A retinal protein complex known as bacteriorhodopsin was investigated by atomic force microscopy to determine whether it possessed qualities that make it favorable for use as a nanoscale actuator or sensor. Bacteriorhodopsin was tested in different forms (layered 2D crystals and disordered clusters), in three different environments (dry air, humidified air, and water), and on a number of surfaces (glass, charged glass, PDAC coated glass, and Gelpak TM adhesive surfaces). Bacteriorhodopsin was not observed to undergo any molecular motion.

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Waddell, Jack Neel

Publisher

• Worcester Polytechnic Institute

Identifier

• 03D054M

Advisor

• Burnham, Nancy A.

Year

• 2003

Date created

• 2003-01-01

Resource type

• Major Qualifying Project

Major

• Physics

Rights statement

• In Copyright