Publications by authors named "Enrico Corliano"
Article Synopsis
- The study investigates the impact of electrostatics on hydrogen exchange (HX) in the unfolded state of proteins, emphasizing its importance for understanding protein stability and dynamics.
- Using the disordered protein α-synuclein as a case study, researchers developed a method to calculate electrostatic potential along the protein chain, providing quantitative insights.
- Findings indicate that the C-terminal region of α-synuclein experiences a significant reduction in hydroxide concentration, which correlates with NMR spectroscopy data, suggesting that reduced HX is not due to hydrogen bonding or structural formation.
NMR spectroscopy is a pivotal technique to measure hydrogen exchange rates in proteins. However, currently available NMR methods to measure backbone exchange are limited to rates of up to a few per second. To raise this limit, we have developed an approach that is capable of measuring proton exchange rates up to approximately 10 s .
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