Effects of his-tags on physical properties of parvalbumins |
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| Institution: | 1. Institute for Biological Instrumentation of the Russian Academy of Sciences, Pushchino, Moscow region, 142290, Russia;2. Department of Molecular Medicine and USF Health Byrd Alzheimer''s Research Institute, Morsani College of Medicine, University of South Florida, Tampa, Florida 33612, USA;1. Division of Endocrinology and Metabolism, Department of Internal Medicine, College of Medicine, Inje University, Busan, South Korea;2. Department of Pharmacology and Clinical Trial Centre, Inje University, Busan Paik Hospital, Busan, South Korea;1. Department of Physical Chemistry, University of Rostock, Dr-Lorenz-Weg 1, 18059 Rostock, Germany;2. Department of Physical Chemistry, Kazan Federal University, Kremlevskaya str. 18, 420008 Kazan, Russia;3. Chemistry Faculty, Belarusian State University, Leningradskaya 14, 220030 Minsk, Belarus;4. Applied Chemicals and Materials Division, National Institute of Standards and Technology, Boulder, CO 80305-3337, USA;5. Mulliken Center for Theoretical Chemistry, University of Bonn, Beringstr. 4+6, D-53115 Bonn, Germany;1. School of Chemistry and Molecular Engineering, East China University of Science and Technology, Shanghai 200237, China;2. Department of Chemistry, Lanzhou University, Lanzhou, Gansu 730000, China;1. Department of Chemistry, Lanzhou University, Lanzhou, Gansu 730000, China;2. School of Chemistry and Molecular Engineering, East China University of Science and Technology, Shanghai 200237, China |
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| 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. |
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| Keywords: | Protein |
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