| 18593585 |
Shibayama N: Circular dichroism study on the early folding events of beta-lactoglobulin entrapped in wet silica gels. FEBS Lett. 2008 Jul 23;582(17):2668-72. 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. |
8(0,0,1,3) |