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Secondary structure conversions of Mycobacterium tuberculosis ribonucleotide reductase protein R2 under varying pH and temperature conditions
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för fysikalisk kemi, oorganisk kemi och strukturkemi.ORCID-id: 0000-0002-7284-2974
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
2008 (engelsk)Inngår i: Biophysical Chemistry, Vol. 137, nr 43-48Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

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.

sted, utgiver, år, opplag, sider
2008. Vol. 137, nr 43-48
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URN: urn:nbn:se:su:diva-14493DOI: doi:10.1016/j.bpc.2008.06.009ISI: 000258890800008OAI: oai:DiVA.org:su-14493DiVA, id: diva2:181013
Tilgjengelig fra: 2008-09-25 Laget: 2008-09-25 Sist oppdatert: 2019-12-17bibliografisk kontrollert

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Forlagets fullteksthttp://www.ncbi.nlm.nih.gov/pubmed/18657348?dopt=Citation%27

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