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On methods for determining solvent accessible surface area for proteins in their unfolded state
BACKGROUND: There are many different methods for estimating solvent accessible surface area for proteins in their unfolded states. In this article, we compare eight methods, assessing whether or not they lead to different estimates of total accessible surface area as well as their impact on relation...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4167527/ https://www.ncbi.nlm.nih.gov/pubmed/25187400 http://dx.doi.org/10.1186/1756-0500-7-602 |
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author | Lu, Shennon Wagaman, Amy S |
author_facet | Lu, Shennon Wagaman, Amy S |
author_sort | Lu, Shennon |
collection | PubMed |
description | BACKGROUND: There are many different methods for estimating solvent accessible surface area for proteins in their unfolded states. In this article, we compare eight methods, assessing whether or not they lead to different estimates of total accessible surface area as well as their impact on relationships with thermodynamic variables. FINDINGS: Our results demonstrate that most pairs of compared methods do result in different unfolded estimates of accessible surface area (only four pairs of methods do not yield significantly different estimates). However, we do not see a significant impact on the relationship between accessible surface area and thermodynamic parameters across the different methods. CONCLUSIONS: We advocate the use of the Gong and Rose transition midpoint method for computing solvent accessible surface area due to its computational ease, physical basis, and performance in terms of relationships with thermodynamic parameters. |
format | Online Article Text |
id | pubmed-4167527 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-41675272014-09-19 On methods for determining solvent accessible surface area for proteins in their unfolded state Lu, Shennon Wagaman, Amy S BMC Res Notes Technical Note BACKGROUND: There are many different methods for estimating solvent accessible surface area for proteins in their unfolded states. In this article, we compare eight methods, assessing whether or not they lead to different estimates of total accessible surface area as well as their impact on relationships with thermodynamic variables. FINDINGS: Our results demonstrate that most pairs of compared methods do result in different unfolded estimates of accessible surface area (only four pairs of methods do not yield significantly different estimates). However, we do not see a significant impact on the relationship between accessible surface area and thermodynamic parameters across the different methods. CONCLUSIONS: We advocate the use of the Gong and Rose transition midpoint method for computing solvent accessible surface area due to its computational ease, physical basis, and performance in terms of relationships with thermodynamic parameters. BioMed Central 2014-09-03 /pmc/articles/PMC4167527/ /pubmed/25187400 http://dx.doi.org/10.1186/1756-0500-7-602 Text en © Lu and Wagaman; licensee BioMed Central Ltd. 2014 This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Technical Note Lu, Shennon Wagaman, Amy S On methods for determining solvent accessible surface area for proteins in their unfolded state |
title | On methods for determining solvent accessible surface area for proteins in their unfolded state |
title_full | On methods for determining solvent accessible surface area for proteins in their unfolded state |
title_fullStr | On methods for determining solvent accessible surface area for proteins in their unfolded state |
title_full_unstemmed | On methods for determining solvent accessible surface area for proteins in their unfolded state |
title_short | On methods for determining solvent accessible surface area for proteins in their unfolded state |
title_sort | on methods for determining solvent accessible surface area for proteins in their unfolded state |
topic | Technical Note |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4167527/ https://www.ncbi.nlm.nih.gov/pubmed/25187400 http://dx.doi.org/10.1186/1756-0500-7-602 |
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