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Updated: Aug 6, 2026
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Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions
Published on: November 21, 2017
Temperature variation of polyribonucleotide conformation by an interaction with basic globular proteins
Biophysical Journal
|May 1, 1973
Abstract:
Chicken lysozyme interacts with polyribonucleotides to form large light-scattering centers. The size of these is critically dependent on conformation of the polynucleotides. Hence, the interaction provides a very sensitive method of determining temperature intervals within which the polynucleotides change from multistranded, stacked-base structures to single-stranded, random coils. This change can be observed with the unaided eye, especially when concentrations of polynucleotides are of the order of a few micrograms per milliliter.
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