AI Article Synopsis
- Thermal unfolding of proteins is crucial for drug screening, as it reveals how protein stability is influenced by interactions with ligands and substrates.
- The study utilizes synchrotron radiation circular dichroism to observe changes in protein secondary structure as they approach their melting point and assess how substrates affect this process.
- Differences in transition strengths were quantified using Landau free energy, revealing that mono-apo albumin exhibited the strongest transition, while lysozyme displayed the weakest transition, demonstrating the varying thermal behaviors of these proteins.
Article Abstract
Thermal unfolding of proteins is used extensively in screening of drug candidates because molecular interactions with ligands and substrates affect strongly protein stability, transition temperature, and cooperativity. We use synchrotron radiation circular dichroism to monitor the thermal evolution of secondary structure in proteins as they approach the melting point and the impact of substrate on their thermal behavior. Using Landau free energy expansion, we quantify transition strength and proximity to a critical point through the relative separation τ between the transition temperature T and the spinodal T, obtained from the equation of state. The weakest transition was observed in lysozyme with τ = -0.0167 followed by holo albumin with τ = -0.0208 with the strongest transition in monomeric apo albumin τ = -0.0242. A structural transition at 45 °C in apo albumin leads to a noncooperative melt with τ = -0.00532 and amyloidogenic increase in beta content.
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| http://dx.doi.org/10.1021/acs.jpcb.7b10643 | DOI Listing |
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