Dissimilar sequence: similar structure of proteins

被引：0

作者：

Banach, Mateusz ^{[1
]}

Konieczny, Leszek ^{[2
]}

Roterman, Irena ^{[1
]}

机构：

[1] Jagiellonian Univ, Dept Bioinformat & Telemed, Med Coll, Lazarza 16, PL-31530 Krakow, Poland

[2] Jagiellonian Univ, Med Biochem, Med Coll, Kopernika 7, PL-31034 Krakow, Poland

来源：

BIO-ALGORITHMS AND MED-SYSTEMS | 2016年 / 12卷 / 03期

关键词：

hydrophobicity; protein structure; protein structure prediction; secondary structure;

D O I：

10.1515/bams-2016-0014

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Sequence-to-structure relation is one of the major objects of the analysis of protein folding problem. The pair of two small proteins (domains) of similar structure (beta-hairpin/alpha-helix/beta-hairpin) generated by the chains of similar length (about 60 amino acids) with very low sequence similarity (15%) is the object of the comparable analysis of 3D structure. The criterion for similarity estimation is the status of polypeptide chain with respect to the hydrophobic core structure. The fuzzy oil drop model is applied to reveal the differentiated status of fragments of the well-defined secondary structure. This analysis allows the interpretation of the structure in other than the geometric form as it is made based on secondary structure classification. The two compared highly similar proteins appear to be different with respect to the hydrophobic core structure.

引用

页码：117 / 121

页数：5

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