Differential Scanning Calorimetry: Theory and Practice
White Paper Aug 19, 2015
Malvern Instruments Limited
Here the thermodynamic background to DSC measurements is discussed and its application in studying the stability of proteins both alone and interacting with ligands.
The key benefit with DSC is that it is based on heat measurements and therefore allows the characterization of native biomolecules. Furthermore, the lack of spectroscopic readings means that the samples do not have to be optically clear. In addition, the characterization is not limited to the melting temperature (Tm), but it also provides data on the forces involved in folding of biomolecules and the mechanisms by which they unfold.
Related White Papers
Using Micro Flow Imaging (MFI) to Measure Protein AggregationWhite Paper
Download this free white paper from Protein Simple to learn about the differences between MFI and how MFI provides crucial information about your protein therapeutic.READ MORE
How to Identify Low-Abundance Modified Peptides with Proteomics Mass SpectrometryWhite Paper
We present a new simplicity-focused analytics methodology, called Sorcerer Score™ that allows low-abundance, modified peptides (LAMPs) to be rigorously identified within a hypothesis-driven framework based on high-accuracy precursor and fragment mass data. Accurate peptide ID is fundamental to accurate protein quantitation and post-translational modification (PTM) analysis.READ MORE
Biophysical Application of Calorimetric Methods to Protein Misfolding and Aggregation ExaminationsWhite Paper
Promoting calorimetry-based studies on protein misfolding by developing treatments and prevention of aggregation-related diseases.READ MORE