Effects of His-tags on Physical Properties of Parvalbumins

Document Type

Article

Publication Date

2019

Keywords

Protein

Digital Object Identifier (DOI)

https://doi.org/10.1016/j.ceca.2018.11.006

Abstract

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.

Was this content written or created while at USF?

Yes

Citation / Publisher Attribution

Cell Calcium, v. 77, p. 1-7

Link to Full Text

Share

COinS