Description:

It is well-known that the core regions of proteins are densely packed. Prior studies have even suggested that the packing fraction of protein cores can approach that for metals. Our recent studies suggest that the structural and mechanical properties of protein cores can be accurately modeled using jammed packings of amino acid-shaped particles without backbone constraints. We have shown that the packing fraction of jammed packings of amino acid-shaped particles is ~0.56, which agrees with that for completely buried amino acids in protein crystal structures. We have also demonstrated that the local and percolating void space of protein cores is identical to that for jammed packings of amino acid-shaped particles. We can use these insights to tackle several outstanding problems in computational protein design. For example, we can predict the changes in the side chain dihedral angles in response to single core amino acid mutations. In current work, we are investigating changes in the backbone dihedral angles in response to amino acid mutations, and in this case, comparisons of protein structures obtained using solution-NMR and x-ray crystallization are important.

Seminar Speaker: Corey S. O'Hern, Yale University

 Host: Motter

Keywords: Physics, Astronomy, Seminar, Colloquium