Entropically driven self-assembly of Lysinibacillus sphaericus S-layer proteins analyzed under various environmental
Leonardo Maestri Teixeira1, Aaron Strickland, Sonny S Mark
1Department of Microbiology, Cornell University, Ithaca, NY 14853, USA.
Abstract:
S-Layer proteins are an example of bionanostructures that can be exploited in nanofabrication. In addition to their ordered structure, the ability to self-assembly is a key feature that makes them a promising technological tool. Here, in vitro self-assembly kinetics of SpbA was investigated, and found that it occurs at a rate that is dependent on temperature, its concentration, and the concentration of calcium ions and sodium chloride. The activation enthalpy (120.81 kJ . mol(-1)) and entropy (129.34 J . mol(-1) . K(-1)) obtained infers that the incorporation of monomers incurs in a net loss of hydrophobic surface. By understanding how the protein monomers drive the self-assembly at different conditions, the rational optimization of this process was feasible.
More Related Videos
08:29Au-Interaction of Slp1 Polymers and Monolayer from Lysinibacillus sphaericus JG-B53 - QCM-D, ICP-MS and AFM as Tools for Biomolecule-metal Studies
Published on: January 19, 2016
11:33Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
Published on: December 17, 2013
Related Concept Videos
Formation of Lipopolysaccharides
Outer Layers of the Cell Envelope
