Dodson Charlotte A, Arbely Eyal
MRC Centre for Protein Engineering, Hills Road, Cambridge CB2 0QH, UK; Molecular Medicine, National Heart & Lung Institute, Imperial College London, SAF Building, London SW7 2AZ, UK.
MRC Centre for Protein Engineering, Hills Road, Cambridge CB2 0QH, UK.
FEBS Lett. 2015 Jul 8;589(15):1740-7. doi: 10.1016/j.febslet.2015.06.002. Epub 2015 Jun 11.
The SAP domain from the Saccharomyces cerevisiae Tho1 protein is comprised of just two helices and a hydrophobic core and is one of the smallest proteins whose folding has been characterised. Φ-value analysis revealed that Tho1 SAP folds through a transition state where helix 1 is the most extensively formed element of secondary structure and flickering native-like core contacts from Leu35 are also present. The contacts that contribute most to native state stability of Tho1 SAP are not formed in the transition state.
酿酒酵母Tho1蛋白的SAP结构域仅由两个螺旋和一个疏水核心组成，是已被表征其折叠过程的最小蛋白质之一。Φ值分析表明，Tho1 SAP通过一个过渡态进行折叠，其中螺旋1是二级结构中形成最广泛的元件，并且还存在来自Leu35的类似天然态的闪烁核心接触。对Tho1 SAP天然态稳定性贡献最大的接触在过渡态中并未形成。
