Structural and Functional Analysis of Hemoglobin and Serum Albumin Through Protein Long-Range Interaction Networks

被引：12
|
作者：
Paci, Paola [2 ]
Di Paola, Luisa [3 ]
Santoni, Daniele
De Ruvo, Micol [3 ]
Giuliani, Alessandro [1 ]
机构：
[1] Ist Super Sanita, Environm & Hlth Dept, I-00161 Rome, Italy
[2] CNR Inst Syst Anal & Comp Sci IASI, BioMathLab, I-00185 Rome, Italy
[3] Univ CAMPUS BioMed, Fac Engn, I-00128 Rome, Italy
来源：
CURRENT PROTEOMICS | 2012年 / 9卷 / 03期
关键词：
Allosteric effect; Bioinformatics; Computational biochemistry; Graph theory; Structural biology; Topological invariants; CONTACT NETWORK; IDENTIFICATION; PRINCIPLES; RESIDUES; BINDING; RATES; ORDER; SITE;
D O I：
10.2174/157016412803251815
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Long-range contacts in protein structures were demonstrated to be predictive of different physiological properties of hemoglobin and albumin proteins. Complex networks based approach was demonstrated to highlight basic principles of protein folding and activity. The presence of a natural scaling region ending at an approximate threshold of 120-150 residues shared by proteins of different size and quaternary structure was highlighted. This threshold is reminiscent of the typical size for a macromolecule to have a binding site sensible to environmental regulation.
引用
收藏
页码：160 / 166
页数：7
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