ARTIFICIAL CHAPERONE FOR RODLIKE PROTEIN STRUCTURE

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DESCRIPTION (Adapted from abstract): The tail fiber attached to the base of bacteriophage T4 is a natural chemomechanical sensor which reacts mechanically to a chemical recognition signal, on the host cell surface, 150 nm away. Dr. Goldberg proposes to use the unique structural properties of the tail fiber as a biomimetic basis for redesign of the parts for self-assembly of new types of materials from the molecular level. Rational genetic redesign of these natural self-assembling components into protein kits for self-assembly of useful structures will require an accurate model of the tail fiber segments and their joints at atomic resolution. The investigators have devised a method for making small overlapping fragments of the protein rod in order to overcome the problem of a large axial ratio which makes both NMR analysis and crystal formation difficult, if not impossible. In addition, the relatively low molecular weight of the fragments will facilitate collection of useful NMR spectra. The overall goal is to solve the total structure of the T4 tail fiber. The atomic model of the rods and joints will serve to facilitate their redesign for more practical purposes for both medical and non-medical uses.