Biomolecules, like proteins, are often marginally stable, with a rigid core that defines the three dimensional structure and flexible regions which are associated with biological function. Using constraint theory, we show how the flexible regions can be determined which then facilitates the computation of the low frequency motions. Various applications of this approach will be discussed – protein unfolding/folding pathways, enzyme activity, drug design, protein complexes and viral capsids.
The work reviewed here has been done in collaboration with B. Hespenheide, D.J. Jacobs, L. A. Kuhn, M. Lei, A.J. Rader, W. Whiteley and M. I. Zavodszky and is supported by the DOE, NSF and NIH.
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