Measuring evolutionary rates of proteins in a structural context [version 2; referees: 4 approved]

We describe how to measure site-specific rates of evolution in protein-coding genes and how to correlate these rates with structural features of the expressed protein, such as relative solvent accessibility, secondary structure, or weighted contact number. We present two alternative approaches to ra...

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Main Authors: Dariya K. Sydykova, Benjamin R. Jack, Stephanie J. Spielman, Claus O. Wilke
Format: Article
Language:English
Published: F1000 Research Ltd 2018-02-01
Series:F1000Research
Subjects:
Online Access:https://f1000research.com/articles/6-1845/v2
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author Dariya K. Sydykova
Benjamin R. Jack
Stephanie J. Spielman
Claus O. Wilke
author_facet Dariya K. Sydykova
Benjamin R. Jack
Stephanie J. Spielman
Claus O. Wilke
author_sort Dariya K. Sydykova
collection DOAJ
description We describe how to measure site-specific rates of evolution in protein-coding genes and how to correlate these rates with structural features of the expressed protein, such as relative solvent accessibility, secondary structure, or weighted contact number. We present two alternative approaches to rate calculations: One based on relative amino-acid rates, and the other based on site-specific codon rates measured as dN/dS. We additionally provide a code repository containing scripts to facilitate the specific analysis protocols we recommend.
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spelling doaj.art-a9e8997a153d444ab94e49429043d6c62022-12-22T02:39:58ZengF1000 Research LtdF1000Research2046-14022018-02-01610.12688/f1000research.12874.215080Measuring evolutionary rates of proteins in a structural context [version 2; referees: 4 approved]Dariya K. Sydykova0Benjamin R. Jack1Stephanie J. Spielman2Claus O. Wilke3Department of Integrative Biology, The University of Texas at Austin, Austin, TX, 78712, USADepartment of Integrative Biology, The University of Texas at Austin, Austin, TX, 78712, USAInstitute for Genomics and Evolutionary Medicine, Temple University, Philadelphia, PA, 19122, USADepartment of Integrative Biology, The University of Texas at Austin, Austin, TX, 78712, USAWe describe how to measure site-specific rates of evolution in protein-coding genes and how to correlate these rates with structural features of the expressed protein, such as relative solvent accessibility, secondary structure, or weighted contact number. We present two alternative approaches to rate calculations: One based on relative amino-acid rates, and the other based on site-specific codon rates measured as dN/dS. We additionally provide a code repository containing scripts to facilitate the specific analysis protocols we recommend.https://f1000research.com/articles/6-1845/v2BioinformaticsProtein Chemistry & Proteomics
spellingShingle Dariya K. Sydykova
Benjamin R. Jack
Stephanie J. Spielman
Claus O. Wilke
Measuring evolutionary rates of proteins in a structural context [version 2; referees: 4 approved]
F1000Research
Bioinformatics
Protein Chemistry & Proteomics
title Measuring evolutionary rates of proteins in a structural context [version 2; referees: 4 approved]
title_full Measuring evolutionary rates of proteins in a structural context [version 2; referees: 4 approved]
title_fullStr Measuring evolutionary rates of proteins in a structural context [version 2; referees: 4 approved]
title_full_unstemmed Measuring evolutionary rates of proteins in a structural context [version 2; referees: 4 approved]
title_short Measuring evolutionary rates of proteins in a structural context [version 2; referees: 4 approved]
title_sort measuring evolutionary rates of proteins in a structural context version 2 referees 4 approved
topic Bioinformatics
Protein Chemistry & Proteomics
url https://f1000research.com/articles/6-1845/v2
work_keys_str_mv AT dariyaksydykova measuringevolutionaryratesofproteinsinastructuralcontextversion2referees4approved
AT benjaminrjack measuringevolutionaryratesofproteinsinastructuralcontextversion2referees4approved
AT stephaniejspielman measuringevolutionaryratesofproteinsinastructuralcontextversion2referees4approved
AT clausowilke measuringevolutionaryratesofproteinsinastructuralcontextversion2referees4approved