Symmetry and the energy landscapes of biomolecules - PubMed (original) (raw)
Symmetry and the energy landscapes of biomolecules
P G Wolynes. Proc Natl Acad Sci U S A. 1996.
Abstract
The role of symmetry in the folding of proteins is discussed using energy landscape theory. An analytical argument shows it is much easier to find sequences with funneled energy landscape capable of fast folding if the structure is symmetric. The analogy with phase transitions of small clusters with magic numbers is discussed.
Figures
Figure 1
The hemoglobin molecule is a tetramer α2β2. If the subunits were identical it would have 222 symmetry.
Figure 2
γ crystallin is a monomeric protein, but clearly its structure arises from gene duplication and drift. The two modules are similar but not identical in sequence.
Figure 3
A four-helix bundle molecule, cytochrome b562. The ribbon diagram actually exaggerates the dissymmetry because of the demanding algorithm for secondary structure assignment.
Figure 4
A protein folding funnel. The width of the funnel represents configurational entropy. The depth is the free energy of an individual configuration. The funnel is shown as anisotropic. The coordinate Q1, which destroys the symmetry rapidly, changes the energy, while Q2, preserving symmetry gives smaller energy changes.
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