Brylinski Michal, Konieczny Leszek, Roterman Irena
Department of Bioinformatics and Telemedicine, Collegium Medicum, Jagiellonian University, Kopernika 17, 31-501 Krakow, Poland.
Int J Bioinform Res Appl. 2007;3(2):234-60. doi: 10.1504/IJBRA.2007.013605.
The model for protein folding (in silico) simulation is presented. Three steps have been implemented: early stage folding based on the backbone conformation; hydrophobic collapse based on the fuzzy-oil-drop model; aim-oriented structure modification by the function-related ligand. The model has been verified taking alpha and beta haemoglobin chains as examples to fold them in two different conditions: with and without haem being present in the folding environment. The presence of haem and its participation in the folding simulation led to the structure more similar to the crystal one. It suggests that the haem presence directs the folding process towards the function-related structure.
本文提出了蛋白质折叠（计算机模拟）模型。该模型实现了三个步骤：基于主链构象的早期折叠；基于模糊油滴模型的疏水塌缩；通过功能相关配体进行目标导向的结构修饰。以α和β血红蛋白链为例，在两种不同条件下对该模型进行了验证：折叠环境中存在或不存在血红素。血红素的存在及其参与折叠模拟导致结构更类似于晶体结构。这表明血红素的存在将折叠过程导向与功能相关的结构。
