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e. coli-optimized codon sequence for ubiquitin  (GenScript corporation)

 
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    GenScript corporation e. coli-optimized codon sequence for ubiquitin
    Internal autocorrelation function for the amide H–N bond vector of Arg 74 in the C-terminal tail of <t>ubiquitin.</t> 15 N R 1 , R 2 , and NOE values were calculated, utilizing the internal autocorrelation function derived from 2 μs CHARMM36 simulations (green) and an isotropic global tumbling time of 4.10 ns. Those derived relaxation values are precisely fitted at 600 MHz (blue) and 900 MHz (red), utilizing the ( S f 2 ,τ s , S 2 ) representation with parameter sets (0.767, 1.252 ns, 0.398) and (0.790, 0.813 ns, 0.423), respectively.
    E. Coli Optimized Codon Sequence For Ubiquitin, supplied by GenScript corporation, 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/result/e. coli-optimized codon sequence for ubiquitin/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    e. coli-optimized codon sequence for ubiquitin - by Bioz Stars, 2026-05
    90/100 stars

    Images

    1) Product Images from "Molecular Dynamics-Assisted Optimization of Protein NMR Relaxation Analysis"

    Article Title: Molecular Dynamics-Assisted Optimization of Protein NMR Relaxation Analysis

    Journal: Journal of Chemical Theory and Computation

    doi: 10.1021/acs.jctc.1c01165

    Internal autocorrelation function for the amide H–N bond vector of Arg 74 in the C-terminal tail of ubiquitin. 15 N R 1 , R 2 , and NOE values were calculated, utilizing the internal autocorrelation function derived from 2 μs CHARMM36 simulations (green) and an isotropic global tumbling time of 4.10 ns. Those derived relaxation values are precisely fitted at 600 MHz (blue) and 900 MHz (red), utilizing the ( S f 2 ,τ s , S 2 ) representation with parameter sets (0.767, 1.252 ns, 0.398) and (0.790, 0.813 ns, 0.423), respectively.
    Figure Legend Snippet: Internal autocorrelation function for the amide H–N bond vector of Arg 74 in the C-terminal tail of ubiquitin. 15 N R 1 , R 2 , and NOE values were calculated, utilizing the internal autocorrelation function derived from 2 μs CHARMM36 simulations (green) and an isotropic global tumbling time of 4.10 ns. Those derived relaxation values are precisely fitted at 600 MHz (blue) and 900 MHz (red), utilizing the ( S f 2 ,τ s , S 2 ) representation with parameter sets (0.767, 1.252 ns, 0.398) and (0.790, 0.813 ns, 0.423), respectively.

    Techniques Used: Plasmid Preparation, Derivative Assay

    Internal bond vector autocorrelation functions for the C-terminal tail (Leu 73 to Gly 76) and mobile internal loop (Leu 8 to Thr 12) of ubiquitin as calculated from 2 μs of simulation with CHARMM36 (panels A and C) and AMBER 14SB (panels B and D).
    Figure Legend Snippet: Internal bond vector autocorrelation functions for the C-terminal tail (Leu 73 to Gly 76) and mobile internal loop (Leu 8 to Thr 12) of ubiquitin as calculated from 2 μs of simulation with CHARMM36 (panels A and C) and AMBER 14SB (panels B and D).

    Techniques Used: Plasmid Preparation

    Standard deviations for the back-prediction of the six force field-derived internal autocorrelation functions at 600 MHz 1 H for the nine mobile residues of ubiquitin utilizing the ( S f 2 , S H 2 , S N 2 ) and ( S f 2 , S 2 ,τ s ) representations (panels A and B, respectively), as averaged over the time interval between 30 ps and the assumed global tumbling time τ M .
    Figure Legend Snippet: Standard deviations for the back-prediction of the six force field-derived internal autocorrelation functions at 600 MHz 1 H for the nine mobile residues of ubiquitin utilizing the ( S f 2 , S H 2 , S N 2 ) and ( S f 2 , S 2 ,τ s ) representations (panels A and B, respectively), as averaged over the time interval between 30 ps and the assumed global tumbling time τ M .

    Techniques Used: Derivative Assay

    Standard deviations for the back-prediction of the six force field-derived internal autocorrelation functions at 600 MHz (panel A) and 900 MHz (panel B) for the nine mobile ubiquitin residues, utilizing the optimized time constant-constrained triexponential (TCCT) representation ( S f 2 , S h 2 , S x 2 ) as averaged over the time interval between 30 ps and the assumed global tumbling time τ M .
    Figure Legend Snippet: Standard deviations for the back-prediction of the six force field-derived internal autocorrelation functions at 600 MHz (panel A) and 900 MHz (panel B) for the nine mobile ubiquitin residues, utilizing the optimized time constant-constrained triexponential (TCCT) representation ( S f 2 , S h 2 , S x 2 ) as averaged over the time interval between 30 ps and the assumed global tumbling time τ M .

    Techniques Used: Derivative Assay

    Experimentally determined values of the internal bond vector autocorrelation functions of the ubiquitin backbone at 4.10 ns are displayed as rainbow coloring, with dark blue set to 1.0, green set to 0.69, and red set to 0.0. Residues lacking experimental measurements are set to dark blue.
    Figure Legend Snippet: Experimentally determined values of the internal bond vector autocorrelation functions of the ubiquitin backbone at 4.10 ns are displayed as rainbow coloring, with dark blue set to 1.0, green set to 0.69, and red set to 0.0. Residues lacking experimental measurements are set to dark blue.

    Techniques Used: Plasmid Preparation

    Experimentally determined internal bond vector autocorrelation functions for the C-terminal tail of a ubiquitin sample having an average τ M of 4.10 ns and an ellipsoidal asymmetry of 1.22 utilizing the optimized TCCT representation, with data from 600 MHz indicated in blue and the 900 MHz data indicated in red. The Monte Carlo-derived 95% confidence limits (dashes) were determined, assuming uncertainties of 1%, 1%, 0.01, and 1% for the R 1 , R 2 , NOE, and bond-specific τ M values, respectively.
    Figure Legend Snippet: Experimentally determined internal bond vector autocorrelation functions for the C-terminal tail of a ubiquitin sample having an average τ M of 4.10 ns and an ellipsoidal asymmetry of 1.22 utilizing the optimized TCCT representation, with data from 600 MHz indicated in blue and the 900 MHz data indicated in red. The Monte Carlo-derived 95% confidence limits (dashes) were determined, assuming uncertainties of 1%, 1%, 0.01, and 1% for the R 1 , R 2 , NOE, and bond-specific τ M values, respectively.

    Techniques Used: Plasmid Preparation, Derivative Assay



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    e. coli-optimized codon sequence for ubiquitin  (GenScript corporation)
    90
    GenScript corporation e. coli-optimized codon sequence for ubiquitin
    Internal autocorrelation function for the amide H–N bond vector of Arg 74 in the C-terminal tail of <t>ubiquitin.</t> 15 N R 1 , R 2 , and NOE values were calculated, utilizing the internal autocorrelation function derived from 2 μs CHARMM36 simulations (green) and an isotropic global tumbling time of 4.10 ns. Those derived relaxation values are precisely fitted at 600 MHz (blue) and 900 MHz (red), utilizing the ( S f 2 ,τ s , S 2 ) representation with parameter sets (0.767, 1.252 ns, 0.398) and (0.790, 0.813 ns, 0.423), respectively.
    E. Coli Optimized Codon Sequence For Ubiquitin, supplied by GenScript corporation, 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/result/e. coli-optimized codon sequence for ubiquitin/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    e. coli-optimized codon sequence for ubiquitin - by Bioz Stars, 2026-05
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    Internal autocorrelation function for the amide H–N bond vector of Arg 74 in the C-terminal tail of ubiquitin. 15 N R 1 , R 2 , and NOE values were calculated, utilizing the internal autocorrelation function derived from 2 μs CHARMM36 simulations (green) and an isotropic global tumbling time of 4.10 ns. Those derived relaxation values are precisely fitted at 600 MHz (blue) and 900 MHz (red), utilizing the ( S f 2 ,τ s , S 2 ) representation with parameter sets (0.767, 1.252 ns, 0.398) and (0.790, 0.813 ns, 0.423), respectively.

    Journal: Journal of Chemical Theory and Computation

    Article Title: Molecular Dynamics-Assisted Optimization of Protein NMR Relaxation Analysis

    doi: 10.1021/acs.jctc.1c01165

    Figure Lengend Snippet: Internal autocorrelation function for the amide H–N bond vector of Arg 74 in the C-terminal tail of ubiquitin. 15 N R 1 , R 2 , and NOE values were calculated, utilizing the internal autocorrelation function derived from 2 μs CHARMM36 simulations (green) and an isotropic global tumbling time of 4.10 ns. Those derived relaxation values are precisely fitted at 600 MHz (blue) and 900 MHz (red), utilizing the ( S f 2 ,τ s , S 2 ) representation with parameter sets (0.767, 1.252 ns, 0.398) and (0.790, 0.813 ns, 0.423), respectively.

    Article Snippet: An E. coli -optimized codon sequence for ubiquitin (Genscript) was cloned into the expression vector pET11a and transformed into BL21-STAR (DE3) (Invitrogen).

    Techniques: Plasmid Preparation, Derivative Assay

    Internal bond vector autocorrelation functions for the C-terminal tail (Leu 73 to Gly 76) and mobile internal loop (Leu 8 to Thr 12) of ubiquitin as calculated from 2 μs of simulation with CHARMM36 (panels A and C) and AMBER 14SB (panels B and D).

    Journal: Journal of Chemical Theory and Computation

    Article Title: Molecular Dynamics-Assisted Optimization of Protein NMR Relaxation Analysis

    doi: 10.1021/acs.jctc.1c01165

    Figure Lengend Snippet: Internal bond vector autocorrelation functions for the C-terminal tail (Leu 73 to Gly 76) and mobile internal loop (Leu 8 to Thr 12) of ubiquitin as calculated from 2 μs of simulation with CHARMM36 (panels A and C) and AMBER 14SB (panels B and D).

    Article Snippet: An E. coli -optimized codon sequence for ubiquitin (Genscript) was cloned into the expression vector pET11a and transformed into BL21-STAR (DE3) (Invitrogen).

    Techniques: Plasmid Preparation

    Standard deviations for the back-prediction of the six force field-derived internal autocorrelation functions at 600 MHz 1 H for the nine mobile residues of ubiquitin utilizing the ( S f 2 , S H 2 , S N 2 ) and ( S f 2 , S 2 ,τ s ) representations (panels A and B, respectively), as averaged over the time interval between 30 ps and the assumed global tumbling time τ M .

    Journal: Journal of Chemical Theory and Computation

    Article Title: Molecular Dynamics-Assisted Optimization of Protein NMR Relaxation Analysis

    doi: 10.1021/acs.jctc.1c01165

    Figure Lengend Snippet: Standard deviations for the back-prediction of the six force field-derived internal autocorrelation functions at 600 MHz 1 H for the nine mobile residues of ubiquitin utilizing the ( S f 2 , S H 2 , S N 2 ) and ( S f 2 , S 2 ,τ s ) representations (panels A and B, respectively), as averaged over the time interval between 30 ps and the assumed global tumbling time τ M .

    Article Snippet: An E. coli -optimized codon sequence for ubiquitin (Genscript) was cloned into the expression vector pET11a and transformed into BL21-STAR (DE3) (Invitrogen).

    Techniques: Derivative Assay

    Standard deviations for the back-prediction of the six force field-derived internal autocorrelation functions at 600 MHz (panel A) and 900 MHz (panel B) for the nine mobile ubiquitin residues, utilizing the optimized time constant-constrained triexponential (TCCT) representation ( S f 2 , S h 2 , S x 2 ) as averaged over the time interval between 30 ps and the assumed global tumbling time τ M .

    Journal: Journal of Chemical Theory and Computation

    Article Title: Molecular Dynamics-Assisted Optimization of Protein NMR Relaxation Analysis

    doi: 10.1021/acs.jctc.1c01165

    Figure Lengend Snippet: Standard deviations for the back-prediction of the six force field-derived internal autocorrelation functions at 600 MHz (panel A) and 900 MHz (panel B) for the nine mobile ubiquitin residues, utilizing the optimized time constant-constrained triexponential (TCCT) representation ( S f 2 , S h 2 , S x 2 ) as averaged over the time interval between 30 ps and the assumed global tumbling time τ M .

    Article Snippet: An E. coli -optimized codon sequence for ubiquitin (Genscript) was cloned into the expression vector pET11a and transformed into BL21-STAR (DE3) (Invitrogen).

    Techniques: Derivative Assay

    Experimentally determined values of the internal bond vector autocorrelation functions of the ubiquitin backbone at 4.10 ns are displayed as rainbow coloring, with dark blue set to 1.0, green set to 0.69, and red set to 0.0. Residues lacking experimental measurements are set to dark blue.

    Journal: Journal of Chemical Theory and Computation

    Article Title: Molecular Dynamics-Assisted Optimization of Protein NMR Relaxation Analysis

    doi: 10.1021/acs.jctc.1c01165

    Figure Lengend Snippet: Experimentally determined values of the internal bond vector autocorrelation functions of the ubiquitin backbone at 4.10 ns are displayed as rainbow coloring, with dark blue set to 1.0, green set to 0.69, and red set to 0.0. Residues lacking experimental measurements are set to dark blue.

    Article Snippet: An E. coli -optimized codon sequence for ubiquitin (Genscript) was cloned into the expression vector pET11a and transformed into BL21-STAR (DE3) (Invitrogen).

    Techniques: Plasmid Preparation

    Experimentally determined internal bond vector autocorrelation functions for the C-terminal tail of a ubiquitin sample having an average τ M of 4.10 ns and an ellipsoidal asymmetry of 1.22 utilizing the optimized TCCT representation, with data from 600 MHz indicated in blue and the 900 MHz data indicated in red. The Monte Carlo-derived 95% confidence limits (dashes) were determined, assuming uncertainties of 1%, 1%, 0.01, and 1% for the R 1 , R 2 , NOE, and bond-specific τ M values, respectively.

    Journal: Journal of Chemical Theory and Computation

    Article Title: Molecular Dynamics-Assisted Optimization of Protein NMR Relaxation Analysis

    doi: 10.1021/acs.jctc.1c01165

    Figure Lengend Snippet: Experimentally determined internal bond vector autocorrelation functions for the C-terminal tail of a ubiquitin sample having an average τ M of 4.10 ns and an ellipsoidal asymmetry of 1.22 utilizing the optimized TCCT representation, with data from 600 MHz indicated in blue and the 900 MHz data indicated in red. The Monte Carlo-derived 95% confidence limits (dashes) were determined, assuming uncertainties of 1%, 1%, 0.01, and 1% for the R 1 , R 2 , NOE, and bond-specific τ M values, respectively.

    Article Snippet: An E. coli -optimized codon sequence for ubiquitin (Genscript) was cloned into the expression vector pET11a and transformed into BL21-STAR (DE3) (Invitrogen).

    Techniques: Plasmid Preparation, Derivative Assay