Effects of His-tags on Physical Properties of Parvalbumins
Digital Object Identifier (DOI)
A comparative study of His-tagged and non-tagged rat β-parvalbumin (rWT β-PA), calcium binding protein with the EF-hand calcium binding domains, has been carried out. The attachment of His-tag increases α-helical content and decreases β-sheets and β-turns content of the metal free form (apo-state) of β-PA. In contrast to this, the attachment of His-tag decreases α-helical content by more than 10% and increases contents of β-sheets and β-turns of the Ca2+-loaded state. According to the dynamic light scattering analysis, apo-state of His-tagged rat β-PA seems to be less compact compared with the apo-state of non-tagged rat β-PA. Surprisingly, the attachment of His-tag practically does not change mean hydrodynamic radius of Ca2+-loaded rat β-PA. The attachment of His-tag shifts thermal denaturation peaks of both apo- and Ca2+-loaded states of rat β-PA towards higher temperatures by 3–4 °C and slightly decreases its Ca2+ affinity. These results should be taken into consideration in the use of His-tagged parvalbumins.
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Citation / Publisher Attribution
Cell Calcium, v. 77, p. 1-7
Scholar Commons Citation
Vologzhannikova, Alisa A.; Khorn, Polina A.; Kazakov, Alexei S.; Permyakov, Eugene A.; Uversky, Vladimir N.; and Permyakov, Sergei E., "Effects of His-tags on Physical Properties of Parvalbumins" (2019). Molecular Medicine Faculty Publications. 129.