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Making a single-chain four-helix bundle for redox chemistry studies
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2008 (English)In: Protein Engineering Design & Selection, ISSN 1741-0126, E-ISSN 1741-0134, Vol. 21, no 11, 645-652 p.Article in journal (Refereed) Published
Abstract [en]

The construction and characteristics of the stable and well-structured alpha W-4 protein are described. The 117-residue, single-chain protein has a molecular weight of 13.1 kDa and is designed to fold into a four-helix bundle. Experimental characterization of the expressed and purified protein shows a 69.8 +/- 0.8% helical content over a 5.5-10.0 pH range. The protein is thermostable with a T-M > 355 K and has a free energy of unfolding as measured by chemical denaturation of -4.7 kcal mol(-1) at 25 degrees C and neutral pH. One-dimensional (1D) proton and 2D N-15-HSQC spectra show narrow, well-dispersed spectral lines consistent with a uniquely structured alpha-helical protein. Analytical ultracentrifugation and NMR data show that the protein is monomeric over a broad protein concentration range. The 324 nm emission maximum of the unique Trp-106 is consistent with a sequestered position of the aromatic residue. Additionally, differential pulse voltammetry characterization indicates an elevated peak potential for Trp-106 when the protein is folded (pH range 7.0-8.5) relative to partly unfolded (pH range 11.4-13.2). The oxidation of Trp-106 is coupled to proton release as shown by a 53 +/- 3 mV/pH unit dependence of the peak potential over the 7.0-8.5 pH range.

Place, publisher, year, edition, pages
2008. Vol. 21, no 11, 645-652 p.
National Category
Natural Sciences Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:su:diva-57886DOI: 10.1093/protein/gzn043ISI: 000260144000002OAI: oai:DiVA.org:su-57886DiVA: diva2:418435
Projects
amino-acid radicals, four-helix bundle, NMR, protein design, Rop
Note
authorCount :7Available from: 2011-05-23 Created: 2011-05-23 Last updated: 2017-12-11Bibliographically approved

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