matlab® deeranalysis routine Search Results


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MathWorks Inc matlab® deeranalysis routine
Orientation-independent analysis of LITTER with [3]. (a) Background-corrected and modulation depth-normalised LITTER traces shown in (colour) and individual orientation-independent fits by Tikhonov regularization using <t>DeerAnalysis</t> (black), α = 10. (b) Spin–spin distance distributions obtained from the analysis shown in panel b. (c) Averaged LITTER trace (red) and corresponding orientation-independent fit by Tikhonov regularization (black). (d) Spin–spin distance distribution obtained from the analysis shown in panel c. 95% confidence bounds (grey) have been estimated using the Comparative Deer Analyzer in DeerAnalysis2022.
Matlab® Deeranalysis Routine, 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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MathWorks Inc deeranalysis (v. 2019)
Shown in ( A ) is a side view of sites 90 and 237 (PDB ID:1NQH). In ( B ) is shown the distribution for the V90R1-S237R1 spin pair in the absence and presence of R14A with and without vitamin B 12 , where the histogram represents prediction from the vitamin B 12 bound structure (PDB ID: 1NHQ). A significant portion of the predicted distance distribution is below the minimum range observable using double electron-electron resonance (DEER) (1.5–2 nm). Shown in ( C ) are the raw data and background for the V90R1-S237R1 spin pair without and with the R14A mutation, and in ( D ) are the background correct DEER data. These data were analyzed using the DeerNet routine in <t>DEERAnalysis</t> . Histograms are predicted distances generated from the in surfo crystal structures (PDB ID: 1NQG (blue) and PDB ID: 1NQH (red)) using MMM .
Deeranalysis (V. 2019), 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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MathWorks Inc matlab routine fminsearch
Shown in ( A ) is a side view of sites 90 and 237 (PDB ID:1NQH). In ( B ) is shown the distribution for the V90R1-S237R1 spin pair in the absence and presence of R14A with and without vitamin B 12 , where the histogram represents prediction from the vitamin B 12 bound structure (PDB ID: 1NHQ). A significant portion of the predicted distance distribution is below the minimum range observable using double electron-electron resonance (DEER) (1.5–2 nm). Shown in ( C ) are the raw data and background for the V90R1-S237R1 spin pair without and with the R14A mutation, and in ( D ) are the background correct DEER data. These data were analyzed using the DeerNet routine in <t>DEERAnalysis</t> . Histograms are predicted distances generated from the in surfo crystal structures (PDB ID: 1NQG (blue) and PDB ID: 1NQH (red)) using MMM .
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Cayman Chemical 1-oxy-2,2,5,5tetramethylpyrrolinyl3-methyl)methanethiosulfonate
Shown in ( A ) is a side view of sites 90 and 237 (PDB ID:1NQH). In ( B ) is shown the distribution for the V90R1-S237R1 spin pair in the absence and presence of R14A with and without vitamin B 12 , where the histogram represents prediction from the vitamin B 12 bound structure (PDB ID: 1NHQ). A significant portion of the predicted distance distribution is below the minimum range observable using double electron-electron resonance (DEER) (1.5–2 nm). Shown in ( C ) are the raw data and background for the V90R1-S237R1 spin pair without and with the R14A mutation, and in ( D ) are the background correct DEER data. These data were analyzed using the DeerNet routine in <t>DEERAnalysis</t> . Histograms are predicted distances generated from the in surfo crystal structures (PDB ID: 1NQG (blue) and PDB ID: 1NQH (red)) using MMM .
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MathWorks Inc matlab (v. 2020a)
Shown in ( A ) is a side view of sites 90 and 237 (PDB ID:1NQH). In ( B ) is shown the distribution for the V90R1-S237R1 spin pair in the absence and presence of R14A with and without vitamin B 12 , where the histogram represents prediction from the vitamin B 12 bound structure (PDB ID: 1NHQ). A significant portion of the predicted distance distribution is below the minimum range observable using double electron-electron resonance (DEER) (1.5–2 nm). Shown in ( C ) are the raw data and background for the V90R1-S237R1 spin pair without and with the R14A mutation, and in ( D ) are the background correct DEER data. These data were analyzed using the DeerNet routine in <t>DEERAnalysis</t> . Histograms are predicted distances generated from the in surfo crystal structures (PDB ID: 1NQG (blue) and PDB ID: 1NQH (red)) using MMM .
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Shown in ( A ) is a side view of sites 90 and 237 (PDB ID:1NQH). In ( B ) is shown the distribution for the V90R1-S237R1 spin pair in the absence and presence of R14A with and without vitamin B 12 , where the histogram represents prediction from the vitamin B 12 bound structure (PDB ID: 1NHQ). A significant portion of the predicted distance distribution is below the minimum range observable using double electron-electron resonance (DEER) (1.5–2 nm). Shown in ( C ) are the raw data and background for the V90R1-S237R1 spin pair without and with the R14A mutation, and in ( D ) are the background correct DEER data. These data were analyzed using the DeerNet routine in <t>DEERAnalysis</t> . Histograms are predicted distances generated from the in surfo crystal structures (PDB ID: 1NQG (blue) and PDB ID: 1NQH (red)) using MMM .
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Image Search Results


Orientation-independent analysis of LITTER with [3]. (a) Background-corrected and modulation depth-normalised LITTER traces shown in (colour) and individual orientation-independent fits by Tikhonov regularization using DeerAnalysis (black), α = 10. (b) Spin–spin distance distributions obtained from the analysis shown in panel b. (c) Averaged LITTER trace (red) and corresponding orientation-independent fit by Tikhonov regularization (black). (d) Spin–spin distance distribution obtained from the analysis shown in panel c. 95% confidence bounds (grey) have been estimated using the Comparative Deer Analyzer in DeerAnalysis2022.

Journal: Physical Chemistry Chemical Physics

Article Title: Determining and controlling conformational information from orientationally selective light-induced triplet–triplet electron resonance spectroscopy for a set of bis-porphyrin rulers

doi: 10.1039/d3cp03454b

Figure Lengend Snippet: Orientation-independent analysis of LITTER with [3]. (a) Background-corrected and modulation depth-normalised LITTER traces shown in (colour) and individual orientation-independent fits by Tikhonov regularization using DeerAnalysis (black), α = 10. (b) Spin–spin distance distributions obtained from the analysis shown in panel b. (c) Averaged LITTER trace (red) and corresponding orientation-independent fit by Tikhonov regularization (black). (d) Spin–spin distance distribution obtained from the analysis shown in panel c. 95% confidence bounds (grey) have been estimated using the Comparative Deer Analyzer in DeerAnalysis2022.

Article Snippet: For the orientation-independent analysis of LITTER and DEER, the dipolar traces acquired at different field positions were averaged weighted by the corresponding spectral intensities to obtain an orientation-independent form factor, which was then analysed via Fourier Transform and Tikhonov regularization using the Matlab® DeerAnalysis routine to extract the corresponding distance distribution.

Techniques:

Shown in ( A ) is a side view of sites 90 and 237 (PDB ID:1NQH). In ( B ) is shown the distribution for the V90R1-S237R1 spin pair in the absence and presence of R14A with and without vitamin B 12 , where the histogram represents prediction from the vitamin B 12 bound structure (PDB ID: 1NHQ). A significant portion of the predicted distance distribution is below the minimum range observable using double electron-electron resonance (DEER) (1.5–2 nm). Shown in ( C ) are the raw data and background for the V90R1-S237R1 spin pair without and with the R14A mutation, and in ( D ) are the background correct DEER data. These data were analyzed using the DeerNet routine in DEERAnalysis . Histograms are predicted distances generated from the in surfo crystal structures (PDB ID: 1NQG (blue) and PDB ID: 1NQH (red)) using MMM .

Journal: eLife

Article Title: Structural intermediates observed only in intact Escherichia coli indicate a mechanism for TonB-dependent transport

doi: 10.7554/eLife.68548

Figure Lengend Snippet: Shown in ( A ) is a side view of sites 90 and 237 (PDB ID:1NQH). In ( B ) is shown the distribution for the V90R1-S237R1 spin pair in the absence and presence of R14A with and without vitamin B 12 , where the histogram represents prediction from the vitamin B 12 bound structure (PDB ID: 1NHQ). A significant portion of the predicted distance distribution is below the minimum range observable using double electron-electron resonance (DEER) (1.5–2 nm). Shown in ( C ) are the raw data and background for the V90R1-S237R1 spin pair without and with the R14A mutation, and in ( D ) are the background correct DEER data. These data were analyzed using the DeerNet routine in DEERAnalysis . Histograms are predicted distances generated from the in surfo crystal structures (PDB ID: 1NQG (blue) and PDB ID: 1NQH (red)) using MMM .

Article Snippet: Software, algorithm , DeerAnalysis (v. 2019) , Gunnar Jeschke (ETH Zürich) , MATLAB routine for the analysis of pulse EPR data , Used to examine DEER data.

Techniques: Mutagenesis, Generated

Journal: eLife

Article Title: Structural intermediates observed only in intact Escherichia coli indicate a mechanism for TonB-dependent transport

doi: 10.7554/eLife.68548

Figure Lengend Snippet:

Article Snippet: Software, algorithm , DeerAnalysis (v. 2019) , Gunnar Jeschke (ETH Zürich) , MATLAB routine for the analysis of pulse EPR data , Used to examine DEER data.

Techniques: Recombinant, Plasmid Preparation, Construct, Sequencing, Membrane, Labeling, Software, In Silico