mcmc calculations Search Results


proc mcmc  (SAS institute)
90
SAS institute proc mcmc
Proc Mcmc, supplied by SAS institute, 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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mcmc tree program  (Abacus Concepts)
90
Abacus Concepts mcmc tree program
Mcmc Tree Program, supplied by Abacus Concepts, 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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mcma  (Cell Signaling Technology Inc)
96
Cell Signaling Technology Inc mcma
Mcma, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mcmc diagnostics toolbox  (MathWorks Inc)
90
MathWorks Inc mcmc diagnostics toolbox
Mcmc Diagnostics Toolbox, 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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mcmc sampling  (Hormel Health Labs)
90
Hormel Health Labs mcmc sampling
Mcmc Sampling, supplied by Hormel Health Labs, 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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mcmc calculations  (MathWorks Inc)
90
MathWorks Inc mcmc calculations
a, Freely jointed chain (FJC) model of a POC-containing peptide βCAT. Each unit in the polymer has an electrical charge and a typical distance α between residues. Phosphoserine PTMs pS1 and pS2 add a charge of −2 to that unit. b, Electric potential profile (color gradient) in the MspA pore26. The POC was confined within the physical boundaries of MspA (black) and anchored at the Hel308 hold point (pink x). The volumetric map of the MspA cross-section is shown in gray. c, Snapshots of the polymer configuration within MspA from <t>MCMC</t> calculations for the p2βCAT POC at five Hel308 steps. The phosphoserine residue (pS2) (purple) is observed to move through the pore in a nonlinear fashion. Note that the POC polymer gets stretched towards Hel308 step 19, after which the PTM moves into the pore lumen and the polymer relaxes. Orange lines indicate the sensing region of MspA. d, Mean z-location of the pS2 PTM versus Hel308 step number. e, Same for all PTMs in the peptide variants. f, Probability that a pS occupied the sensing region for various βCAT PTM variants versus Hel308 step. g, Experimentally measured ion currents for βCAT phosphopeptide variants where the ion current measured for the non-PTM βCAT was subtracted (from data in Fig. 1g). Shaded error bar is the standard deviation.
Mcmc Calculations, 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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abbott’s formula  (Abbott Laboratories)
90
Abbott Laboratories abbott’s formula
a, Freely jointed chain (FJC) model of a POC-containing peptide βCAT. Each unit in the polymer has an electrical charge and a typical distance α between residues. Phosphoserine PTMs pS1 and pS2 add a charge of −2 to that unit. b, Electric potential profile (color gradient) in the MspA pore26. The POC was confined within the physical boundaries of MspA (black) and anchored at the Hel308 hold point (pink x). The volumetric map of the MspA cross-section is shown in gray. c, Snapshots of the polymer configuration within MspA from <t>MCMC</t> calculations for the p2βCAT POC at five Hel308 steps. The phosphoserine residue (pS2) (purple) is observed to move through the pore in a nonlinear fashion. Note that the POC polymer gets stretched towards Hel308 step 19, after which the PTM moves into the pore lumen and the polymer relaxes. Orange lines indicate the sensing region of MspA. d, Mean z-location of the pS2 PTM versus Hel308 step number. e, Same for all PTMs in the peptide variants. f, Probability that a pS occupied the sensing region for various βCAT PTM variants versus Hel308 step. g, Experimentally measured ion currents for βCAT phosphopeptide variants where the ion current measured for the non-PTM βCAT was subtracted (from data in Fig. 1g). Shaded error bar is the standard deviation.
Abbott’s Formula, supplied by Abbott Laboratories, 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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cfx system  (Bio-Rad)
90
Bio-Rad cfx system
a, Freely jointed chain (FJC) model of a POC-containing peptide βCAT. Each unit in the polymer has an electrical charge and a typical distance α between residues. Phosphoserine PTMs pS1 and pS2 add a charge of −2 to that unit. b, Electric potential profile (color gradient) in the MspA pore26. The POC was confined within the physical boundaries of MspA (black) and anchored at the Hel308 hold point (pink x). The volumetric map of the MspA cross-section is shown in gray. c, Snapshots of the polymer configuration within MspA from <t>MCMC</t> calculations for the p2βCAT POC at five Hel308 steps. The phosphoserine residue (pS2) (purple) is observed to move through the pore in a nonlinear fashion. Note that the POC polymer gets stretched towards Hel308 step 19, after which the PTM moves into the pore lumen and the polymer relaxes. Orange lines indicate the sensing region of MspA. d, Mean z-location of the pS2 PTM versus Hel308 step number. e, Same for all PTMs in the peptide variants. f, Probability that a pS occupied the sensing region for various βCAT PTM variants versus Hel308 step. g, Experimentally measured ion currents for βCAT phosphopeptide variants where the ion current measured for the non-PTM βCAT was subtracted (from data in Fig. 1g). Shaded error bar is the standard deviation.
Cfx System, supplied by Bio-Rad, 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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mcmc and particle filters  (MathWorks Inc)
90
MathWorks Inc mcmc and particle filters
a, Freely jointed chain (FJC) model of a POC-containing peptide βCAT. Each unit in the polymer has an electrical charge and a typical distance α between residues. Phosphoserine PTMs pS1 and pS2 add a charge of −2 to that unit. b, Electric potential profile (color gradient) in the MspA pore26. The POC was confined within the physical boundaries of MspA (black) and anchored at the Hel308 hold point (pink x). The volumetric map of the MspA cross-section is shown in gray. c, Snapshots of the polymer configuration within MspA from <t>MCMC</t> calculations for the p2βCAT POC at five Hel308 steps. The phosphoserine residue (pS2) (purple) is observed to move through the pore in a nonlinear fashion. Note that the POC polymer gets stretched towards Hel308 step 19, after which the PTM moves into the pore lumen and the polymer relaxes. Orange lines indicate the sensing region of MspA. d, Mean z-location of the pS2 PTM versus Hel308 step number. e, Same for all PTMs in the peptide variants. f, Probability that a pS occupied the sensing region for various βCAT PTM variants versus Hel308 step. g, Experimentally measured ion currents for βCAT phosphopeptide variants where the ion current measured for the non-PTM βCAT was subtracted (from data in Fig. 1g). Shaded error bar is the standard deviation.
Mcmc And Particle Filters, 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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jags version 3.3.0  (SourceForge net)
90
SourceForge net jags version 3.3.0
a, Freely jointed chain (FJC) model of a POC-containing peptide βCAT. Each unit in the polymer has an electrical charge and a typical distance α between residues. Phosphoserine PTMs pS1 and pS2 add a charge of −2 to that unit. b, Electric potential profile (color gradient) in the MspA pore26. The POC was confined within the physical boundaries of MspA (black) and anchored at the Hel308 hold point (pink x). The volumetric map of the MspA cross-section is shown in gray. c, Snapshots of the polymer configuration within MspA from <t>MCMC</t> calculations for the p2βCAT POC at five Hel308 steps. The phosphoserine residue (pS2) (purple) is observed to move through the pore in a nonlinear fashion. Note that the POC polymer gets stretched towards Hel308 step 19, after which the PTM moves into the pore lumen and the polymer relaxes. Orange lines indicate the sensing region of MspA. d, Mean z-location of the pS2 PTM versus Hel308 step number. e, Same for all PTMs in the peptide variants. f, Probability that a pS occupied the sensing region for various βCAT PTM variants versus Hel308 step. g, Experimentally measured ion currents for βCAT phosphopeptide variants where the ion current measured for the non-PTM βCAT was subtracted (from data in Fig. 1g). Shaded error bar is the standard deviation.
Jags Version 3.3.0, supplied by SourceForge net, 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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jags version 3.3.0 - by Bioz Stars, 2026-04
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mx3000p software  (Agilent technologies)
90
Agilent technologies mx3000p software
a, Freely jointed chain (FJC) model of a POC-containing peptide βCAT. Each unit in the polymer has an electrical charge and a typical distance α between residues. Phosphoserine PTMs pS1 and pS2 add a charge of −2 to that unit. b, Electric potential profile (color gradient) in the MspA pore26. The POC was confined within the physical boundaries of MspA (black) and anchored at the Hel308 hold point (pink x). The volumetric map of the MspA cross-section is shown in gray. c, Snapshots of the polymer configuration within MspA from <t>MCMC</t> calculations for the p2βCAT POC at five Hel308 steps. The phosphoserine residue (pS2) (purple) is observed to move through the pore in a nonlinear fashion. Note that the POC polymer gets stretched towards Hel308 step 19, after which the PTM moves into the pore lumen and the polymer relaxes. Orange lines indicate the sensing region of MspA. d, Mean z-location of the pS2 PTM versus Hel308 step number. e, Same for all PTMs in the peptide variants. f, Probability that a pS occupied the sensing region for various βCAT PTM variants versus Hel308 step. g, Experimentally measured ion currents for βCAT phosphopeptide variants where the ion current measured for the non-PTM βCAT was subtracted (from data in Fig. 1g). Shaded error bar is the standard deviation.
Mx3000p Software, supplied by Agilent technologies, 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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mean mcmc phase-space density  (PhaseSpace Inc)
90
PhaseSpace Inc mean mcmc phase-space density
a, Freely jointed chain (FJC) model of a POC-containing peptide βCAT. Each unit in the polymer has an electrical charge and a typical distance α between residues. Phosphoserine PTMs pS1 and pS2 add a charge of −2 to that unit. b, Electric potential profile (color gradient) in the MspA pore26. The POC was confined within the physical boundaries of MspA (black) and anchored at the Hel308 hold point (pink x). The volumetric map of the MspA cross-section is shown in gray. c, Snapshots of the polymer configuration within MspA from <t>MCMC</t> calculations for the p2βCAT POC at five Hel308 steps. The phosphoserine residue (pS2) (purple) is observed to move through the pore in a nonlinear fashion. Note that the POC polymer gets stretched towards Hel308 step 19, after which the PTM moves into the pore lumen and the polymer relaxes. Orange lines indicate the sensing region of MspA. d, Mean z-location of the pS2 PTM versus Hel308 step number. e, Same for all PTMs in the peptide variants. f, Probability that a pS occupied the sensing region for various βCAT PTM variants versus Hel308 step. g, Experimentally measured ion currents for βCAT phosphopeptide variants where the ion current measured for the non-PTM βCAT was subtracted (from data in Fig. 1g). Shaded error bar is the standard deviation.
Mean Mcmc Phase Space Density, supplied by PhaseSpace 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


a, Freely jointed chain (FJC) model of a POC-containing peptide βCAT. Each unit in the polymer has an electrical charge and a typical distance α between residues. Phosphoserine PTMs pS1 and pS2 add a charge of −2 to that unit. b, Electric potential profile (color gradient) in the MspA pore26. The POC was confined within the physical boundaries of MspA (black) and anchored at the Hel308 hold point (pink x). The volumetric map of the MspA cross-section is shown in gray. c, Snapshots of the polymer configuration within MspA from MCMC calculations for the p2βCAT POC at five Hel308 steps. The phosphoserine residue (pS2) (purple) is observed to move through the pore in a nonlinear fashion. Note that the POC polymer gets stretched towards Hel308 step 19, after which the PTM moves into the pore lumen and the polymer relaxes. Orange lines indicate the sensing region of MspA. d, Mean z-location of the pS2 PTM versus Hel308 step number. e, Same for all PTMs in the peptide variants. f, Probability that a pS occupied the sensing region for various βCAT PTM variants versus Hel308 step. g, Experimentally measured ion currents for βCAT phosphopeptide variants where the ion current measured for the non-PTM βCAT was subtracted (from data in Fig. 1g). Shaded error bar is the standard deviation.

Journal: Nature biotechnology

Article Title: Detection of phosphorylation post-translational modifications along single peptides with nanopores

doi: 10.1038/s41587-023-01839-z

Figure Lengend Snippet: a, Freely jointed chain (FJC) model of a POC-containing peptide βCAT. Each unit in the polymer has an electrical charge and a typical distance α between residues. Phosphoserine PTMs pS1 and pS2 add a charge of −2 to that unit. b, Electric potential profile (color gradient) in the MspA pore26. The POC was confined within the physical boundaries of MspA (black) and anchored at the Hel308 hold point (pink x). The volumetric map of the MspA cross-section is shown in gray. c, Snapshots of the polymer configuration within MspA from MCMC calculations for the p2βCAT POC at five Hel308 steps. The phosphoserine residue (pS2) (purple) is observed to move through the pore in a nonlinear fashion. Note that the POC polymer gets stretched towards Hel308 step 19, after which the PTM moves into the pore lumen and the polymer relaxes. Orange lines indicate the sensing region of MspA. d, Mean z-location of the pS2 PTM versus Hel308 step number. e, Same for all PTMs in the peptide variants. f, Probability that a pS occupied the sensing region for various βCAT PTM variants versus Hel308 step. g, Experimentally measured ion currents for βCAT phosphopeptide variants where the ion current measured for the non-PTM βCAT was subtracted (from data in Fig. 1g). Shaded error bar is the standard deviation.

Article Snippet: MCMC calculations 26 were implemented in MATLAB.

Techniques: Polymer, Residue, Phospho-proteomics, Standard Deviation