AI Article Synopsis

  • The study introduces 2D NMR spectroscopy as a new method to analyze protein unfolding, specifically focusing on individual residue resonances rather than just an overall average.
  • The researchers examined the Yfh1 protein, which can undergo both cold and heat denaturation, to explore how individual resonances provide unique insights into their stability.
  • Findings reveal that individual stability curves can highlight differences between cold and heat denaturation processes, suggesting that these unfolding mechanisms are fundamentally different.

Article Abstract

Most techniques allow detection of protein unfolding either by following the behaviour of single reporters or as an averaged all-or-none process. We recently added 2D NMR spectroscopy to the well-established techniques able to obtain information on the process of unfolding using resonances of residues in the hydrophobic core of a protein. Here, we questioned whether an analysis of the individual stability curves from each resonance could provide additional site-specific information. We used the Yfh1 protein that has the unique feature to undergo both cold and heat denaturation at temperatures above water freezing at low ionic strength. We show that stability curves inconsistent with the average NMR curve from hydrophobic core residues mainly comprise exposed outliers that do nevertheless provide precious information. By monitoring both cold and heat denaturation of individual residues we gain knowledge on the process of cold denaturation and convincingly demonstrate that the two unfolding processes are intrinsically different.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7612453PMC
http://dx.doi.org/10.1038/s42004-021-00566-3DOI Listing

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