Thermodynamics, recombinant prion

Swietnicki W, Petersen RB, Gambetti P et al (1998) Familial mutations and the thermodynamic stability of the recombinant human prion protein. J Biol Chem 273 31048-31052... 

IV. Influence of Point Mutations Linked with Inherited Human Prion Diseases on the Thermodynamic Stability oe Recombinant PrP ... 

Fig. 6. Influence of amino acid replacements associated with inherited human TSEs on the thermodynamic stability of recombinant murine PrP( 121-231) at pH 7.0 and 22°C (Liemann and Glockshuber, 1999). The upper panel indicates the amino acid replacements in mature human PrP that are linked with inherited prion diseases in humans. The lower panel shows the difference between the free energy of unfolding of wild-type murine PrP(121-231) and the corresponding variant (AAG). The difference is defined such that a destabilization relative to the wild-type leads to positive values of AAG. The free energy of folding of wild-type murine PrP (121-231) at pH 7.0 and 22°C is -29.7 + 1.0 kj moPh The maximum error of the measured AAG values is + 2.6 kj moPh Variants of PrP( 121-231) that could not be expressed in a soluble form in the E. coli periplasm and formed periplasmic inclusion bodies are marked by asterisks. AAG for the replacement E200Khas also been determined for human PrP(90-231) with guani-dinium chloride as denaturant, and has a value of 4.1 + 2.6 kJ moP (Swietnicki et al., 1998, dashed bar frame).

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