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Protein–Water–Ice Contact Angle

[Image: see text] The protein–water–ice contact angle is a controlling parameter in diverse fields. Here we show that data from three different experiments, at three different length scales, with three different proteins, in three different laboratories yield a consistent value for the protein–water...

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Autores principales: Karlsson, Jens O. M., Braslavsky, Ido, Elliott, Janet A. W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2018
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6563840/
https://www.ncbi.nlm.nih.gov/pubmed/29979046
http://dx.doi.org/10.1021/acs.langmuir.8b01276
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author Karlsson, Jens O. M.
Braslavsky, Ido
Elliott, Janet A. W.
author_facet Karlsson, Jens O. M.
Braslavsky, Ido
Elliott, Janet A. W.
author_sort Karlsson, Jens O. M.
collection PubMed
description [Image: see text] The protein–water–ice contact angle is a controlling parameter in diverse fields. Here we show that data from three different experiments, at three different length scales, with three different proteins, in three different laboratories yield a consistent value for the protein–water–ice contact angle (88.0 ± 1.3°) when analyzed using the Gibbs–Thomson equation. The measurements reinforce the validity of each other, and the fact that similar values are obtained across diverse length scales, experiments, and proteins yields insight into protein–water interactions and the applicability of thermodynamics at the nanoscale.
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spelling pubmed-65638402019-07-06 Protein–Water–Ice Contact Angle Karlsson, Jens O. M. Braslavsky, Ido Elliott, Janet A. W. Langmuir [Image: see text] The protein–water–ice contact angle is a controlling parameter in diverse fields. Here we show that data from three different experiments, at three different length scales, with three different proteins, in three different laboratories yield a consistent value for the protein–water–ice contact angle (88.0 ± 1.3°) when analyzed using the Gibbs–Thomson equation. The measurements reinforce the validity of each other, and the fact that similar values are obtained across diverse length scales, experiments, and proteins yields insight into protein–water interactions and the applicability of thermodynamics at the nanoscale. American Chemical Society 2018-07-06 2019-06-11 /pmc/articles/PMC6563840/ /pubmed/29979046 http://dx.doi.org/10.1021/acs.langmuir.8b01276 Text en Copyright © 2018 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Karlsson, Jens O. M.
Braslavsky, Ido
Elliott, Janet A. W.
Protein–Water–Ice Contact Angle
title Protein–Water–Ice Contact Angle
title_full Protein–Water–Ice Contact Angle
title_fullStr Protein–Water–Ice Contact Angle
title_full_unstemmed Protein–Water–Ice Contact Angle
title_short Protein–Water–Ice Contact Angle
title_sort protein–water–ice contact angle
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6563840/
https://www.ncbi.nlm.nih.gov/pubmed/29979046
http://dx.doi.org/10.1021/acs.langmuir.8b01276
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