Shear-induced unfolding of lysozyme monitored in situ.

ABSTRACT: Conformational changes due to externally applied physiochemical parameters, including pH, temperature, solvent composition, and mechanical forces, have been extensively reported for numerous proteins. However, investigations on the effect of fluid shear flow on protein conformation remain inconclusive despite its importance not only in the research of protein dynamics but also for biotechnology applications where processes such as pumping, filtration, and mixing may expose protein solutions to changes in protein structure. By combining particle image velocimetry and Raman spectroscopy, we have successfully monitored reversible, shear-induced structural changes of lysozyme in well-characterized flows. Shearing of lysozyme in water altered the protein's backbone structure, whereas similar sh

SUBMITTER: Ashton L 

PROVIDER: S-EPMC2712145 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature