The rational design of allosteric interactions in a monomeric protein and its applications to the construction of biosensors.

ABSTRACT: Rational protein design is an emerging approach for testing general theories of structure and function. The ability to manipulate function rationally also offers the possibility of creating new proteins of biotechnological value. Here we use the design approach to test the current understanding of the structural principles of allosteric interactions in proteins and demonstrate how a simple allosteric system can form the basis for the construction of a generic biosensor molecular engineering system. We have identified regions in Escherichia coli maltose-binding protein that are predicted to be allosterically linked to its maltose-binding site. Environmentally sensitive fluorophores were covalently attached to unique thiols introduced by cysteine mutations at specific sites within these regi

SUBMITTER: Marvin JS 

PROVIDER: S-EPMC20728 | biostudies-literature | 1997 Apr

REPOSITORIES: biostudies-literature