This award is supported by the Major Research Instrumentation (MRI) and the Chemistry Instrumentation and Facilities (CRIF) programs. Professor Jaroslaw Drelich from Michigan Technological University and colleagues are acquiring an atomic force microscope (AFM). An AFM is a powerful tool to look at single molecules on a surface. It operates through an atomically sharp tip attached to an extremely soft cantilever that can sense forces at tiny atomic levels (pico-newton forces). Utilizing the forces between tip and a molecule, AFM can even be used to manipulate single molecules moving them to desired locations. Using this information, projects measure the mechanical strength of single covalent bonds. This can lead to practical applications, for example, preparing better quick-response and moisture-resistant smart adhesives. Adhesion forces between materials for civil engineering application can be investigated. The research enabled by the AFM will have broad impacts in areas such as health, energy, environment and national security, and even the economy. Faculty, postdoctoral researchers, graduate students, and undergraduate researchers in at least 16 research groups at Michigan Tech are trained to use this powerful instrument.
This atomic force microscope enhances research and education in areas by measuring van der Waals and magnetic forces between the tip and surface; the rupture force of non-covalent interactions between molecules and tip, and the scission force of covalent bonds in a molecule anchored between the tip and surface. Applications to projects include monitoring enzyme catalysis in real-time, and performing surface charge microscopy of biological cells. The microscope is used in the study of quick-response and moisture-resistant smart adhesives, and adhesion forces between materials for civil engineering applications. In other projects the shape and surface characteristics of atmospheric particles and atmospheric processing of black carbon are studied. The lattice structures of proteoglycan-galectin-3 cross-linked complexes are imaged and the ligand binding force of galectin-3 is measured.
