Nguyen Houbi, Jäger Marcus, Kelly Jeffery W, Gruebele Martin
J Phys Chem B. 2005 Aug 18;109(32):15182-6. doi: 10.1021/jp052373y.
Recent experimental studies have shown that alpha-helical proteins can approach the folding "speed limit", where folding switches from an activated to a downhill process in free energy. beta-sheet proteins are generally thought to fold more slowly than helix bundles. However, based on studies of hairpins, folding should still be able to approach the microsecond time scale. Here we demonstrate how the hPin1 WW domain, a triple-stranded beta-sheet protein with a sharp thermodynamic melting transition, can be engineered toward the folding "speed limit" without a significant loss in thermal denaturation cooperativity.
最近的实验研究表明，α-螺旋蛋白能够接近折叠的“速度极限”，即在此处折叠在自由能方面从活化过程转变为下坡过程。β-折叠蛋白通常被认为比螺旋束折叠得更慢。然而，基于对发夹结构的研究，折叠仍应能够接近微秒时间尺度。在此，我们展示了hPin1 WW结构域，一种具有尖锐热力学解链转变的三链β-折叠蛋白，如何能够在不显著损失热变性协同性的情况下，朝着折叠的“速度极限”进行改造。
