible. Parameters describing the dynamics in a quantitative manner have been determined and discussed. |
format | Online Article Text |
id | pubmed-9963861 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-99638612023-02-26 Water Dynamics in Highly Concentrated Protein Systems—Insight from Nuclear Magnetic Resonance Relaxometry Kruk, Danuta Kasparek, Adam Masiewicz, Elzbieta Kolodziejski, Karol Cybulski, Radoslaw Nowak, Bartosz Int J Mol Sci Article (1)H spin-lattice relaxation experiments have been performed for water–Bovine Serum Albumin (BSA) mixtures, including 20%wt and 40%wt of BSA. The experiments have been carried out in a frequency range encompassing three orders of magnitude, from 10 kHz to 10 MHz, versus temperature. The relaxation data have been thoroughly analyzed in terms of several relaxation models with the purpose of revealing the mechanisms of water motion. For this purpose, four relaxation models have been used: the data have been decomposed into relaxation contributions expressed in terms of Lorentzian spectral densities, then three-dimensional translation diffusion has been assumed, next two-dimensional surface diffusion has been considered, and eventually, a model of surface diffusion mediated by acts of adsorption to the surface has been employed. In this way, it has been demonstrated that the last concept is the most plausible. Parameters describing the dynamics in a quantitative manner have been determined and discussed. MDPI 2023-02-17 /pmc/articles/PMC9963861/ /pubmed/36835511 http://dx.doi.org/10.3390/ijms24044093 Text en © 2023 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 Kruk, Danuta Kasparek, Adam Masiewicz, Elzbieta Kolodziejski, Karol Cybulski, Radoslaw Nowak, Bartosz Water Dynamics in Highly Concentrated Protein Systems—Insight from Nuclear Magnetic Resonance Relaxometry |
title | Water Dynamics in Highly Concentrated Protein Systems—Insight from Nuclear Magnetic Resonance Relaxometry |
title_full | Water Dynamics in Highly Concentrated Protein Systems—Insight from Nuclear Magnetic Resonance Relaxometry |
title_fullStr | Water Dynamics in Highly Concentrated Protein Systems—Insight from Nuclear Magnetic Resonance Relaxometry |
title_full_unstemmed | Water Dynamics in Highly Concentrated Protein Systems—Insight from Nuclear Magnetic Resonance Relaxometry |
title_short | Water Dynamics in Highly Concentrated Protein Systems—Insight from Nuclear Magnetic Resonance Relaxometry |
title_sort | water dynamics in highly concentrated protein systems—insight from nuclear magnetic resonance relaxometry |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9963861/ https://www.ncbi.nlm.nih.gov/pubmed/36835511 http://dx.doi.org/10.3390/ijms24044093 |
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