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The University of Montana
CBSD
ISB 106
Missoula, MT 59812
Phone: 406.243.6003
Fax: 406.243.6024 
cbsd@umontana.edu

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BioSpectroscopy Core Research Laboratory

Services

The BioSpectroscopy Core Research Laboratory (BCRL) offers consultation, experimental design, measurement, and data analysis on a collaborative or contractual basis using the spectroscopy techniques outlined below.

  • Steady-state absorption and fluorescence (emission and excitation)
  • Time-resolved spectroscopy techniques
    • Anisotropy
    • Luminescence (fluorescence and phosphorescence) decay
    • Förster Resonance Energy Transfer (FRET)
    • Time-Resolved Emission Spectra (TRES)
    • Fluorescence Correlation Spectroscopy (FCS)
    • Single-Molecule FRET
    • Fluorescence Lifetime Imaging (FLIM)

Due to the range of techniques available and their diverse applications, the services provided by the BCRL are often unique to each research project.  Examples of present and past collaborative projects include:

  • BCRL Applications
  • Protein-protein and DNA-Protein Interactions — development of novel approaches for studying protein-protein and protein-nucleic acid interactions by replacing the endogenous tryptophan residues in recombinant proteins with tryptophan analogs; and similarly, fluorescent base analogs for DNA or RNA. These pseudo-intrinsic spectroscopic probes allow us to dissect complex biological interactions and link functionally important conformational dynamics and thermodynamics to the observed biology and associated molecular structures.
  • Membrane-Protein Interactions — study of the dynamics and assembly of proteins that interact on membranes and via phospholipid-bilayer nanodiscs.
  • Probe development to study microsecond dynamics — development of novel metal-ligand complex (MLC) probes to provide new tools for observing microsecond time-scale dynamics.
  • G Protein Structural Dynamics — investigation, on the single-molecule and ensemble average levels, of the conformational states and dynamic motions involved in G protein nucleotide exchange during receptor-independent cell signaling.

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