APS March Meeting 2016
Volume 61, Number 2
Monday–Friday, March 14–18, 2016;
Baltimore, Maryland
Session A37: Phase Transitions and Self-Assembly in Biological Systems I
8:00 AM–11:00 AM,
Monday, March 14, 2016
Room: 340
Sponsoring
Units:
GSOFT DBIO
Chair: Jens Glaser, University of Michigan
Abstract ID: BAPS.2016.MAR.A37.4
Abstract: A37.00004 : Using Symmetry to Design Self-Assembling Protein Cages and Nanomaterials on the Mid-Nanometer Scale
8:36 AM–9:12 AM
Preview Abstract
Abstract
Author:
Todd Yeates
(UCLA Department of Chemistry and Biochemistry)
Self-assembling molecular structures having diverse cellular functions are
widespread in nature. Some of the largest and most sophisticated types are
built from many copies of the same or similar protein molecules arranged
following principles of symmetry. A long-standing engineering goal has been
to design novel protein molecules to self-assemble into geometrically
specific structures similar to the extraordinary structures that have
evolved in Nature. Practical routes to this goal have been developed by
using ideas in symmetry to articulate the minimum design requirements for
achieving various types of symmetric architectures, including cages,
extended two-dimensional layers, and three-dimensional crystalline
materials. The key requirement is that two distinct self-associating
interfaces, each conferring one element of rotational symmetry, have to be
engineered into the protein molecule (or molecules), following particular
geometric specifications. The main principle is that combining two separate
symmetry elements into a single molecular entity produces a molecule that
necessarily assembles into an architecture dictated by a symmetry group that
is the product of the two simpler contributing symmetries. Recent
experiments have demonstrated success using a variety of symmetry-based
strategies. Strategic variations are emerging that differ from each other
with respect to biophysical features such as flexibility vs rigidity in the
assembled structures, and with respect to design aspects such as whether the
protein interfaces are inherited from natural oligomeric proteins or are
designed de novo by advanced computational methods. The success of these
strategies has been proven by determining crystal structures of several
giant, self-assembling protein cages and clusters (10-25 nm in diameter),
created by design. The ability to create sophisticated supramolecular
structures from designed protein subunits opens the way to broad
applications in synthetic biology and nanotechnology.
To cite this abstract, use the following reference: http://meetings.aps.org/link/BAPS.2016.MAR.A37.4