How does a biopolymer (protein) fold into a unique 3D structure?
In: Vestnik Moskovskogo universiteta. Seria 16. Biologia, Band 78, Heft №3s, 2023, S. 9-12
The current state of the problem of folding proteins and other biopolymers is discussed. The
concept of a multidimensional potential energy surface and a free energy surface for linear
polymers is detailed, taking into account the topology of the configuration space and the
presence of symmetry elements with respect to the permutation of identical monomer units. The
presence of kinematic bonds for conformational movements in a viscous medium leads to a
tendency to form helical structures of linear polymers. The dynamic effects of viscosity also lead
to an almost uniform distribution of energy dissipation rates over the chain nodes. The
combination of potential energy surface topography and viscosity effects provides a physical
basis for the development of the theory of folding in the direction of interpreting various
experimental observations and elucidating the principles for the formation of an amino acid
code for 3D protein structures. The relationship between the denaturation temperature of the
folded state of the biopolymer and the energy of non-valent interactions between monomers in
the chain is analyzed.