| Popis: |
The interaction of a protein with water can be considered to be similar in nature to that of a multi-substituted alkane. The energies involved in the movement out of water of such compounds have been estimated by a number of methods 1 , 2 , 3 , 4 , 5 , 6 , 7 , 8 , 9 , 10 , 11 , 12 , 13 , 14 , 15 , but without regard to the individual lone pair basicities, electrostatic and hydrophobicity contributions. Further refinement of the solvation analysis methodology developed previously [16] , provides, we believe, a potentiality for new insights into the energetics of protein folding and protein-cofactor/ substrate/ drug interactions. |
