An alternative approach in the structure-based predictions of the thermodynamics of protein unfolding

Stabilizing an amyloidogenic λ6 light chain variable domain

“…where T is 298 K, and DC p is the change in heat capacity associated with unfolding, calculated theoretically according to the method described by Milardi et al [27].…”

Principles, approaches, and challenges for predicting protein aggregation rates and shelf life

“…[151][152][153] Independent of how Dc p,un is obtained, typical experimental values range from 1 to 4 kcal mol À1 K À1 for globular proteins or similarly sized subdomains of larger proteins. 62 Considering this, Figure 3 illustrates that if one is extrapolating over only a relatively small temperature range ($5-108C) and can tolerate significant error in k obs or t shelf (a factor of 2 or more), then an Arrhenius extrapolation may be sufficiently accurate.…”

Mutational and genetic determinants of λ6 light chain amyloidogenesis

“…where T is 298 K and DC p is the heat capacity change associated with unfolding and is calculated according to the method described by Milardi et al [42].…”

“…DG 25°C was calculated as described by Pace and colleagues [41]. T m , DH m and DS m were calculated from the plot of DG versus T. DC p was calculated as described by Milardi et al [42]. DDG is the cumulative free energy change relative to 6aJL2-R25G:…”

“…The midpoint temperature (T m ) and enthalpy (DH m ) and entropy (DS m ) changes at temperature T m were determined from a DG versus T plot. The value of DG at room temperature (25°C) was calculated according to [41] DGðTÞ ¼ DH m ð1 À T=T m Þ À DC p ½ðT m À TÞ þ TlnðT=T m Þ (3) where T is 298 K and DC p is the heat capacity change associated with unfolding and is calculated according to the method described by Milardi et al [42].…”