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The Optima AUC* Analytical Ultracentrifuge
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The Optima AUC* is a versatile method to characterize the hydrodynamic behaviors of biological (and other samples) in solution. It is based on the principles of sedimentation - the passage down a tube in a centrifugal field. The Optima AUC* instrument can detect samples based on UV-vis absorbance as well as refractive index.

Unique Advantages of AUC* Analysis

  • Fully native state analysis: no substrate/matrix interaction
  • No calibration standards required: results obtained from first principles
  • Large dynamic range: characterize anything from peptides to viruses and nanoparticles

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Register for this AUC* User Group Event at the Minnesota Nano Center by choosing one option below, clicking on the button and then filling out the registration form:

You only need to select one option. The event is in-person. However, you may choose to register to attend in-person or virtually; but not both. It's important for us to account for the number of participants who will be attending the event in-person to reserve the proper number of seats in the meeting room.
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AUC* Applications

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fmna-liqh-biomek-i-7-22-02-img-3345x3559.png
Nanoparticles
  • Core size determination
  • Drug payload
Quantum Dots
RNA Aptamers
Polysaccharides
Viral Vectors for Gene Therapy
  • Empty vectors versus full capsids
Membrane Protein-Lipid Interactions
Protein-Protein Interactions
  • Fusion proteins (YFP, GFP, SNAP)
  • Heme proteins
  • Flavins
  • Metalloproteins
Protein-Nucleic Acid Interactions
  • Recombinases
  • Terminases
  • ATPases
and many more!
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More Questions? More Answers

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In one experiment, AUC* technology can provide more answers to critical questions than any other comparable technique:

  • Shape: How spherical is my protein?
  • Diameter: What’s the size of my particle?
  • Mass: What’s the molecular weight of my protein or complex in solution?
  • Stoichiometry: How many subunits comprise my protein?
  • Purity: Are there other particles in my sample?
  • Formulation: How does my protein behave in this buffer?
  • Heterogeneity: Is my protein bound to other molecules, and what’s the configuration of the complex?
  • Aggregation: Is my protein still in a usable form? Should I expect an immune response with my drug formulation?
  • Association: Does my protein associate and/or dissociate with other proteins?
  • Conformation: Does the conformation of my protein change upon binding to a ligand?


Questions to understand the behavior of macromolecules** :

  • "Is the sample homogeneous? i.e., is it pure? or is there more than one type of molecule present?"
  • "If there is a single component, what is the molecular weight?"
  • "If more than one type of molecule is present, can the molecular weight distribution of the sample be obtained?"
  • "Can an estimate be obtained of the size and shape of the particles of the macromolecule? Are the molecules compact and spherical, like the globular proteins; long, thin and rod-like, like sections of DNA; or are they highly expanded and full of solvent, like many organic polymers in a good solvent?"
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Learn More About the Presenters


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James J. Marti, Ph.D.

James Marti is Senior Scientist and Outreach Coordinator for the Minnesota Nano Center, where he manages two research laboratories focusing on nanomaterials and the biological applications of nanotechnology. Prior to joining the MNC, Dr. Marti conducted research on nanoparticles for academic and government labs, and served as R&D director for several small companies with a nanotechnology product focus. A physicist by training, his primary scientific interest has been the physics and chemistry of micron-and nanometer-scale particles, particle systems, and related materials.

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Borries Demeler, Ph.D.

Borries Demeler, Ph.D. is the Canada 150 Research Chair for Biophysics at the University of Lethbridge in Canada, with cross appointments at UT Health in San Antonio and at the University of Montana. Dr. Demeler is well known for his contributions to the field of solution biophysics, in particular for the hydrodynamic modeling of analytical ultracentrifugation experiments. He has published over 190 manuscripts and book chapters. He is the principal author of the open source UltraScan software, and has created a world-wide network of laboratory information management systems (LIMS servers) to support high resolution hydrodynamic modeling with high-performance computing. Together with Prof. Helmut Coelfen in Germany he has pioneered the use of multi-wavelength analytical ultracentrifugation for the study of hetero-interacting systems and measuring binding stoichiometry in the solution state. At the University of Lethbridge he manages the Canadian Center for Hydrodynamics. His NIH-funded research group at the University of Montana develops GMP validation and automation of the analytical ultracentrifugation technique. He is the CEO of AUC Solutions LLC based in Houston Texas, where he provides consulting services to the biopharma industry.


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* Product is not verified or validated for use in diagnostic procedures.

References:


**Introduction to Analytical Ultracentrifugation
Author: GREG RALSTON - DEPARTMENT OF CHEMISTRY, THE UNIVERSITY OF SYDNEY AUSTRALIA
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