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CARd-3D: Carbon Distribution in 3D Structure Program for Globular Proteins
Spatial arrangement of carbon in protein structure is analyzed here. Particularly, the carbon fractions around individual atoms are compared. It is hoped that it follows the principle of 31.45% carbon around individual atoms. The results reveal that globular protein's atoms follow this principl...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Biomedical Informatics
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3974240/ https://www.ncbi.nlm.nih.gov/pubmed/24748753 http://dx.doi.org/10.6026/97320630010138 |
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author | Ekambaram, Rajasekaran Kannaiyan, Akila Marimuthu, Vijayasarathy Swaminathan, Vinobha Chinnaiah Renganathan, Senthil Perumal, Ananda Gopu |
author_facet | Ekambaram, Rajasekaran Kannaiyan, Akila Marimuthu, Vijayasarathy Swaminathan, Vinobha Chinnaiah Renganathan, Senthil Perumal, Ananda Gopu |
author_sort | Ekambaram, Rajasekaran |
collection | PubMed |
description | Spatial arrangement of carbon in protein structure is analyzed here. Particularly, the carbon fractions around individual atoms are compared. It is hoped that it follows the principle of 31.45% carbon around individual atoms. The results reveal that globular protein's atoms follow this principle. A comparative study on monomer versus dimer reveal that carbon is better distributed in dimeric form than in its monomeric form. Similar study on solid versus liquid structures reveals that the liquid (NMR) structure has better carbon distribution over the corresponding solid (X-Ray) structure. The carbon fraction distributions in fiber and toxin protein are compared. Fiber proteins follow the principle of carbon fraction distribution. At the same time it has another broad spectrum of carbon distribution than in globular proteins. The toxin protein follows an abnormal carbon fraction distribution. The carbon fraction distribution plays an important role in deciding the structure and shape of proteins. It is hoped to help in understanding the protein folding and function. |
format | Online Article Text |
id | pubmed-3974240 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Biomedical Informatics |
record_format | MEDLINE/PubMed |
spelling | pubmed-39742402014-04-18 CARd-3D: Carbon Distribution in 3D Structure Program for Globular Proteins Ekambaram, Rajasekaran Kannaiyan, Akila Marimuthu, Vijayasarathy Swaminathan, Vinobha Chinnaiah Renganathan, Senthil Perumal, Ananda Gopu Bioinformation Hypothesis Spatial arrangement of carbon in protein structure is analyzed here. Particularly, the carbon fractions around individual atoms are compared. It is hoped that it follows the principle of 31.45% carbon around individual atoms. The results reveal that globular protein's atoms follow this principle. A comparative study on monomer versus dimer reveal that carbon is better distributed in dimeric form than in its monomeric form. Similar study on solid versus liquid structures reveals that the liquid (NMR) structure has better carbon distribution over the corresponding solid (X-Ray) structure. The carbon fraction distributions in fiber and toxin protein are compared. Fiber proteins follow the principle of carbon fraction distribution. At the same time it has another broad spectrum of carbon distribution than in globular proteins. The toxin protein follows an abnormal carbon fraction distribution. The carbon fraction distribution plays an important role in deciding the structure and shape of proteins. It is hoped to help in understanding the protein folding and function. Biomedical Informatics 2014-03-19 /pmc/articles/PMC3974240/ /pubmed/24748753 http://dx.doi.org/10.6026/97320630010138 Text en © 2014 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 Ekambaram, Rajasekaran Kannaiyan, Akila Marimuthu, Vijayasarathy Swaminathan, Vinobha Chinnaiah Renganathan, Senthil Perumal, Ananda Gopu CARd-3D: Carbon Distribution in 3D Structure Program for Globular Proteins |
title | CARd-3D: Carbon Distribution in 3D Structure Program for Globular Proteins |
title_full | CARd-3D: Carbon Distribution in 3D Structure Program for Globular Proteins |
title_fullStr | CARd-3D: Carbon Distribution in 3D Structure Program for Globular Proteins |
title_full_unstemmed | CARd-3D: Carbon Distribution in 3D Structure Program for Globular Proteins |
title_short | CARd-3D: Carbon Distribution in 3D Structure Program for Globular Proteins |
title_sort | card-3d: carbon distribution in 3d structure program for globular proteins |
topic | Hypothesis |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3974240/ https://www.ncbi.nlm.nih.gov/pubmed/24748753 http://dx.doi.org/10.6026/97320630010138 |
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