Insights into protein stability in cell lysate by 19F NMR spectroscopy.
 

Insights into protein stability in cell lysate by 19F NMR spectroscopy.

Related Articles Insights into protein stability in cell lysate by 19F NMR spectroscopy.

Chembiochem. 2020 Aug 12;:

Authors: Welte H, Kovermann M

Abstract
In living organisms, protein folding and function take place in an inhomogeneous, highly crowded environment possessing a concentration of diverse macromolecules of up to 400*g/L. It has been shown that the intracellular environment has a pronounced effect on the stability, dynamics and function of the protein under study and has for this reason to be considered. However, most protein studies are neglecting the presence of these macromolecules. Consequently, we probe here the overall thermodynamic stability of cold shock protein B from* Bacillus subtilis *( Bs CspB) in cell lysate. We found that an increase in cell lysate concentration causes a monotonic increase in thermodynamic stability of* Bs CspB. This result strongly underlines the importance of considering the biological environment when inherent protein parameters shall be quantitatively determined. Moreover, we demonstrate that the targeted application of* 19 F NMR spectroscopy operates as an ideal tool utilized to protein studies performed in complex cellular surroundings.


PMID: 32786103 [PubMed - as supplied by publisher]



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