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Elucidating the Structural Impacts of Protein InDels

The effects of amino acid insertions and deletions (InDels) remain a rather under-explored area of structural biology. These variations oftentimes are the cause of numerous disease phenotypes. In spite of this, research to study InDels and their structural significance remains limited, primarily due...

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Autores principales: Jilani, Muneeba, Turcan, Alistair, Haspel, Nurit, Jagodzinski, Filip
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9599607/
https://www.ncbi.nlm.nih.gov/pubmed/36291643
http://dx.doi.org/10.3390/biom12101435
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author Jilani, Muneeba
Turcan, Alistair
Haspel, Nurit
Jagodzinski, Filip
author_facet Jilani, Muneeba
Turcan, Alistair
Haspel, Nurit
Jagodzinski, Filip
author_sort Jilani, Muneeba
collection PubMed
description The effects of amino acid insertions and deletions (InDels) remain a rather under-explored area of structural biology. These variations oftentimes are the cause of numerous disease phenotypes. In spite of this, research to study InDels and their structural significance remains limited, primarily due to a lack of experimental information and computational methods. In this work, we fill this gap by modeling InDels computationally; we investigate the rigidity differences between the wildtype and a mutant variant with one or more InDels. Further, we compare how structural effects due to InDels differ from the effects of amino acid substitutions, which are another type of amino acid mutation. We finish by performing a correlation analysis between our rigidity-based metrics and wet lab data for their ability to infer the effects of InDels on protein fitness.
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spelling pubmed-95996072022-10-27 Elucidating the Structural Impacts of Protein InDels Jilani, Muneeba Turcan, Alistair Haspel, Nurit Jagodzinski, Filip Biomolecules Article The effects of amino acid insertions and deletions (InDels) remain a rather under-explored area of structural biology. These variations oftentimes are the cause of numerous disease phenotypes. In spite of this, research to study InDels and their structural significance remains limited, primarily due to a lack of experimental information and computational methods. In this work, we fill this gap by modeling InDels computationally; we investigate the rigidity differences between the wildtype and a mutant variant with one or more InDels. Further, we compare how structural effects due to InDels differ from the effects of amino acid substitutions, which are another type of amino acid mutation. We finish by performing a correlation analysis between our rigidity-based metrics and wet lab data for their ability to infer the effects of InDels on protein fitness. MDPI 2022-10-07 /pmc/articles/PMC9599607/ /pubmed/36291643 http://dx.doi.org/10.3390/biom12101435 Text en © 2022 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
Jilani, Muneeba
Turcan, Alistair
Haspel, Nurit
Jagodzinski, Filip
Elucidating the Structural Impacts of Protein InDels
title Elucidating the Structural Impacts of Protein InDels
title_full Elucidating the Structural Impacts of Protein InDels
title_fullStr Elucidating the Structural Impacts of Protein InDels
title_full_unstemmed Elucidating the Structural Impacts of Protein InDels
title_short Elucidating the Structural Impacts of Protein InDels
title_sort elucidating the structural impacts of protein indels
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9599607/
https://www.ncbi.nlm.nih.gov/pubmed/36291643
http://dx.doi.org/10.3390/biom12101435
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