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2. Secondary structure estimation of recombinant psbH, encoding a photosynthetic membrane protein of cyanobacterium Synechocystis sp. PCC 6803

Creator:
Štys, D., Schoefberger, W., Halbhuber, Z., Ristvejova, J., Müller, N., and Ettrich, R.
Format:
bez média and svazek
Type:
model:article and TEXT
Subject:
CD spectroscopy, molecular dynamics calculations, NMR spectroscopy, photosystem 2, and protein folding
Language:
Multiple languages
Description:
The PsbH protein of cyanobacterium Synechocystis sp. PCC 6803 was expressed as a fusion protein with glutathione-S transferase (GST) in E. coli grown on a mineral medium enriched in 15N isotope. After enzymatic cleavage of the fusion protein, the 1H-15N-HSQC spectrum of PsbH protein in presence of the detergent β-D-octyl-glucopyranoside (OG) was recorded on a Bruker DRX 500 MHz NMR spectrometer equipped with a 5 mm TXI cryoprobe to enhance the sensitivity and resolution. Non-labelled protein was used for secondary structure estimation by deconvolution from circular dichroism (CD) spectra. Experimental results were compared with our results from a structural model of PsbH using a restraint-based comparative modelling approach combined with molecular dynamics and energetic modelling. We found that PsbH shows 34-38% α-helical structure (Thr36-Ser60), a maximum of around 15% of β-sheet, and 12-19% of β-turn. and D. Štys ... [et al.].
Rights:
http://creativecommons.org/licenses/by-nc-sa/4.0/ and policy:public