Never born proteins as a test case for ab initio protein structures prediction

被引:3
|
作者
Minervini, Giovanni [1 ]
Evangelista, Giuseppe [1 ]
Polticelli, Fabio [1 ]
Piwowar, Monika [2 ]
Kochanczyk, Marek [2 ,3 ]
Flis, Lukasz [3 ]
Malawski, Maciej [4 ]
Szepieniec, Tomasz [5 ]
Wisniowski, Zdzislaw [2 ]
Matczynska, Ewa [2 ,6 ]
Prymula, Katarzyna [2 ,7 ]
Roterman, Irena [2 ]
机构
[1] Univ Roma Tre, Dept Biol, I-00146 Rome, Italy
[2] Jagiellonian Univ, Dept Bioinformat & Telemed, Coll Med, Lazarza 16, PL-31530 Krakow, Poland
[3] Fac Phys Astron & Appl Informat, PL-30059 Krakow, Poland
[4] Inst Comp Sci AGH, PL-30059 Krakow, Poland
[5] Cadem Comp Ctr CYFRONET, PL-30950 Krakow, Poland
[6] Jagiellonian Univ, Fac Math & Informat, PL-30348 Krakow, Poland
[7] Jagiellonian Univ, Fac Chem, PL-30060 Krakow, Poland
关键词
ab initio; never born proteins; structure prediction; software; grid;
D O I
10.6026/97320630003177
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
The number of natural proteins although large is significantly smaller than the theoretical number of proteins that can be obtained combining the 20 natural amino acids, the so-called "never born proteins" (NBPs). The study of the structure and properties of these proteins allows to investigate the sources of the natural proteins being of unique characteristics or special properties. However the structural study of NPBs can also been intended as an ideal test for evaluating the efficiency of software packages for the ab initio protein structure prediction. In this research, 10.000 three-dimensional structures of proteins of completely random sequence generated according to ROSETTA and FOD model were compared. The results show the limits of these software packages, but at the same time indicate that in many cases there is a significant agreement between the prediction obtained.
引用
收藏
页码:177 / 179
页数:3
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