AI Article Synopsis
- The study examines the spatial arrangement of carbon in protein structures, specifically analyzing the carbon fractions around individual atoms.
- Results indicate that globular proteins conform to an expected carbon distribution of 31.45%, with dimeric forms showing better carbon distribution compared to monomers.
- Additionally, liquid structures (analyzed through NMR) exhibit superior carbon distribution compared to solid structures (analyzed through X-Ray), while fiber proteins align with expected carbon distribution patterns, unlike toxin proteins that display abnormal distributions.
Article 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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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3974240 | PMC |
| http://dx.doi.org/10.6026/97320630010138 | DOI Listing |
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