Shibayama Naoya
Department of Physiology, Division of Biophysics, Jichi Medical University, 3311-1 Yakushiji, Shimotsuke, Tochigi, Japan.
FEBS Lett. 2008 Jul 23;582(17):2668-72. doi: 10.1016/j.febslet.2008.06.047. Epub 2008 Jun 30.
beta-Lactoglobulin is a predominantly beta-sheet protein that folds by forming excess alpha-helices within milliseconds. In this study, the refolding of beta-lactoglobulin was dramatically decelerated by entrapping in wet nanoporous silica gel matrices, and monitored on a time scale of minutes or hours by far-UV circular dichroism spectroscopy. Analysis of kinetics and transient spectra allowed to define the sequence of folding events that consist of alpha-helical formation, beta-sheet core formation, and alpha-to-beta transition. The results suggest that the initially formed alpha-helices, presumably including the native alpha-helix, help to guide the formation of the adjacent beta-sheet core.
β-乳球蛋白是一种主要由β-折叠组成的蛋白质，它能在几毫秒内通过形成过量的α-螺旋进行折叠。在本研究中，β-乳球蛋白的重折叠因被困在湿纳米多孔硅胶基质中而显著减速，并通过远紫外圆二色光谱在数分钟或数小时的时间尺度上进行监测。动力学和瞬态光谱分析有助于确定折叠事件的顺序，这些事件包括α-螺旋的形成、β-折叠核心的形成以及α-螺旋向β-折叠的转变。结果表明，最初形成的α-螺旋，可能包括天然α-螺旋，有助于引导相邻β-折叠核心的形成。
