DispHScan: A Multi-Sequence Web Tool for Predicting Protein Disorder as a Function of pH

Proteins are exposed to fluctuating environmental conditions in their cellular context and during their biotechnological production. Disordered regions are susceptible to these fluctuations and may experience solvent-dependent conformational switches that affect their local dynamism and activity. In...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Carlos Pintado-Grima, Valentín Iglesias, Jaime Santos, Vladimir N. Uversky, Salvador Ventura
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	conditional disorder pH sequence analysis protein structure bioinformatics Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/a721b402a68b43ca97d907efc1919c9f
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:a721b402a68b43ca97d907efc1919c9f
record_format	dspace
spelling	oai:doaj.org-article:a721b402a68b43ca97d907efc1919c9f2021-11-25T16:52:40ZDispHScan: A Multi-Sequence Web Tool for Predicting Protein Disorder as a Function of pH10.3390/biom111115962218-273Xhttps://doaj.org/article/a721b402a68b43ca97d907efc1919c9f2021-10-01T00:00:00Zhttps://www.mdpi.com/2218-273X/11/11/1596https://doaj.org/toc/2218-273XProteins are exposed to fluctuating environmental conditions in their cellular context and during their biotechnological production. Disordered regions are susceptible to these fluctuations and may experience solvent-dependent conformational switches that affect their local dynamism and activity. In a recent study, we modeled the influence of pH in the conformational state of IDPs by exploiting a charge–hydrophobicity diagram that considered the effect of solution pH on both variables. However, it was not possible to predict context-dependent transitions for multiple sequences, precluding proteome-wide analysis or the screening of collections of mutants. In this article, we present DispHScan, the first computational tool dedicated to predicting pH-induced disorder–order transitions in large protein datasets. The DispHScan web server allows the users to run pH-dependent disorder predictions of multiple sequences and identify context-dependent conformational transitions. It might provide new insights on the role of pH-modulated conditional disorder in the physiology and pathology of different organisms. The DispHScan web server is freely available for academic users, it is platform-independent and does not require previous registration.Carlos Pintado-GrimaValentín IglesiasJaime SantosVladimir N. UverskySalvador VenturaMDPI AGarticleconditional disorderpHsequence analysisprotein structurebioinformaticsMicrobiologyQR1-502ENBiomolecules, Vol 11, Iss 1596, p 1596 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	conditional disorder pH sequence analysis protein structure bioinformatics Microbiology QR1-502
spellingShingle	conditional disorder pH sequence analysis protein structure bioinformatics Microbiology QR1-502 Carlos Pintado-Grima Valentín Iglesias Jaime Santos Vladimir N. Uversky Salvador Ventura DispHScan: A Multi-Sequence Web Tool for Predicting Protein Disorder as a Function of pH
description	Proteins are exposed to fluctuating environmental conditions in their cellular context and during their biotechnological production. Disordered regions are susceptible to these fluctuations and may experience solvent-dependent conformational switches that affect their local dynamism and activity. In a recent study, we modeled the influence of pH in the conformational state of IDPs by exploiting a charge–hydrophobicity diagram that considered the effect of solution pH on both variables. However, it was not possible to predict context-dependent transitions for multiple sequences, precluding proteome-wide analysis or the screening of collections of mutants. In this article, we present DispHScan, the first computational tool dedicated to predicting pH-induced disorder–order transitions in large protein datasets. The DispHScan web server allows the users to run pH-dependent disorder predictions of multiple sequences and identify context-dependent conformational transitions. It might provide new insights on the role of pH-modulated conditional disorder in the physiology and pathology of different organisms. The DispHScan web server is freely available for academic users, it is platform-independent and does not require previous registration.
format	article
author	Carlos Pintado-Grima Valentín Iglesias Jaime Santos Vladimir N. Uversky Salvador Ventura
author_facet	Carlos Pintado-Grima Valentín Iglesias Jaime Santos Vladimir N. Uversky Salvador Ventura
author_sort	Carlos Pintado-Grima
title	DispHScan: A Multi-Sequence Web Tool for Predicting Protein Disorder as a Function of pH
title_short	DispHScan: A Multi-Sequence Web Tool for Predicting Protein Disorder as a Function of pH
title_full	DispHScan: A Multi-Sequence Web Tool for Predicting Protein Disorder as a Function of pH
title_fullStr	DispHScan: A Multi-Sequence Web Tool for Predicting Protein Disorder as a Function of pH
title_full_unstemmed	DispHScan: A Multi-Sequence Web Tool for Predicting Protein Disorder as a Function of pH
title_sort	disphscan: a multi-sequence web tool for predicting protein disorder as a function of ph
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/a721b402a68b43ca97d907efc1919c9f
work_keys_str_mv	AT carlospintadogrima disphscanamultisequencewebtoolforpredictingproteindisorderasafunctionofph AT valentiniglesias disphscanamultisequencewebtoolforpredictingproteindisorderasafunctionofph AT jaimesantos disphscanamultisequencewebtoolforpredictingproteindisorderasafunctionofph AT vladimirnuversky disphscanamultisequencewebtoolforpredictingproteindisorderasafunctionofph AT salvadorventura disphscanamultisequencewebtoolforpredictingproteindisorderasafunctionofph
_version_	1718412914602278912

DispHScan: A Multi-Sequence Web Tool for Predicting Protein Disorder as a Function of pH

Ejemplares similares