Combining New Experimental and Informatic Tools for Protein Investigation and Engineering
09 Jan 2008 | Online Presentations | Contributor(s): Alan Friedman
The stability and activity of proteins is dependent on both the correct functioning and placement of individual amino acids and their interactions. Great attention has been paid to critical individual residues (generally revealed by their location in the active site and their conservation among homologous sequences). While the interactions between residues have been much less studied, they offer great potential for understanding how an entire protein functions and provide a source of variability (that is obviously not accessible to conserved residues) to engineer new and improved functions. I will present a series of new tools that we have been developing to computationally detect and analyze residue interactions and experimentally test and modify them with the twin goals of better understanding protein structure and function and of more efficiently generating novel variants with desirable properties.