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Elastic Properties of Protein Structures
Figure 1: Proteins are made of universal secondary structures such as alpha-helices and beta-sheets. A coiled coil is a common protein structure made of bundled alpha-helices. Prof. Sun and colleagues showed that components of the protein structure have mechanical rigidity and can be described using continuum elastic theories. The theory is generic and can explain energy scales associated with conformational changes seen in proteins.
Description
Proteins are biological macromolecules that undergo large conformational dynamics. Predictions of conformational changes using all-atom simulations are computationally unfeasible. Prof. Sean Sun is developing coarse-grained elastic models to describe protein deformations. Together with postdoc Seungho Choe and Prof. Charles Wolgemuth at university of Connecticut, Prof. Sun showed that protein secondary structures have common structural properties and behave like simple mechanical objects. His model, for example, can predict bending and twisiting properties of proteins such as a coiled coil, shown in the figure. Other protein structures such as beta-sheets (lower figure) can be described similarly.
References
S. Choe and S. X. Sun, J. Chem. Phys. 122, 244912 (2005).
C. Wolgemuth and S. X. Sun, Phys. Rev. Lett. 97, 248101 (2006).
S. Choe and S. X. Sun, Biophys. J. 92, 1204-1214 (2007)