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Updated: Jul 3, 2026

Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
Secondary structure conversions of Mycobacterium tuberculosis ribonucleotide reductase protein R2 under varying pH
Elka R Georgieva1, Ana Julia Narvaez, Niklas Hedin
1Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences, Svante Arrhenius väg 10-12, S-10691 Stockholm, Sweden. erg54@cornell.edu
Abstract:
The structural properties of Mycobacterium tuberculosis (Mtb) ribonucleotide reductase R2 protein were studied under varying pH and temperature conditions by circular dichroism (CD) spectroscopy as well as dynamic light scattering (DLS). Under physiological conditions this protein has a high alpha-helical content, similar to the corresponding protein from other species, e.g. mouse. Decreasing the pH induced significant structure conversions. When pH was below 6.5 an aggregated structure was observed and reached a maximum at pH 4. The aggregated state of this protein was verified by DLS and was found to be rich in beta-structure. This amyloid-like structure transformed into a molten globule state with high temperature stability (between 25 and 80 degrees C) at pH below 3. The corresponding mouse protein R2 under similar conditions showed no evidence of an aggregated state around pH 4.
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