nonlinear curve-fitting program prism v, version 2.0 Search Results


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Akoya Biosciences codex decay curve
At the mixing time of 250 ms, the bound state <t>CODEX</t> signal decays to 0.65 of the reference experiment (A, inset yellow); the decay rate fits to an inter-CF 3 distance of 13.6 ±3.0 Å, with the exponential decay fit curve of 0.5 * e −0.0053*t −0.5, matching the expected inter-dimer distance at the C-terminus of the parallel dimer (C). In contrast, the free state CODEX signal is almost the same as the reference experiment (A, inset blue) through all mixing times, corresponding to a large inter dimer distance at the C-terminus of more than 20 Å, agreeing with the anti-parallel dimer (B). Example <t>CODEX</t> <t>decay</t> curves at different inter fluorine distances are shown (A, grey). 30% of the bound state CitApc protein present in the citrate free sample caused the minor CODEX decay. The CODEX decay curve could be acquired beyond the 19 F T 1 of 321ms (Figure S10), thanks to an eight-fold DNP signal enhancement (Figure S9B).
Codex Decay Curve, supplied by Akoya Biosciences, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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MyAssays Ltd online data analysis tool
At the mixing time of 250 ms, the bound state <t>CODEX</t> signal decays to 0.65 of the reference experiment (A, inset yellow); the decay rate fits to an inter-CF 3 distance of 13.6 ±3.0 Å, with the exponential decay fit curve of 0.5 * e −0.0053*t −0.5, matching the expected inter-dimer distance at the C-terminus of the parallel dimer (C). In contrast, the free state CODEX signal is almost the same as the reference experiment (A, inset blue) through all mixing times, corresponding to a large inter dimer distance at the C-terminus of more than 20 Å, agreeing with the anti-parallel dimer (B). Example <t>CODEX</t> <t>decay</t> curves at different inter fluorine distances are shown (A, grey). 30% of the bound state CitApc protein present in the citrate free sample caused the minor CODEX decay. The CODEX decay curve could be acquired beyond the 19 F T 1 of 321ms (Figure S10), thanks to an eight-fold DNP signal enhancement (Figure S9B).
Online Data Analysis Tool, supplied by MyAssays Ltd, 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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online data analysis tool - by Bioz Stars, 2026-08
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OriginLab corp 20 iteration logged data fit function originpro version 8
At the mixing time of 250 ms, the bound state <t>CODEX</t> signal decays to 0.65 of the reference experiment (A, inset yellow); the decay rate fits to an inter-CF 3 distance of 13.6 ±3.0 Å, with the exponential decay fit curve of 0.5 * e −0.0053*t −0.5, matching the expected inter-dimer distance at the C-terminus of the parallel dimer (C). In contrast, the free state CODEX signal is almost the same as the reference experiment (A, inset blue) through all mixing times, corresponding to a large inter dimer distance at the C-terminus of more than 20 Å, agreeing with the anti-parallel dimer (B). Example <t>CODEX</t> <t>decay</t> curves at different inter fluorine distances are shown (A, grey). 30% of the bound state CitApc protein present in the citrate free sample caused the minor CODEX decay. The CODEX decay curve could be acquired beyond the 19 F T 1 of 321ms (Figure S10), thanks to an eight-fold DNP signal enhancement (Figure S9B).
20 Iteration Logged Data Fit Function Originpro Version 8, supplied by OriginLab corp, 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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20 iteration logged data fit function originpro version 8 - by Bioz Stars, 2026-08
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OriginLab corp origin 8.5 software
At the mixing time of 250 ms, the bound state <t>CODEX</t> signal decays to 0.65 of the reference experiment (A, inset yellow); the decay rate fits to an inter-CF 3 distance of 13.6 ±3.0 Å, with the exponential decay fit curve of 0.5 * e −0.0053*t −0.5, matching the expected inter-dimer distance at the C-terminus of the parallel dimer (C). In contrast, the free state CODEX signal is almost the same as the reference experiment (A, inset blue) through all mixing times, corresponding to a large inter dimer distance at the C-terminus of more than 20 Å, agreeing with the anti-parallel dimer (B). Example <t>CODEX</t> <t>decay</t> curves at different inter fluorine distances are shown (A, grey). 30% of the bound state CitApc protein present in the citrate free sample caused the minor CODEX decay. The CODEX decay curve could be acquired beyond the 19 F T 1 of 321ms (Figure S10), thanks to an eight-fold DNP signal enhancement (Figure S9B).
Origin 8.5 Software, supplied by OriginLab corp, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nonlinear+curve-fitting+program+prism+v%2C+version+2%2E0/origin+8+0+software/pm26976361-85-12-15
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origin 8.5 software - by Bioz Stars, 2026-08
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SoftMax Inc jo urn al pr e-p roo f 20 pro-based four-parameter method
At the mixing time of 250 ms, the bound state <t>CODEX</t> signal decays to 0.65 of the reference experiment (A, inset yellow); the decay rate fits to an inter-CF 3 distance of 13.6 ±3.0 Å, with the exponential decay fit curve of 0.5 * e −0.0053*t −0.5, matching the expected inter-dimer distance at the C-terminus of the parallel dimer (C). In contrast, the free state CODEX signal is almost the same as the reference experiment (A, inset blue) through all mixing times, corresponding to a large inter dimer distance at the C-terminus of more than 20 Å, agreeing with the anti-parallel dimer (B). Example <t>CODEX</t> <t>decay</t> curves at different inter fluorine distances are shown (A, grey). 30% of the bound state CitApc protein present in the citrate free sample caused the minor CODEX decay. The CODEX decay curve could be acquired beyond the 19 F T 1 of 321ms (Figure S10), thanks to an eight-fold DNP signal enhancement (Figure S9B).
Jo Urn Al Pr E P Roo F 20 Pro Based Four Parameter Method, supplied by SoftMax Inc, 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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OriginLab corp data analysis software originpro 7.5
At the mixing time of 250 ms, the bound state <t>CODEX</t> signal decays to 0.65 of the reference experiment (A, inset yellow); the decay rate fits to an inter-CF 3 distance of 13.6 ±3.0 Å, with the exponential decay fit curve of 0.5 * e −0.0053*t −0.5, matching the expected inter-dimer distance at the C-terminus of the parallel dimer (C). In contrast, the free state CODEX signal is almost the same as the reference experiment (A, inset blue) through all mixing times, corresponding to a large inter dimer distance at the C-terminus of more than 20 Å, agreeing with the anti-parallel dimer (B). Example <t>CODEX</t> <t>decay</t> curves at different inter fluorine distances are shown (A, grey). 30% of the bound state CitApc protein present in the citrate free sample caused the minor CODEX decay. The CODEX decay curve could be acquired beyond the 19 F T 1 of 321ms (Figure S10), thanks to an eight-fold DNP signal enhancement (Figure S9B).
Data Analysis Software Originpro 7.5, supplied by OriginLab corp, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nonlinear+curve-fitting+program+prism+v%2C+version+2%2E0/originpro+software/pm22921426-85-25-30
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data analysis software originpro 7.5 - by Bioz Stars, 2026-08
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Satlantic Inc firepro
At the mixing time of 250 ms, the bound state <t>CODEX</t> signal decays to 0.65 of the reference experiment (A, inset yellow); the decay rate fits to an inter-CF 3 distance of 13.6 ±3.0 Å, with the exponential decay fit curve of 0.5 * e −0.0053*t −0.5, matching the expected inter-dimer distance at the C-terminus of the parallel dimer (C). In contrast, the free state CODEX signal is almost the same as the reference experiment (A, inset blue) through all mixing times, corresponding to a large inter dimer distance at the C-terminus of more than 20 Å, agreeing with the anti-parallel dimer (B). Example <t>CODEX</t> <t>decay</t> curves at different inter fluorine distances are shown (A, grey). 30% of the bound state CitApc protein present in the citrate free sample caused the minor CODEX decay. The CODEX decay curve could be acquired beyond the 19 F T 1 of 321ms (Figure S10), thanks to an eight-fold DNP signal enhancement (Figure S9B).
Firepro, supplied by Satlantic Inc, 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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Image Search Results


At the mixing time of 250 ms, the bound state CODEX signal decays to 0.65 of the reference experiment (A, inset yellow); the decay rate fits to an inter-CF 3 distance of 13.6 ±3.0 Å, with the exponential decay fit curve of 0.5 * e −0.0053*t −0.5, matching the expected inter-dimer distance at the C-terminus of the parallel dimer (C). In contrast, the free state CODEX signal is almost the same as the reference experiment (A, inset blue) through all mixing times, corresponding to a large inter dimer distance at the C-terminus of more than 20 Å, agreeing with the anti-parallel dimer (B). Example CODEX decay curves at different inter fluorine distances are shown (A, grey). 30% of the bound state CitApc protein present in the citrate free sample caused the minor CODEX decay. The CODEX decay curve could be acquired beyond the 19 F T 1 of 321ms (Figure S10), thanks to an eight-fold DNP signal enhancement (Figure S9B).

Journal: bioRxiv

Article Title: Mechanism of sensor kinase CitA transmembrane signaling

doi: 10.1101/2023.02.06.527302

Figure Lengend Snippet: At the mixing time of 250 ms, the bound state CODEX signal decays to 0.65 of the reference experiment (A, inset yellow); the decay rate fits to an inter-CF 3 distance of 13.6 ±3.0 Å, with the exponential decay fit curve of 0.5 * e −0.0053*t −0.5, matching the expected inter-dimer distance at the C-terminus of the parallel dimer (C). In contrast, the free state CODEX signal is almost the same as the reference experiment (A, inset blue) through all mixing times, corresponding to a large inter dimer distance at the C-terminus of more than 20 Å, agreeing with the anti-parallel dimer (B). Example CODEX decay curves at different inter fluorine distances are shown (A, grey). 30% of the bound state CitApc protein present in the citrate free sample caused the minor CODEX decay. The CODEX decay curve could be acquired beyond the 19 F T 1 of 321ms (Figure S10), thanks to an eight-fold DNP signal enhancement (Figure S9B).

Article Snippet: An inter-CF 3 group distance shorter than about 20 Å is measurable by fitting the CODEX decay curve, and a distance larger than 20 Å can be determined in the absence of decay within the 250 ms of CODEX.

Techniques: