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The TMCrys server for supporting crystallization of transmembrane proteins

MOTIVATION: Due to their special properties, the structures of transmembrane proteins are extremely hard to determine. Several methods exist to predict the propensity of successful completion of the structure determination process. However, available predictors incorporate data of any kind of protei...

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Detalles Bibliográficos
Autores principales: Varga, Julia K, Tusnády, Gábor E
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6792070/
https://www.ncbi.nlm.nih.gov/pubmed/30793168
http://dx.doi.org/10.1093/bioinformatics/btz108
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author Varga, Julia K
Tusnády, Gábor E
author_facet Varga, Julia K
Tusnády, Gábor E
author_sort Varga, Julia K
collection PubMed
description MOTIVATION: Due to their special properties, the structures of transmembrane proteins are extremely hard to determine. Several methods exist to predict the propensity of successful completion of the structure determination process. However, available predictors incorporate data of any kind of proteins, hence they can hardly differentiate between crystallizable and non-crystallizable membrane proteins. RESULTS: We implemented a web server to simplify running TMCrys prediction method that was developed specifically to separate crystallizable and non-crystallizable membrane proteins. AVAILABILITY AND IMPLEMENTATION: http://tmcrys.enzim.ttk.mta.hu SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.
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spelling pubmed-67920702019-10-18 The TMCrys server for supporting crystallization of transmembrane proteins Varga, Julia K Tusnády, Gábor E Bioinformatics Applications Notes MOTIVATION: Due to their special properties, the structures of transmembrane proteins are extremely hard to determine. Several methods exist to predict the propensity of successful completion of the structure determination process. However, available predictors incorporate data of any kind of proteins, hence they can hardly differentiate between crystallizable and non-crystallizable membrane proteins. RESULTS: We implemented a web server to simplify running TMCrys prediction method that was developed specifically to separate crystallizable and non-crystallizable membrane proteins. AVAILABILITY AND IMPLEMENTATION: http://tmcrys.enzim.ttk.mta.hu SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online. Oxford University Press 2019-10-15 2019-02-21 /pmc/articles/PMC6792070/ /pubmed/30793168 http://dx.doi.org/10.1093/bioinformatics/btz108 Text en © The Author(s) 2019. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle Applications Notes
Varga, Julia K
Tusnády, Gábor E
The TMCrys server for supporting crystallization of transmembrane proteins
title The TMCrys server for supporting crystallization of transmembrane proteins
title_full The TMCrys server for supporting crystallization of transmembrane proteins
title_fullStr The TMCrys server for supporting crystallization of transmembrane proteins
title_full_unstemmed The TMCrys server for supporting crystallization of transmembrane proteins
title_short The TMCrys server for supporting crystallization of transmembrane proteins
title_sort tmcrys server for supporting crystallization of transmembrane proteins
topic Applications Notes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6792070/
https://www.ncbi.nlm.nih.gov/pubmed/30793168
http://dx.doi.org/10.1093/bioinformatics/btz108
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