Jose M. Sanchez-Ruiz

TL;DR: It is shown that ligand and protein concentration effects on transitions corresponding to situation C (strongly rate-limited transitions) are similar to those predicted by equilibrium thermodynamics for simple reversible unfolding models.

TL;DR: It is shown that the proposed model may be considered as being one particular case of that proposed by Lumry and Eyring, where N in equilibrium D----I is the native state, D the unfolded one, and I a final state, irreversibly arrived at from D.

TL;DR: The experimental evidence supporting widespread kinetic stabilization of proteins is summarized, the role of natural selection in determining this feature is discussed, possible molecular mechanisms responsible for kinetic stability are described and the relation between kinetic destabilization and protein misfolding diseases is highlighted.

TL;DR: This work investigated the thermal unfolding of the peripheral subunit binding domain from Escherichia coli's 2-oxoglutarate dehydrogenase multienzyme complex with a combination of spectroscopic techniques and calorimetry, and identified BBL as a downhill-folding protein.

TL;DR: The results indicate that substrate conformational changes may be important in the regulation of Trx activity under conditions of oxidative stress and mechanical injury, such as those experienced in cardiovascular disease, and support the view that the Trx active site regulates the geometry of the participating sulphur atoms with sub-ångström precision to achieve efficient catalysis.