[The effect of external restrictions on the stability of the globular state]

The delta Td changes of heat denaturation temperature for globule proteins were estimated, for a globule inserted into pores of a inert carrier, that limits the conformational set of the denatured chain. Based on calculations for a grated selfintercepted chain in a slit-like pore, with no interactions with the pore walls, functions of delta Td depending on the rigidity of the unfolded chain, its length and pore sizes were determined. For alpha-chymotrypsin in polyacrylamide gels the estimated delta Td was of several degrees. The possible influence of the pore form and intramolecular interactions for a denatured chain on the value of the stabilizing effect is discussed.