Novel microscale approaches for easy, rapid determination of protein stability in academic and commercial settings.

ABSTRACT: Chemical denaturant titrations can be used to accurately determine protein stability. However, data acquisition is typically labour intensive, has low throughput and is difficult to automate. These factors, combined with high protein consumption, have limited the adoption of chemical denaturant titrations in commercial settings. Thermal denaturation assays can be automated, sometimes with very high throughput. However, thermal denaturation assays are incompatible with proteins that aggregate at high temperatures and large extrapolation of stability parameters to physiological temperatures can introduce significant uncertainties. We used capillary-based instruments to measure chemical denaturant titrations by intrinsic fluorescence and microscale thermophoresis. This allowed higher throughp

SUBMITTER: Alexander CG 

PROVIDER: S-EPMC4332417 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature