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CARd-3D: Carbon Distribution in 3D Structure Program for Globular Proteins.

Authors
  • Ekambaram, Rajasekaran
  • Kannaiyan, Akila
  • Marimuthu, Vijayasarathy
  • Swaminathan, Vinobha Chinnaiah
  • Renganathan, Senthil
  • Perumal, Ananda Gopu
Type
Published Article
Journal
Bioinformation
Publisher
Biomedical Informatics
Publication Date
Jan 01, 2014
Volume
10
Issue
3
Pages
138–143
Identifiers
DOI: 10.6026/97320630010138
PMID: 24748753
Source
Medline
Keywords
License
Unknown

Abstract

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.

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