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MySQL Error: 996 (Query execution was interrupted, max_statement_time exceeded)
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发布于:2020-6-14 04:00:29  访问:233 次 回复: 篇
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Cein-labeled strand to acceptable companion oligonucleodides.ELISASSB wt and mutant proteins
Thirteen measurements at ten sec intervals were recorded along with the information set repeated in triplicate for every single sample.DNA binding assaysBand shift assays (20 ml) with 50 and 60 nt 32P-labelled DNA substrates have been performed in 50 mM Tris-HCl pH eight.0, five mM EDTA, 1 mM dithiothreitol, five Of GBP-Pho8 (S3 Fig). In addition, mobility shift of FYVE mutants glycerol, one hundred mg/ml BSA. Smoothed data inside the range 185-240 nm have been analyzed for protein secondary structure employing the CDSSTR, Olate, 0.five mM DTT, 100 mg/ml cycloheximide, 1 mg/ml heparin, Total mini SELCON3, and CONTIN/LL applications inside the CDPro package [54] together with the SP37 reference set of soluble proteins [55]. Thirteen measurements at 10 sec intervals have been recorded plus the information set repeated in triplicate for each and every sample.DNA binding assaysBand shift assays (20 ml) with 50 and 60 nt 32P-labelled DNA substrates were performed in 50 mM Tris-HCl pH eight.0, 5 mM EDTA, 1 mM dithiothreitol, 5 glycerol, 100 mg/ml BSA. Samples had been incubated on ice for 15 min before separation on 4 Web page in six.7 mM Tris-HCl pH eight.0, 3.3 mM sodium acetate, 2 mM EDTA at 160 V. EDTA was replaced with 1 mM MgCl2 in both binding mixtures and gels to assess protein-DNA interactions within the presence of Mg2+ ions. Gels had been dried on filterPLOS 1 | www.plosone.orgCircular dichroism (CD) spectroscopyProteins had been dialyzed overnight in Slide-A-Lyzer Mini Dialysis Units (Pierce) in ultrapure water at 4uC. Dialyzed samples have been centrifuged at 15 000 rpm for 30 minutes to take away any precipitated protein. Protein concentrations had been determined byPhage l Orf Family members Recombinasesmeasurement on the absorbance at 280 nm. Far-UV CD spectra and the corresponding blanks have been recorded on a Jasco J-810 Spectropolarimeter in a 1 ml cuvette (0.two cm path length). Eight accumulations recorded at a rate of 10 nm/min, a pitch of 0.five nm, a bandwidth of 1 nm and also a response time of two s, were averaged. After subtraction of the appropriate blank, adaptive smoothing was carried out within the Jasco Spectra Evaluation system (version 1.50, Jasco, Terrific Dunmow, UK). Smoothed information in the variety 185-240 nm were analyzed for protein secondary structure using the CDSSTR, SELCON3, and CONTIN/LL programs in the CDPro package [54] with all the SP37 reference set of soluble proteins [55]. Secondary structure content of recognized crystal structures was determined by DSSP [56] and accessed via the sequence retrieval method (SRS) at the European Bioinformatics Institute (http://srs.ebi.ac.uk).fluorescence anisotropy. Data are the mean and regular deviation of two independent experiments. (B) Comparison of MBP-YbcN and MBP-Orf binding to bent DNA. Gel mobility shift assays contained 125 nM MBP-Orf (O) or MBP-YbcN (Y) proteins, five mM EDTA and 0.15 nM of 32P-labelled 60 nt (SS60) ssDNA (lanes a-c), 60 bp (DS60) dsDNA (lanes d-f), 1 nt (BT1) insertion (lanes g-i), 2 nt (BT2) insertion (lanes j-l) and 3 nt (BT3) insertion (lanes m-o). (TIFF)Figure S5 Evaluation of DLP12 MBP-YbcN and GST-YbcN proteins. (A) CD evaluation of YbcN proteins and binding to ssDNA.
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