Molecular Biotechnology Core

About

The Molecular Biotechnology Core offers biomolecular interaction analysis and equilibrium and kinetic measurements using Biacore S200, Isothermal Titration Calorimetry and Microscale Thermophoresis, and CD Spectroscopy.

The Core provides a wide range of high quality services of surface plasmon resonance (SPR) and other biophysical technologies. Biomolecular interactions are quantified using Biacore S200 and NanoTemper (NT, LabelFree and NT.115), while isothermal titration calometer (iTC MicroCal 200) is used for measuring the thermodynamic parameters (kinetics, enthalpy, entropy and number of binding sites) of biomolecular interactions. Jasco 815 CD spectrophotometer is capable for analysis of secondary structure of proteins in solution and protein folding and confirmation changes.

  • Surface Plasmon Resonance
  • Isothermal Titration Calorimetry
  • Circular Dichroism Spectroscopy
  • Microscale Thermophoresis

Contacts

Smarajit  Bandyopadhyay, PhD

Smarajit Bandyopadhyay, PhD
Project Staff
Director, Molecular Biotechnology Core
Location:NB2-37
Phone:(216) 445-7095
bandyos1@ccf.org

Xiuxua  Cheng

Xiuxua Cheng
Research Technologist
chengx@ccf.org

Services




Grant Information

The Molecular Biotechnology Core offers consultation and services in the areas of biomolecular interaction analysis and equilibrium and kinetic measurements, and secondary structure determination.

The Core offers training and facilitates biomolecular interactions analysis using the Biacore S200 system, based on the principle of Surface Plasmon Resonance (SPR). The Biacore S200 is highly sensitive and used for measuring the interactions of macromolecules with each other or with small ligands, and for equilibrium and kinetic measurements, competition assays, and epitope mapping. The core provides hands-on training on both Biacore S200 and the S200 Evaluation software to users.

The Core offers training and assists researchers in using Isothermal Titration Calorimetry (ITC Microcal 200). ITC is a thermodynamic technique that measures the heat released or absorbed during a biomolecular binding event. It allows accurate determination of binding constants (KB), reaction stoichiometry (n), enthalpy (δH) and entropy (δS), thus providing a complete thermodynamic profile of the molecular interaction in a single experiment.

The Core provides training and assists researchers in using Microscale Thermophoresis (MST). It is a powerful technique for quantifying molecular interactions. This technique is based on thermophoresis, which is defined as temperature gradient-induced directed motion of molecules. In experiments using the Monolith NT.115, one of the binding-partner must be a biomolecule with covalently attached fluorophore or a fluorescent fusion protein like GFP. MST experiments can also be performed in a label-free setting using intrinsic fluorescence of protein in another Monolith model (NT.LabelFree). It also permits studying of the interaction of small molecules and proteins with ease or membrane proteins stabilized in buffers of choice. Thus its high adaptability over other techniques renders it unique and unparalleled.

The Core maintains and provides training to use CD spectroscopy. CD Spectroscopy is a valuable instrument for rapid analysis of structural and conformational changes in a protein upon perturbation by mutation, temperature, pH and buffers. CD spectra arising due to peptide bond transitions in the "far-uv" spectral region (190-250 nm) provide information on secondary structure of protein, while CD spectra of proteins in the "near-uv" spectral region (250-350 nm) provide information on certain aspects of tertiary structure.

Molecular Biotechnology Core

  • Molecular Biotechnology Lab
    NE5-214
    216.444.5845
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