Unfolding and partial refolding of a cellulase from the SDS-denatured state: From β-sheet to α-helix and back

• Published in: Biochimica et biophysica acta. General subjects Vol. 1864; no. 1; p. 129434
• Main Authors: Rasmussen, Helena Ø., Enghild, Jan J., Otzen, Daniel E., Pedersen, Jan Skov
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 01.01.2020
• Subjects: beta-lactoglobulin; calorimetry; Cellulase; Charge neutralisation; circular dichroism spectroscopy; detergents; endo-1,4-beta-glucanase; enzyme activity; gel chromatography; Humicola insolens; industry; micelles; neutralization; nonionic surfactants; Refolding; SAXS; small-angle X-ray scattering; Surfactant; titration; ultraviolet radiation; Unfolding; Unfolding; Charge neutralisation; Surfactant; Cellulase; Refolding; SAXS
• ISSN: 0304-4165; 1872-8006; 1872-8006
• DOI: 10.1016/j.bbagen.2019.129434

Globular proteins are typically unfolded by SDS to form protein-decorated micelle-like structures. Several proteins have been shown subsequently to refold by addition of the nonionic surfactant octaethylene glycol monododecyl ether (C12E8). Thus SDS converts β-lactoglobulin, which has mainly β-sheet...