[Establishment of fundamentals for protein research. Stabilization of protein].
Proteins are usually in an equilibrium between the folded and the unfolded state. Therefore, for the stabilization of proteins against reversible denaturation, the free energy change for the unfolding should be increased by stabilizing the folded state by lowering the energy level of the folded state or by destabilizing the unfolded state by raising the energy level of the unfolded state. On the other hand, various processes can be coupled with the unfolded state of proteins. For example, protease digestion of proteins at physiological temperature may be one of such processes. The process would lead to an irreversible denaturation. For the stabilization of proteins against the irreversible denaturation coupled with the unfolded state, a kinetic stabilization is important, that is, the activation free energy for the unfolding should be increased. Methods for the kinetic stabilization were discussed. Finally, the irreversible chemical deterioration of proteins was considered.
Imoto
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Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka, Japan.
D000818:Animals; D004355:Drug Stability; D011487:Protein Conformation; D011489:Protein Denaturation; D015202:Protein Engineering; D017510:Protein Folding; D011506:Proteins
D011506:Proteins