How Does a Biopolymer (Protein) Fold into a Unique 3D Structure?

The current state of the protein folding problem and other biopolymers folding is discussed. The concept of a multidimensional potential energy surface and free energy surface for linear polymers is detailed, taking into account the topology of the configuration space and the presence of symmetry el...

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Bibliographic Details
Published in:Moscow University biological sciences bulletin 2023-12, Vol.78 (Suppl 1), p.S5-S8
Main Author: Shaitan, K. V.
Format: Article
Language:English
Subjects:
Amino acids
Biochemistry
Biomedical and Life Sciences
Biopolymers
Cell Biology
Denaturation
Free energy
Life Sciences
Monomers
Plant Sciences
Protein folding
Proteins
Review
Viscosity
Zoology
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Summary:The current state of the protein folding problem and other biopolymers folding is discussed. The concept of a multidimensional potential energy surface and 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 rearrangement of identical monomer units. The presence of kinematic connections for conformational movements in a viscous medium leads to a tendency for the formation of helical structures of linear polymers. The dynamic effects of viscosity also lead to an almost uniform distribution of energy dissipation rates across the nodes of the chain. The combination of free energy surface topography and viscosity effects provides a physical basis for advancing folding theory toward interpreting a variety of experimental observations and elucidating principles of amino acid code formation for 3D protein structures. The relationship between the denaturation temperature of the folded state of the biopolymer and the energy of nonvalent interactions between monomers in the chain is analyzed.
ISSN:0096-3925
1934-791X
DOI:10.3103/S009639252370013X