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Circular dichroism study on the early folding events of β‐lactoglobulin entrapped in wet silica gels
Author(s) -
Shibayama Naoya
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.06.047
Subject(s) - circular dichroism , folding (dsp implementation) , chemistry , beta lactoglobulin , biophysics , protein folding , chromatography , crystallography , whey protein , biochemistry , biology , electrical engineering , engineering
β‐Lactoglobulin is a predominantly β‐sheet protein that folds by forming excess α‐helices within milliseconds. In this study, the refolding of β‐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 α‐helical formation, β‐sheet core formation, and α‐to‐β transition. The results suggest that the initially formed α‐helices, presumably including the native α‐helix, help to guide the formation of the adjacent β‐sheet core.