Solid-state synthesis and mechanical unfolding of polymers of T4 lysozyme.

ABSTRACT: Recent advances in single molecule manipulation methods offer a novel approach to investigating the protein folding problem. These studies usually are done on molecules that are naturally organized as linear arrays of globular domains. To extend these techniques to study proteins that normally exist as monomers, we have developed a method of synthesizing polymers of protein molecules in the solid state. By introducing cysteines at locations where bacteriophage T4 lysozyme molecules contact each other in a crystal and taking advantage of the alignment provided by the lattice, we have obtained polymers of defined polarity up to 25 molecules long that retain enzymatic activity. These polymers then were manipulated mechanically by using a modified scanning force microscope to characterize the

SUBMITTER: Yang G 

PROVIDER: S-EPMC26629 | biostudies-literature | 2000 Jan

REPOSITORIES: biostudies-literature