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Cooperativity calculation from protein structure

The value of 2(- 8gt can be calculated from standard values8 and a from the structure of the protein. A low value of mD N, compared with that calculated, indicates that the protein does not become highly unfolded on denaturation. The value of mD N thus provides a test for the degree of unfolding. A low value of mD N may also indicate that the denaturation process is occurring stepwise rather than in a single cooperative transition. [Pg.596]

On the other hand, the ratio obtained for pancreatic trypsin inhibitor calculated per mole of monomer unit is near 0.5, suggesting that the cooperative unit of this protein is a dimer. Thus, we see that it is not possible to generalize completely about the size of a cooperative unit from a knowledge of the protein structure, but that the comparison of these two enthalpy measurements provides insights into the presence of discrete units within the protein domain. [Pg.242]


See other pages where Cooperativity calculation from protein structure is mentioned: [Pg.28]    [Pg.119]    [Pg.312]    [Pg.68]    [Pg.170]    [Pg.346]    [Pg.465]    [Pg.232]    [Pg.93]    [Pg.275]    [Pg.199]    [Pg.545]    [Pg.62]    [Pg.169]    [Pg.544]   
See also in sourсe #XX -- [ Pg.335 , Pg.336 , Pg.337 , Pg.338 , Pg.339 ]




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