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CARd-3D:球状蛋白质三维结构中的碳分布程序

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

作者信息

Ekambaram Rajasekaran, Kannaiyan Akila, Marimuthu Vijayasarathy, Swaminathan Vinobha Chinnaiah, Renganathan Senthil, Perumal Ananda Gopu

机构信息

Department of Bioinformatics, School of Biotechnology and Health Sciences, Karunya University, Karunya Nagar, Coimbatore -641114, Tamil Nadu, India.

Department of Bioinformatics, Bishop Heber College, Trichy-620017, Tamil Nadu, India.

出版信息

Bioinformation. 2014 Mar 19;10(3):138-43. doi: 10.6026/97320630010138. eCollection 2014.

DOI:10.6026/97320630010138
PMID:24748753
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3974240/
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.

摘要

本文分析了蛋白质结构中碳的空间排列。特别地,比较了单个原子周围的碳含量。希望单个原子周围的碳含量遵循31.45%的原则。结果表明,球状蛋白质的原子遵循这一原则。对单体与二聚体的比较研究表明,碳以二聚体形式比以单体形式分布得更好。对固态与液态结构的类似研究表明,液态(核磁共振)结构比相应的固态(X射线)结构具有更好的碳分布。比较了纤维蛋白和毒素蛋白中的碳含量分布。纤维蛋白遵循碳含量分布原则。同时,它具有比球状蛋白更广泛的碳分布范围。毒素蛋白的碳含量分布异常。碳含量分布在决定蛋白质的结构和形状方面起着重要作用。希望有助于理解蛋白质的折叠和功能。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/caa7/3974240/8f312f33cc54/97320630010138F4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/caa7/3974240/3d619eeb1f50/97320630010138F1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/caa7/3974240/bef64c475015/97320630010138F2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/caa7/3974240/f18f491f1df0/97320630010138F3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/caa7/3974240/8f312f33cc54/97320630010138F4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/caa7/3974240/3d619eeb1f50/97320630010138F1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/caa7/3974240/bef64c475015/97320630010138F2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/caa7/3974240/f18f491f1df0/97320630010138F3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/caa7/3974240/8f312f33cc54/97320630010138F4.jpg

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本文引用的文献

1
CARd: Carbon distribution analysis program for protein sequences.CARd:用于蛋白质序列的碳分布分析程序。
Bioinformation. 2012;8(11):508-12. doi: 10.6026/97320630008508. Epub 2012 Jun 16.
2
The search for a spin crossover transition in small sized π-conjugated molecules: a Monte Carlo study.寻找小尺寸π共轭分子中的自旋交叉转变:蒙特卡罗研究。
J Phys Condens Matter. 2011 Aug 10;23(31):316001. doi: 10.1088/0953-8984/23/31/316001. Epub 2011 Jul 14.
3
CARBANA: Carbon analysis program forprotein sequences.CARBANA:蛋白质序列的碳分析程序。
Bioinformation. 2011 Feb 15;5(10):455-7. doi: 10.6026/97320630005455.
4
Backbones of folded proteins reveal novel invariant amino acid neighborhoods.折叠蛋白质的骨架揭示了新颖的不变氨基酸邻域。
J Biomol Struct Dyn. 2011 Feb;28(4):443-54. doi: 10.1080/073911011010524954.
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THE THREE DIMENSIONAL STRUCTURES OF PROTEINS.蛋白质的三维结构
Biophys J. 1964 Jan;4(1 Pt 2):SUPPL43-58. doi: 10.1016/s0006-3495(64)86925-3.
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Ferromagnetism of a graphite nodule from the Canyon Diablo meteorite.迪亚布罗峡谷陨石中石墨球粒的铁磁性。
Nature. 2002 Nov 14;420(6912):156-9. doi: 10.1038/nature01100.