Section 72
Chapter 71,984

Insights into Protein Stability in Cell Lysate by 19 F NMR Spectroscopy

Welte, H.; Kovermann, M.

Chembiochem a European Journal of Chemical Biology 21(24): 3575-3579


ISSN/ISBN: 1439-7633
PMID: 32786103
DOI: 10.1002/cbic.202000413
Accession: 071983636

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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 neglect the presence of these macromolecules. Consequently, we probe here the overall thermodynamic stability of cold shock protein B from Bacillus subtilis (BsCspB) in cell lysate. We found that an increase in cell lysate concentration causes a monotonic increase in the thermodynamic stability of BsCspB. This result strongly underlines the importance of considering the biological environment when inherent protein parameters are quantitatively determined. Moreover, we demonstrate that targeted application of 19 F NMR spectroscopy operates as an ideal tool for protein studies performed in complex cellular surroundings.

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