Biophysics

Biophysics

The Biophysics Facility consists of microcalorimetry (isothermal titration calorimetry and differential scanning calorimetry) and microscale thermophoresis. These approaches support research specializing in the study of characteristics of molecules and the interaction between molecules. These biophysical characteristics are of great interest to many biological, pharmaceutical, and chemical research questions.

Contacts

Staff

pacman

Emery Ng, Ph.D.

Facility Scientist
Biology Physics Building
Room G05A
emery.ng@uconn.edu
860.486.4550

Faculty Scientific Advisers

jlc02020

James L. Cole, Ph.D.

Professor
james.cole@uconn.edu
860.486.4333
vlr04001

Victoria Robinson, Ph.D.

Associate Professor
victoria.robinson@uconn.edu
860.486.4353
pacman

Dennis Wright, Ph.D.

Professor
School of Pharmacy Room 629
dennis.wright@uconn.edu
860.486.9451

Location

Campus Address

Biology Physics Building
Room G05
Storrs Campus

Mailing Address

Center for Open Research Resources and Equipment
91 North Eagleville Road, Unit 3149
Storrs, CT 06269

Instrumentation

CvELuiLyaEsYCFsOx7HKoqh47EQfzBtX

Nano-ITC (Isothermal Titration) Calorimeter

ITC is a quantitative technique that can directly measure the binding affinity, enthalpy changes, and binding stoichiometry of the interaction between two or more molecules in solution. From these initial measurements Gibbs energy and entropy changes can be determined in a relatively straightforward manner.

ypD6MznHBI0QTiVePFJ2gLbwtzN0BbPO

Nano-DSC (Differential Scanning) Calorimeter

DSC is a thermo-analytical technique which can be used to monitor phase transitions in different systems. The Nano-DSC is specifically designed to determine the thermal stability and heat capacity of proteins and other macromolecules in dilute solution, with versatility to allow the screening of ligands and pressure perturbation measurements.

NXtpQuRZvhHNAKyyXtsx20LvQBTpSX8a

Monolith NT.115pico (MST)

The Monolith system provides fast and highly sensitive detection and quantification of molecular interactions in glass capillaries. This user-friendly system uses MicroScale Thermophoresis (MST) to obtain binding parameters such as dissociation constants (Kd) or EC50 values in a high-throughput manner.

Analytical Ultracentrifugation

G05 of the Biology/Physics building also houses two Beckman XL-I analytical ultracentrifuges, one of which is equipped with an Aviv AU-FDS fluorescence detector, using HeteroAnalysis, and an Optima analytical ultracentrifuge. These are not supported by the Biophysics facility and are available on a self-service basis at no charge. Prospective users with any questions should contact Dr. James Cole james.cole@uconn.edu.

E1y7V555s3wkEKsh1lfs5al3ZgWTbq9a

Services & Rates

Service & Rates

The Biophysics Facility offers training and access to calorimetric and novel thermophoretic techniques. Approved users can independently use equipment by making reservations on CIDER, and billing is calculated by CORE.

  • Consultation, training, and assistance for microcalorimetry and microscale thermophoresis instruments is available
  • Fee-based use for approved users on equipment is available 24/7
  • TA Instruments’ NanoAnalyze software for NanoDSC and NanoITC analysis is available to download from the TA Instruments’ website
  • Monolith Analysis software, which fits runs to dissociation constant (Kd) or Hill model (EC50) is available on the Monolith NT.115pico PC laptop for use for free

Research Potential

Nano-ITC and Nano-DSC Calorimeters: 

The complete thermodynamic profiles of the interactions in question are of enormous value in drug design because they provide information about the balance of driving forces that cannot be obtained from structural or computational methods alone.

ITC applications for studying macromolecule/small molecule and macromolecule/macromolecule binding reactions include measurement of:

  • Binding constant
  • Stoichiometry
  • Enthalpy-entropy compensation
  • Environmental effects on binding
  • Enzyme kinetics

DSC applications for macromolecular characterization include the studying of:

  • Stability
  • Unfolding
  • Domain structure
  • Interactions with membranes
  • Binding

NanoTemper Monolith

The Monolith instrument measures molecular interactions based on the theory of microscale thermophoresis (MST), or the change in mobility of a molecule due to the property changes under an IR-induced microscopic temperature gradient. The Monolith has a large application range, ability to detect picomolar affinity, low sample volume requirement, and fast measurements of up to 16 samples.

MST applications for binding measurements determined by the Monolith include:

  • Affinity
  • Stoichiometry
  • Enthalpy
  • Enzyme kinetics