Alternative Hydrophobic Core in Proteins—The Effect of Specific Synergy

Symmetry

Leszek Konieczny¹  Irena Roterman²  Magdalena Ptak-Kaczor²  Mateusz Banach²  Katarzyna Stapor³  Piotr Fabian³ 

[1] Chair of Medical Biochemistry, Medical College, Jagiellonian University, Kopernika 7, 31-034 Krakow, Poland;Department of Bioinformatics and Telemedicine, Medical College, Jagiellonian University, Lazarza 16, 31-530 Krakow, Poland;Institute of Computer Science, Silesian University of Technology, Akademicka 16, 44-100 Gliwice, Poland;

关键词: homology;    protein structure;    hydrophobic core;    hydrophobicity;    synergy;    spherical symmetry;   

DOI  :  10.3390/sym12020273

来源: DOAJ

【 摘 要 】

Proteins with a high degree of sequence similarity representing different structures provide a key to understand how protein sequence codes for 3D structure. An analysis using the fuzzy oil drop model was carried out on two pairs of proteins with different secondary structures and with high sequence identities. It has been shown that distributions of hydrophobicity for these proteins are approximated well using single 3D Gaussian function. In other words, the similar sequences fold into different 3D structures, however, alternative structures also have symmetric and monocentric hydrophobic cores. It should be noted that a significant change in the helical to beta-structured form in the N-terminal section takes places in the fragment much preceding the location of the mutated regions. It can be concluded that the final structure is the result of a complicated synergy effect in which the whole chain participates simultaneously.

【 授权许可】

Unknown