nonlinear regression curve-fitting computer program prism version 2.0 Search Results


codex decay curve  (Akoya Biosciences)
99
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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20 iteration logged data fit function originpro version 8  (OriginLab corp)
90
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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online data analysis tool  (MyAssays Ltd)
90
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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pristine kynol 507–20 carbon  (Kynol Inc)
90
Kynol Inc pristine kynol 507–20 carbon
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).
Pristine Kynol 507–20 Carbon, supplied by Kynol 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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curve fitting program multicycle  (Actimetrics Inc)
90
Actimetrics Inc curve fitting program multicycle
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).
Curve Fitting Program Multicycle, supplied by Actimetrics 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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one-site non-linear regression model graphpad prism 5.03  (GraphPad Software Inc)
90
GraphPad Software Inc one-site non-linear regression model graphpad prism 5.03
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).
One Site Non Linear Regression Model Graphpad Prism 5.03, supplied by GraphPad Software 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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triboscope software  (Hysitron Inc)
90
Hysitron Inc triboscope 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).
Triboscope Software, supplied by Hysitron 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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genfit software  (Genfit Inc)
90
Genfit Inc genfit 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).
Genfit Software, supplied by Genfit 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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prism version 3.0  (GraphPad Software Inc)
90
GraphPad Software Inc prism version 3.0
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).
Prism Version 3.0, supplied by GraphPad Software 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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xrd pw 1130 hv generator  (Philips Healthcare)
90
Philips Healthcare xrd pw 1130 hv generator
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).
Xrd Pw 1130 Hv Generator, supplied by Philips Healthcare, 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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nonnegative least-squares curve fitting  (MathWorks Inc)
90
MathWorks Inc nonnegative least-squares curve fitting
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).
Nonnegative Least Squares Curve Fitting, supplied by MathWorks 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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statistical software version 20  (SPSS Inc)
90
SPSS Inc statistical software version 20
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).
Statistical Software Version 20, supplied by SPSS 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: