Protein Cages as Nanomaterials
Nature has evolved active bio-architectures that are both dynamic and responsive individually
as well as collectively when assembled into hierarchical structures. In fact, dynamic
protein regions are responsible for biological mineral nucleation, surface recognition,
chemical reactivity, and targeting. The concerted protein motion that is part of a
multi-component biomolecular complex is rarely obvious from the high resolution three-dimensional
structure. Protein function is intimately connected to dynamics and therefore knowledge
of the frequency, range, and coordination of motion by supramolecular complexes is
critical to understanding function and the development of bio-inspired nanomaterials.
The extremely large size and icosahedral architecture of virus capsids limit the use
of many standard techniques for studying protein motion such as NMR and FRET. To overcome
these problems, we employ an array of biophysical techniques to study the solution
phase behavior of viruses. Kinetic hydrolysis, an approach being developed in our
lab, is a straight-forward and powerful technique for identifying the dynamic regions
within a single protein or in the context of a multi-component complex. Protein dynamics
is being investigated at three levels: the dynamics of the subunit, the assembled
cage architecture, and the dynamics associated with higher order particle/particle
and surface/particle interactions. The long-term goal of this effort is to understand
dynamics of the nanoparticle/cage system at each distinct level of complexity so that
the underlying mechanism of nucleation, recognition, and functionality can be elucidated
and exploited. This work is being conducted in collaboration with other research groups
in the Center for Bio-Inspired Nanomaterials.
Graduate students: Navid Movahed and Vamseedhar Rayaprolu.
Analytical, Biochemistry, Biophysical, Protein Chemistry, Structure