Abstract
This chapter contains tabulated data of Gibbs energy changes (ΔGunf) enthalpy changes (ΔHunf), and heat capacity changes (ΔCp, unf) associated with protein unfolding. The data are relevant for various purposes, ranging from practical applications to theoretical considerations on structure stabilizing forces. For the diversity of these aspects the reader is referred to reviews and monographs [1–17].
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Abbreviations
- Kunf :
-
equilibrium constant for protein unfolding
- K0 unf :
-
equilibrium constant for protein unfolding at standard conditions (zero denaturant concentration)
- K:
-
denaturant binding constant
- a:
-
denaturant activity
- Δn:
-
preferential interaction parameter
- ΔGunf :
-
Gibbs energy change for protein unfolding
- ΔG 0unf :
-
Gibbs energy change for protein unfolding at standard conditions (zero denaturant concentration)
- ΔG resunf :
-
Gibbs energy change for protein unfolding per mole of residues
- ΔHunf :
-
enthalpy change for protein unfolding
- ΔH calunf :
-
enthalpy change for protein unfolding obtained by calorimetry
- ΔH vHunf :
-
enthalpy change for protein unfolding obtained by van’t Hoff treatment
- ΔCp,unf :
-
heat capacity change for protein unfolding
- T:
-
temperature
- Ttrs :
-
transition temperature (referring to LlGunf=O)
- N, X, U:
-
native, intermediate and unfolded states of protein
- Ki :
-
rate constant
- vH:
-
equilibrium treatment by means of the van’t Hoff equation
- *:
-
the value was calculated using other thermodynamic quantities in the original paper
- DSC:
-
differential scanning calorimetry
- GuHCl:
-
guanidine hydrochloride
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Pfeil, W. (1986). Unfolding of Proteins. In: Hinz, HJ. (eds) Thermodynamic Data for Biochemistry and Biotechnology. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71114-5_13
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