Mohanty Sandipan, Hansmann U H E
John von Neumann Institut für Computing, Forschungszentrum Jülich, Jülich D-52425, Germany.
J Chem Phys. 2007 Jul 21;127(3):035102. doi: 10.1063/1.2753835.
Using the 28 residue betabetaalpha protein FSD-EY as a target system, we examine correction terms for the ECEPP/3 force field. We find an increased probability of formation of the native state at low temperatures resulting from a reduced propensity to form alpha helices and increased formation of beta sheets. Our analysis of the observed folding events suggests that the C-terminal helix of FSD-EY is much more stable than the N-terminal beta hairpin and forms first. The hydrophobic groups of the helix provide a template which promotes the formation of the beta hairpin that is never observed to form without the helix.
以28个残基的ββα蛋白FSD-EY作为目标系统，我们检验了ECEPP/3力场的校正项。我们发现，由于形成α螺旋的倾向降低以及β折叠的形成增加，在低温下天然态形成的概率增加。我们对观察到的折叠事件的分析表明，FSD-EY的C端螺旋比N端β发夹稳定得多，且首先形成。螺旋的疏水基团提供了一个模板，促进了β发夹的形成，而没有螺旋时从未观察到β发夹的形成。
