STRUCTURAL DYNAMICS, STABILITY AND FOLDING OF PROTEINS
I. M. Kuznetsova,1 V. Forge,2 K. K. Turoverov 1
1 Institute of Cytology, RAS, St. Petersburg, Russia, and
2 Structural Biology of the Commissariat of Atomic Energy, Grenoble, France;
1 e-mail: kkt@mail.cytspb.rssi.ru
The present concepts of protein folding in vitro are reviewed. According to these concepts, amino acid sequence
of protein, which has appeared a result of evolutionary selection, determines the native structure of protein, the pathway of
protein folding, and the existence of free energy barrier between native and denatured states of protein. The latter means that
protein macromolecule can exist in either native or denatured state. And all macromolecules in the native state are identical but
for structural fluctuations due to Brownian motion of their atoms. Identity of all molecules in native state is of primary
importance for their correct functioning. The dependence of protein stability, which is measured as the difference between free
energy of protein in native and denatured states, on temperature and denaturant concentration is discussed. The modern approaches
characterizing transition state and nucleation are regarded. The role of intermediate and misfolded states in amorphous aggregate
and amyloid fibril formation is discussed.
Key words: protein folding, equilibrium protein dynamics, intermediate states, transition state, folding nucleus,
amyloid fibril, protein stability
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