nanoDSF – Comparison

Comparing the nanoDSF to other biophysical methods

Important methods used to investigate protein stability include Differential Scanning Fluorimetry (DSF), Differential Scanning Calorimetry (DSC), and Circular Dichroism Spectroscopy (CD). Comparing datasets obtained by these technologies with nanoDSF data reveals high similarity. This indicates that the output data of these technologies are absolutely comparable. However, nanoDSF assays provide valuable advantages as shown in the summary below.

FACTS & FEATURES: nanoDSF compared to other methods
  • protein stability analysis under close to native conditions
  • low sample consumption
  • free choice of buffers and detergents
  • ultra-high resolution due to high data point density
  • rapid analysis
Draw Backs
  • unfolding transitions of proteins lacking tryptophanes might be difficult to detect
MethodDifferential Scanning Fluorimetry (DSF)
  • measurement can be done by a conventional q-PCR machine
Draw Backs
  • dyes may affect structural protein unfolding transitions by stabilization of the unfolded state
  • probability of background noise due to detergent dye complexes
  • not applicable to all biomolecular species
MethodDifferential Scanning Calorimetry (DSC)
  • direct measurement of thermodynamic properties
  • analysis of biomolecules to nano-sized materials
Draw Backs
  • large amount of sample is necessary
  • analysis is sensitive to aggregation, precipitation and self-association effects
MethodCircular Dichroism Spectroscopy (CD)
  • additional information on protein configuration (distribution of alpha-helix or beta-sheet, etc.)
Draw Backs
  • requirement of specific buffer conditions
  • detergents absorb light and affect measurement

For detailed informations, download the 2bind – nanoDSF booklet