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compounds npe gtp  (Jena Bioscience)
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Jena Bioscience compounds npe gtp
( A ) Molecular mechanism of the two-step experiment to monitor GC and RGC enzyme activity. ( B ) Ca GC crystal structure with bound <t>GTP</t> (PDB 6SIR). The Ca 2+ ion is shown as green and water molecules as red spheres. ( C ) FTIR measurement protocols for GC and RGC experiments corresponding to E and G. Colors indicate time intervals over which FTIR spectra in D and F were averaged. ( D ) RGC·NPE-GTP (blue line) and <t>NPE-GTP</t> (light blue area) photolysis FTIR difference spectra. Spectrum averaged from 10 to 20 s (green line) after green illumination start and RGC steady state spectrum (light green area). Clipping of cGMP absolute spectrum (light red area). Spectrum averaged over last 200 s (purple line) compared to green light activation (light green area). ( E ) Kinetic traces of marker bands 1070(+) and 1117(-) (binding), 1630(+) (RGC activation) and 1087(+) (cGMP formation). Gray lines represent sections of constant slope during different illumination conditions. (inset) Normalized, smoothed (eight points) and dark activity corrected kinetic traces of 1087(+) (red line) and 1630(+) (black line) bands at green illumination onset. ( F ) UV-light-induced FTIR difference spectra of GC·NPE-GTP. Averaged spectra over first 20 s (purple line) and last 64 s (blue line) after photolysis. (light blue area) Photolysis spectrum of NPE-GTP. ( G ) Kinetic traces of GC·NPE-GTP photolysis marker bands 1527(-) (NPE cleavage), 1122 and 1087(+) (GTP to cGMP turnover). (inset) Experiment with 10-fold increased NPE-GTP concentration.
Compounds Npe Gtp, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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( A ) Molecular mechanism of the two-step experiment to monitor GC and RGC enzyme activity. ( B ) Ca GC crystal structure with bound GTP (PDB 6SIR). The Ca 2+ ion is shown as green and water molecules as red spheres. ( C ) FTIR measurement protocols for GC and RGC experiments corresponding to E and G. Colors indicate time intervals over which FTIR spectra in D and F were averaged. ( D ) RGC·NPE-GTP (blue line) and NPE-GTP (light blue area) photolysis FTIR difference spectra. Spectrum averaged from 10 to 20 s (green line) after green illumination start and RGC steady state spectrum (light green area). Clipping of cGMP absolute spectrum (light red area). Spectrum averaged over last 200 s (purple line) compared to green light activation (light green area). ( E ) Kinetic traces of marker bands 1070(+) and 1117(-) (binding), 1630(+) (RGC activation) and 1087(+) (cGMP formation). Gray lines represent sections of constant slope during different illumination conditions. (inset) Normalized, smoothed (eight points) and dark activity corrected kinetic traces of 1087(+) (red line) and 1630(+) (black line) bands at green illumination onset. ( F ) UV-light-induced FTIR difference spectra of GC·NPE-GTP. Averaged spectra over first 20 s (purple line) and last 64 s (blue line) after photolysis. (light blue area) Photolysis spectrum of NPE-GTP. ( G ) Kinetic traces of GC·NPE-GTP photolysis marker bands 1527(-) (NPE cleavage), 1122 and 1087(+) (GTP to cGMP turnover). (inset) Experiment with 10-fold increased NPE-GTP concentration.

Journal: eLife

Article Title: The inner mechanics of rhodopsin guanylyl cyclase during cGMP-formation revealed by real-time FTIR spectroscopy

doi: 10.7554/eLife.71384

Figure Lengend Snippet: ( A ) Molecular mechanism of the two-step experiment to monitor GC and RGC enzyme activity. ( B ) Ca GC crystal structure with bound GTP (PDB 6SIR). The Ca 2+ ion is shown as green and water molecules as red spheres. ( C ) FTIR measurement protocols for GC and RGC experiments corresponding to E and G. Colors indicate time intervals over which FTIR spectra in D and F were averaged. ( D ) RGC·NPE-GTP (blue line) and NPE-GTP (light blue area) photolysis FTIR difference spectra. Spectrum averaged from 10 to 20 s (green line) after green illumination start and RGC steady state spectrum (light green area). Clipping of cGMP absolute spectrum (light red area). Spectrum averaged over last 200 s (purple line) compared to green light activation (light green area). ( E ) Kinetic traces of marker bands 1070(+) and 1117(-) (binding), 1630(+) (RGC activation) and 1087(+) (cGMP formation). Gray lines represent sections of constant slope during different illumination conditions. (inset) Normalized, smoothed (eight points) and dark activity corrected kinetic traces of 1087(+) (red line) and 1630(+) (black line) bands at green illumination onset. ( F ) UV-light-induced FTIR difference spectra of GC·NPE-GTP. Averaged spectra over first 20 s (purple line) and last 64 s (blue line) after photolysis. (light blue area) Photolysis spectrum of NPE-GTP. ( G ) Kinetic traces of GC·NPE-GTP photolysis marker bands 1527(-) (NPE cleavage), 1122 and 1087(+) (GTP to cGMP turnover). (inset) Experiment with 10-fold increased NPE-GTP concentration.

Article Snippet: Caged compounds NPE-GTP and NPE-ATP were purchased from Jena Bioscience GmbH (Jena, Germany).

Techniques: Activity Assay, Activation Assay, Marker, Binding Assay, Concentration Assay

( A ) Absorption spectra of PP, cGMP, and GTP in presence of Mn 2+ in a substrate to ion ratio of 1:2. The spectra were baseline corrected and smoothed using 25 spectral points. Bands discussed in context with GTP to cGMP and PP turnover by GC and RGC are shown in red. ( B ) FTIR difference spectra of catalytic interaction of RGC with NPE-ATP in the presence of Mn 2+ measured with the same protocol as shown in . NPE-ATP+RGC to ATP+RGC photolysis spectrum (blue line) was derived via global fit analysis and has been smoothed using 18 spectral points due to the poor signal-to-noise-ratio. For comparison, an NPE-ATP+Mn 2+ photolysis spectrum (light blue area) is underlaid. Using the spectra measured for 85 s after UV-light-induced photolysis as baseline the RGC photo-activation difference spectrum averaged over 20–300 s during green illumination with a 532 nm CW laser is shown (green line). A Rh steady state difference spectrum is underlaid for comparison (light green area).

Journal: eLife

Article Title: The inner mechanics of rhodopsin guanylyl cyclase during cGMP-formation revealed by real-time FTIR spectroscopy

doi: 10.7554/eLife.71384

Figure Lengend Snippet: ( A ) Absorption spectra of PP, cGMP, and GTP in presence of Mn 2+ in a substrate to ion ratio of 1:2. The spectra were baseline corrected and smoothed using 25 spectral points. Bands discussed in context with GTP to cGMP and PP turnover by GC and RGC are shown in red. ( B ) FTIR difference spectra of catalytic interaction of RGC with NPE-ATP in the presence of Mn 2+ measured with the same protocol as shown in . NPE-ATP+RGC to ATP+RGC photolysis spectrum (blue line) was derived via global fit analysis and has been smoothed using 18 spectral points due to the poor signal-to-noise-ratio. For comparison, an NPE-ATP+Mn 2+ photolysis spectrum (light blue area) is underlaid. Using the spectra measured for 85 s after UV-light-induced photolysis as baseline the RGC photo-activation difference spectrum averaged over 20–300 s during green illumination with a 532 nm CW laser is shown (green line). A Rh steady state difference spectrum is underlaid for comparison (light green area).

Article Snippet: Caged compounds NPE-GTP and NPE-ATP were purchased from Jena Bioscience GmbH (Jena, Germany).

Techniques: Derivative Assay, Activation Assay