表面固定されたタンパク質のナノ力学

抄録

Proteins and polypeptides were first covalently immobilized on a solid surface and then extended by a tensile force applied at the two ends of the polymer chain. The method consisted of introducing cysteine residues at N-and C-termini of protein molecules and covalently immobiling them on an amino-silanized surface of a crystalline silicon wafer. The other end of the protein molecule was cross-linked to a functionalized AFM (atomic force microscope) tip with covalent cross-linkers. The relationship between the tensile force and the extension length of the molecule was measured using the force curve mode of AFM. Results obtained with a polyglutamic acid that takes helical conformation in acidic and random coil state in neutral and alkaline media is described. Also the relationships measured with β-sheet globular protein, carbonic dehydratase are given.