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Tycho nt 6

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The Tycho NT.6 is a label-free biomolecular interaction analysis system designed for characterizing the binding kinetics and affinities of molecular interactions. It utilizes microscale thermophoresis technology to measure changes in the motion of molecules in response to a local temperature gradient, providing insights into the binding events between biomolecules.

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Lab products found in correlation

Tycho nt 6 capillaries, by NanoTemper (2 mentions) Prism 7, by GraphPad (2 mentions) Uv capillaries, by NanoTemper (1 mentions) Nanodrop nd 1000 spectrophotometer, by Marshall Scientific (1 mentions) Superdex 200, by Cytiva (1 mentions) Human ace2 protein, by Sino Biological (1 mentions) Xylobiose, by Megazyme (1 mentions) Xylotriose, by Megazyme (1 mentions) Bnzglca, by Biosynth (1 mentions) Cellobiose, by Merck Group (1 mentions) Xylotetraose, by Megazyme (1 mentions) Fetal calf serum (fcs), by Thermo Fisher Scientific (1 mentions) Rpmi medium, by Thermo Fisher Scientific (1 mentions) Ty c001, by NanoTemper (1 mentions)

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Tycho NT.6 instrument (15 citations) Tycho NT.6 capillaries (8 citations) Tycho (7 citations) Tycho NT.6 system (4 citations) Tycho NT.6 device (2 citations) Tycho NT.6 capillaries (TY-C001, (2 citations)

83 protocols using tycho nt 6

1

Redox State Regulation of PTP4A1

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The preparation of uniformly reduced PTP4A1 was accomplished by incubating PTP4A1 with 10 mM DTT at 40°C for 2 hours. The preparation of uniformly oxidized PTP4A1 was accomplished by incubating with 40 mM oxidized glutathione at 25°C for 16 hours. The oxidation state of PTP4A1 was monitored by measuring the melting temperature using a Tycho NT.6 (Nanotemper) using standard capillaries (10 μL) using a 30°C/min ramp (from 35°C to 95°C) and evaluated using Tycho NT.6 software version 1.1.5.668. The oxidized, reduced, and mixture of PTP4A1 species showed melting temperatures of 71°C, 77°C, and 74°C, respectively.
Zhang R., Kumar G.S., Hansen U., Zoccheddu M., Sacchetti C., Holmes Z.J., Lee M.C., Beckmann D., Wen Y., Mikulski Z., Yang S., Santelli E., Page R., Boin F., Peti W, & Bottini N. (2022). Oxidative stress promotes fibrosis in systemic sclerosis through stabilization of a kinase-phosphatase complex. JCI Insight, 7(8), e155761.
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2

Thermostability Analysis of AjFER Proteins

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The thermostability of the AjFER, MF, M3, and M4 proteins was determined using a label-free thermal shift assay with the Tycho NT.6 (NanoTemper Technologies, Munich, Germany) via the intrinsic tryptophan and tyrosine fluorescence. The 10 µL solutions of protein samples (approx. 5 mg/mL) were prepared and loaded into Tycho NT.6 capillaries (NanoTemper Technologies, Munich, Germany; catalog no. TYC001). The thermal profiles of the proteins were recorded during a quick thermal ramp from 35 to 95 °C, with a heating rate of 30 °C/min. The inflection unfolding temperatures (Ti) were assessed based on the changes in the 350/330 nm fluorescence emission ratio values. Thereafter, AjFER and its variants were heated at 90 °C for 10 min, and their structural integrity was analyzed using TEM and DLS methods, as described above.
Wu Y., Huo C., Ming T., Liu Y., Su C., Qiu X., Lu C., Zhou J., Li Y., Zhang Z., Han J., Feng Y, & Su X. (2022). Structural and Functional Insights into the Roles of Potential Metal-Binding Sites in Apostichopus japonicus Ferritin. Polymers, 14(24), 5378.
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3

Bax Thermal Stability Assay

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Purified recombinant BAX (25 µM) was combined with DMSO or EO (1:10 BAX:EO) and loaded into Tycho NT.6 (NanoTemper Technologies) capillaries. First derivative (330/350 nm) melting point curves were generated automatically using the Tycho NT.6 (NanoTemper Technologies). Data were exported and to GraphPad PRISM software for analysis and visualization.
Spitz A.Z., Zacharioudakis E., Reyna D.E., Garner T.P, & Gavathiotis E. (2021). Eltrombopag directly inhibits BAX and prevents cell death. Nature Communications, 12, 1134.
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4

Thermal Unfolding of Proteins

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For each condition, 10 μL of sample per capillary were prepared. The protein samples were loaded into UV capillaries (NanoTemper Technologies, Germany) and experiments were carried out using the NanoTemper Tycho NT.6 (NanoTemper Technologies, Germany). The temperature gradient was set to an increase of 20 °C min−1 in a range from 35 °C to 95 °C. Protein unfolding was measured by detecting the temperature-dependent change in tryptophan fluorescence at emission wavelengths of 330 and 350 nm. Inflection temperatures (Ti) were determined by detecting the maximum of the first derivative of the fluorescence ratios (F350/F330). For this, an 8th order polynomial fit was calculated for the transition region. Next, the first derivative of the fit was formed and the peak position (at Ti) was determined.
Singh R.K., Blossom B.M., Russo D.A., van Oort B., Croce R., Jensen P.E., Felby C, & Bjerrum M.J. (2019). Thermal unfolding and refolding of a lytic polysaccharide monooxygenase from Thermoascus aurantiacus. RSC Advances, 9(51), 29734-29742.
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5

Thermal Stability of Conk-C3 Derivatives

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The thermal stability of Conk-C3 derivatives was determined by differential scanning fluorimetry on a NanoTemper Tycho NT.6 (NanoTemper Technologies, Germany) with a back-reflection aggregation detection at a range from 35 to 95°C and with a heating rate of 20 °C min -1 . Protein unfolding at 0.1mM in ND96 buffer was followed by tyrosine fluorescence intensity at 330 and 350 nm. The melting temperature (Tm) was determined by detecting the maximum of the first derivative of the fluorescence ratios (F350/F330) after fitting experimental data with a polynomial function. Data were acquired in triplicates.
Saikia C., Dym O., Altman-Gueta H., Gordon D., Reuveny E, & Karbat I. (2021). A Molecular Lid Mechanism of K+ Channel Blocker Action Revealed by a Cone Peptide. Journal of molecular biology, 433(17).
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6

Thermal Stability of Conk-C3 Derivatives

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The thermal stability of Conk-C3 derivatives was determined by differential scanning fluorimetry on a NanoTemper Tycho NT.6 (NanoTemper Technologies, Germany) with a back-reflection aggregation detection at a range from 35 to 95°C and with a heating rate of 20 °C min -1 . Protein unfolding at 0.1mM in ND96 buffer was followed by tyrosine fluorescence intensity at 330 and 350 nm. The melting temperature (Tm) was determined by detecting the maximum of the first derivative of the fluorescence ratios (F350/F330) after fitting experimental data with a polynomial function. Data were acquired in triplicates.
Saikia C., Dym O., Altman-Gueta H., Gordon D., Reuveny E., & Karbat I. (2020). A molecular lid mechanism of K+ channel blocker action revealed by a cone peptide.
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7

Protein Melting Point Analysis

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Protein melting points were determined with a Tycho NT.6 instrument (NanoTemper Technologies GmbH). Proteins dissolved to 0.5–3 mg/ml in the indicated buffer were loaded into glass capillaries and the melting temperature was obtained as the inflection point of the fluorescence ratio at 350 and 330 nm with respect to temperature.
Borgert S.R., Henke S., Witzgall F., Schmelz S., zur Lage S., Hotop S.K., Stephen S., Lübken D., Krüger J., Gomez N.O., van Ham M., Jänsch L., Kalesse M., Pich A., Brönstrup M., Häussler S, & Blankenfeldt W. (2022). Moonlighting chaperone activity of the enzyme PqsE contributes to RhlR-controlled virulence of Pseudomonas aeruginosa. Nature Communications, 13, 7402.
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8

Protein Melting Point Analysis

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Protein melting points were determined with a Tycho NT.6 instrument (NanoTemper Technologies GmbH). Proteins dissolved to 0.5–3 mg/ml in the indicated buffer were loaded into glass capillaries and the melting temperature was obtained as the inflection point of the fluorescence ratio at 350 and 330 nm with respect to temperature.
Borgert S.R., Henke S., Witzgall F., Schmelz S., zur Lage S., Hotop S.K., Stephen S., Lübken D., Krüger J., Gomez N.O., van Ham M., Jänsch L., Kalesse M., Pich A., Brönstrup M., Häussler S, & Blankenfeldt W. (2022). Moonlighting chaperone activity of the enzyme PqsE contributes to RhlR-controlled virulence of Pseudomonas aeruginosa. Nature Communications, 13, 7402.
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9

Thermal Stability of RBD Mutant

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The impact of the Y453F substitution on protein stability was analyzed on a Tycho NT.6 (NanoTemper technologies GmbH, Munich, Germany). RBD WT and Y453F were subjected in triplicates to a thermal ramp of 30 °C/min in PBS. Protein denaturation was monitored from the intrinsic fluorescence detected at 350 and 330 nm. Inflection temperatures representing a discrete unfolding event were calculated by the Tycho system from the 350:330 ratio.
Bayarri-Olmos R., Rosbjerg A., Johnsen L.B., Helgstrand C., Bak-Thomsen T., Garred P, & Skjoedt M.O. (2021). The SARS-CoV-2 Y453F mink variant displays a pronounced increase in ACE-2 affinity but does not challenge antibody neutralization. The Journal of Biological Chemistry, 296, 100536.
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10

Tycho NT.6 Thermal Shift Assay

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Prior to Ti measurement, wild-type (WT) and various HpMsrAB mutants were diluted to a concentration of 1 mg/mL for Tycho NT.6 experiments. The samples were then loaded as duplicates into Tycho NT.6 capillaries (Cat# TY-C001; NanoTemper Technologies; Munich, Germany). Ti measurements were taken using a Tycho NT.6 (NanoTemper Technologies) and calculated by plotting the first derivative of the 350/330 nm ratio against temperature.
Kim S., Lee K., Park S.H., Kwak G.H., Kim M.S., Kim H.Y, & Hwang K.Y. (2021). Structural Insights into a Bifunctional Peptide Methionine Sulfoxide Reductase MsrA/B Fusion Protein from Helicobacter pylori. Antioxidants, 10(3), 389.
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