cellulase has been researched along with dodecyloctaethyleneglycol-monoether* in 1 studies
1 other study(ies) available for cellulase and dodecyloctaethyleneglycol-monoether
Article | Year |
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Unfolding and partial refolding of a cellulase from the SDS-denatured state: From β-sheet to α-helix and back.
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 (C Topics: Calorimetry; Cellulase; Circular Dichroism; Kinetics; Polyethylene Glycols; Protein Conformation; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protein Unfolding; Scattering, Small Angle; Sodium Dodecyl Sulfate; Sordariales; Surface-Active Agents; X-Ray Diffraction | 2020 |