https://www.selleckchem.com/pr....oducts/hydroxychloro
Several protein monomers were unfolded using CIU, including multiple charge states of both cations and anions, and activation energies determined. ΔH⧧ and ΔS⧧ values are found to be correlated, leading to ΔG⧧ values that lie within a narrow range (∼70-80 kJ/mol) and vary more with charge state than with protein identity. ΔG⧧ is anticorrelated with charge density, highlighting the key role of Coulombic repulsion in gas-phase unfolding. Measured ΔG⧧ values are similar to those computed for proton transfer within small p
Like
Comment
Share
