Heat capacity studies of BPTI by Differential scanning calorimetry (DSC) (CAT#: STEM-MB-0471-WXH)

Introduction

Bovine pancreatic trypsin inhibitor (BPTI) is one of the smallest and simplest globular proteins. BPTI’s function is the suppression of protein digestion, i.e., the breakdown of proteins into their peptide building blocks, by means of inhibiting the action of the enzyme trypsin which is produced in the bovine pancreas.
The heat capacity plays a major role in the determination of the energetics of protein folding and molecular recognition. As such, a better understanding of this thermodynamic parameter and its structural origin will provide new insights for the development of better molecular design strategies.

Add to Cart Please Inquire

Principle Applications Procedure Materials Notes Related Products

Principle

Calorimetry is a primary technique for measuring the thermal properties of materials to establish a connection between temperature and specific physical properties of substances and is the only method for direct determination of the enthalpy associated with the process of interest. Calorimeters are used frequently in chemistry, biochemistry, cell biology, biotechnology, pharmacology, and recently, in nanoscience to measure thermodynamic properties of the biomolecules and nano-sized materials.
Amongst various types of calorimeters, differential scanning calorimeter (DSC) is a popular one. DSC is a thermal analysis apparatus measuring how physical properties of a sample change, along with temperature against time.1In other words, the device is a thermal analysis instrument that determines the temperature and heat flow associated with material transitions as a function of time and temperature. During a change in temperature, DSC measures a heat quantity, which is radiated or absorbed excessively by the sample on the basis of a temperature difference between the sample and the reference material.

Applications

Determination of equilibrium thermodynamic stability.
Study of folding mechanism.
Screening for thermal stability as an indicator for, ligand binding, pharmaceutical formulation or conditions conducive to crystal growth.
Study of the denaturation process.

Procedure

1. Instrument Start-up
2. Sample Preparation
(1) Dialyze the sample against the buffer that will be used as the reference for the experiment.
(2) Determine the concentration of the protein sample using the most suitable protein concentration determination method.
(3) Degas the sample and reference buffer in vacuum to get rid of microbubbles that can cause volume inaccuracy.
(4) load the samples and their respective buffer in pairs into 96 well plates compatible with the instrument.
(5) Place the plate in the sample holding compartment in the proper orientation.
3. Experimental Parameter Setup
Set the starting temperature, final temperature and the scan rate of the experiment.
4. Data Analysis

Materials

Differential Scanning Calorimeters

Other recommended products

Isolatation and characterization of paracetamol form III by RHDSC (CAT#: STEM-MB-0506-WXH)
Heat capacity studies of Ubiquitin by Differential scanning calorimetry (DSC) (CAT#: STEM-MB-0476-WXH)
Study of the oxidative stability of complex (lecithin) lipids by Differential scanning calorimetry (DSC) (CAT#: STEM-MB-0495-WXH)
Thermal study of whey proteins by Differential scanning calorimetry (DSC) (CAT#: STEM-MB-0491-WXH)
Self-Assembly Study of Supramolecular Nanostructures by Differential scanning calorimetry (DSC) (CAT#: STEM-MB-0503-WXH)
Heat capacity studies of SOX5 by Differential scanning calorimetry (DSC) (CAT#: STEM-MB-0484-WXH)
Thermal study of Carboxypeptidase B by Differential scanning calorimetry (DSC) (CAT#: STEM-MB-0490-WXH)
Heat capacity studies of Lysozyme by Differential scanning calorimetry (DSC) (CAT#: STEM-MB-0474-WXH)