CalFitter 2.0: Leveraging the power of singular value decomposition to analyse protein thermostability.

ABSTRACT: The importance of the quantitative description of protein unfolding and aggregation for the rational design of stability or understanding the molecular basis of protein misfolding diseases is well established. Protein thermostability is typically assessed by calorimetric or spectroscopic techniques that monitor different complementary signals during unfolding. The CalFitter webserver has already proved integral to deriving invaluable energy parameters by global data analysis. Here, we introduce CalFitter 2.0, which newly incorporates singular value decomposition (SVD) of multi-wavelength spectral datasets into the global fitting pipeline. Processed time- or temperature-evolved SVD components can now be fitted together with other experimental data types. Moreover, deconvoluted basis spectra

SUBMITTER: Kunka A 

PROVIDER: S-EPMC9252748 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature