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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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