Open Access. Powered by Scholars. Published by Universities.®
- Discipline
-
- Amino Acids, Peptides, and Proteins (1)
- Analytical, Diagnostic and Therapeutic Techniques and Equipment (1)
- Biochemical and Biomolecular Engineering (1)
- Biochemistry (1)
- Biochemistry, Biophysics, and Structural Biology (1)
-
- Bioelectrical and Neuroengineering (1)
- Biological Engineering (1)
- Biological Phenomena, Cell Phenomena, and Immunity (1)
- Biology and Biomimetic Materials (1)
- Biomaterials (1)
- Biomedical (1)
- Biomedical Engineering and Bioengineering (1)
- Biophysics (1)
- Biotechnology (1)
- Cellular and Molecular Physiology (1)
- Chemical Engineering (1)
- Chemical and Pharmacologic Phenomena (1)
- Chemistry (1)
- Complex Fluids (1)
- Complex Mixtures (1)
- Condensed Matter Physics (1)
- Digestive, Oral, and Skin Physiology (1)
- Dynamics and Dynamical Systems (1)
Articles 1 - 2 of 2
Full-Text Articles in Nanotechnology
Frontiers In The Self-Assembly Of Charged Macromolecules, Khatcher O. Margossian
Frontiers In The Self-Assembly Of Charged Macromolecules, Khatcher O. Margossian
Doctoral Dissertations
The self-assembly of charged macromolecules forms the basis of all life on earth. From the synthesis and replication of nucleic acids, to the association of DNA to chromatin, to the targeting of RNA to various cellular compartments, to the astonishingly consistent folding of proteins, all life depends on the physics of the organization and dynamics of charged polymers. In this dissertation, I address several of the newest challenges in the assembly of these types of materials. First, I describe the exciting new physics of the complexation between polyzwitterions and polyelectrolytes. These materials open new questions and possibilities within the context …
Controlling Myosin’S Function Via Interactions Between The Substrate And The Active Site, Mike K. Woodward
Controlling Myosin’S Function Via Interactions Between The Substrate And The Active Site, Mike K. Woodward
Doctoral Dissertations
Molecular motors, such as myosin, have evolved to transduce chemical energy from ATP into mechanical work to drive essential cellular processes, from muscle contraction to vesicular transport. Dysfunction in these motors is a root cause of many pathologies necessitating the application of intrinsic control over molecular motor function. We hypothesized that altering the myosin’s energy substrate via minor positional changes to the triphosphate portion of the molecule will allow us to control the protein and affect its in vitro function. We utilized positional isomers of a synthetic non-nucleoside triphosphate, azobenzene triphosphate, and assessed whether myosin’s force- and motion-generating capacity could …