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CARd: Carbon distribution analysis program for protein sequences

Carbon distribution is responsible for stability and structure of proteins. Arrangement of carbon along the protein sequence is depends on how the amino acids are organized and is guided by mRNAs. An atomic level revision is important for understanding these codes. This will ultimately help in ident...

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Detalles Bibliográficos
Autor principal: Rajasekaran, Ekambaram
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Biomedical Informatics 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3398768/
https://www.ncbi.nlm.nih.gov/pubmed/22829720
http://dx.doi.org/10.6026/97320630008508
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author Rajasekaran, Ekambaram
author_facet Rajasekaran, Ekambaram
author_sort Rajasekaran, Ekambaram
collection PubMed
description Carbon distribution is responsible for stability and structure of proteins. Arrangement of carbon along the protein sequence is depends on how the amino acids are organized and is guided by mRNAs. An atomic level revision is important for understanding these codes. This will ultimately help in identification of disorders and suggest mutations. For this purpose a carbon distribution analysis program has been developed. This program captures the hydrophobic / hydrophilic / disordered regions in a protein. The program gives accurate results. The calculations are precise and sensitive to single amino acid resolution. This program is to help in mutational studies leading to protein stabilisation.
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spelling pubmed-33987682012-07-24 CARd: Carbon distribution analysis program for protein sequences Rajasekaran, Ekambaram Bioinformation Hypothesis Carbon distribution is responsible for stability and structure of proteins. Arrangement of carbon along the protein sequence is depends on how the amino acids are organized and is guided by mRNAs. An atomic level revision is important for understanding these codes. This will ultimately help in identification of disorders and suggest mutations. For this purpose a carbon distribution analysis program has been developed. This program captures the hydrophobic / hydrophilic / disordered regions in a protein. The program gives accurate results. The calculations are precise and sensitive to single amino acid resolution. This program is to help in mutational studies leading to protein stabilisation. Biomedical Informatics 2012-06-16 /pmc/articles/PMC3398768/ /pubmed/22829720 http://dx.doi.org/10.6026/97320630008508 Text en © 2012 Biomedical Informatics This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.
spellingShingle Hypothesis
Rajasekaran, Ekambaram
CARd: Carbon distribution analysis program for protein sequences
title CARd: Carbon distribution analysis program for protein sequences
title_full CARd: Carbon distribution analysis program for protein sequences
title_fullStr CARd: Carbon distribution analysis program for protein sequences
title_full_unstemmed CARd: Carbon distribution analysis program for protein sequences
title_short CARd: Carbon distribution analysis program for protein sequences
title_sort card: carbon distribution analysis program for protein sequences
topic Hypothesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3398768/
https://www.ncbi.nlm.nih.gov/pubmed/22829720
http://dx.doi.org/10.6026/97320630008508
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