By James F. Rusling
Examines motion pictures of biomolecules which could offer stable surfaces for catalyzing enzyme reactions, serve in biosensors and as biorecognition parts, mediate nanoparticle formation, and supply a uncomplicated for basic reports and purposes in biomedical units.
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Extra info for Biomolecular Films Design Function and Applications
Results suggested that binding of the protein to the BLM is strongly facilitated by electrostatic interactions between the cyt c and the BLM . Studies of thioredoxins (MW ca. 12,000) featuring disul¢de=dithiol redox sites at BLM electrodes indicated voltammetry was controlled by di¡usion of the proteins . 5 mg=mL) or phosphatidylcholine (50 mg=mL) including dioctadecyldimethylammonium bromide (DODAB) . Linear di¡usion control of the electrochemistry was found, and binding of the negative ferredoxins to the positive BLMs was largely electrostatic.
15), with polyions associated with head groups. Copyright 2003 by Marcel Dekker, Inc. All Rights Reserved. FIG. 15 Idealized model of a cast multibilayer surfactant film on a surface. Proteins incorporated into stacked lipid bilayers can lead to larger concentrations of redox sites per unit electrode area, resulting in larger voltammetric peaks. Self-assembled ¢lms are made by casting from aqueous vesicle dispersions containing the protein. Vesicles are closed globular structures. They are essentially water pools surrounded by a bilayer of lipid.
All Rights Reserved. Rotating-disk electrode voltammetry (RDV) employs an electrode which rotates at ¢xed speed to control mass transport to and from the electrode. In the absence of reactive substrate in solution, rotating the electrode has no e¡ect on the shape of a reversible thin protein ¢lm voltammogram because the electrochemistry is insensitive to mass transport external to the ¢lm. Addition of substrate to the solution provides catalytic steady-state voltammograms by RDV. The currentÀpotential curve now assumes a sigmoid shape (Fig.