Review



th-(1-43  (Accelrys)

 
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 90
      Buy from Supplier

    Structured Review

    Accelrys th-(1-43
    B factors (Panel A) were calculated from the aqueous simulations for <t>TH-(1-43)</t> (black line) and THp-(1-43) (red line) and from the peptide/membrane simulations for TH-(1-43) (blue line) and THp-(1-43) (green line), and are represented as a function of residue number. Panel B: Representative structure of THp-(1-43) which shows the intrapeptide sidechain-sidechain hydrogen bonds with occupancies >25% (dashed lines) in the aqueous simulation. The peptide is coloured as a continuous gradient going from blue (N-terminal) to red (C-terminal). The last 100 ns of each simulation were used for both analyses.
    Th (1 43, supplied by Accelrys, 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/th-(1-43/th++1+43/pmc03872242-162-10-24
    Average 90 stars, based on 1 article reviews
    th-(1-43 - by Bioz Stars, 2026-09
    90/100 stars

    Images

    1) Product Images from "The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes"

    Article Title: The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes

    Journal: Journal of molecular biology

    doi: 10.1016/j.jmb.2013.09.012

    B factors (Panel A) were calculated from the aqueous simulations for TH-(1-43) (black line) and THp-(1-43) (red line) and from the peptide/membrane simulations for TH-(1-43) (blue line) and THp-(1-43) (green line), and are represented as a function of residue number. Panel B: Representative structure of THp-(1-43) which shows the intrapeptide sidechain-sidechain hydrogen bonds with occupancies >25% (dashed lines) in the aqueous simulation. The peptide is coloured as a continuous gradient going from blue (N-terminal) to red (C-terminal). The last 100 ns of each simulation were used for both analyses.
    Figure Legend Snippet: B factors (Panel A) were calculated from the aqueous simulations for TH-(1-43) (black line) and THp-(1-43) (red line) and from the peptide/membrane simulations for TH-(1-43) (blue line) and THp-(1-43) (green line), and are represented as a function of residue number. Panel B: Representative structure of THp-(1-43) which shows the intrapeptide sidechain-sidechain hydrogen bonds with occupancies >25% (dashed lines) in the aqueous simulation. The peptide is coloured as a continuous gradient going from blue (N-terminal) to red (C-terminal). The last 100 ns of each simulation were used for both analyses.

    Techniques Used:

    A) Representative sensorgrams for the interaction of TH-(1-43) with POPS liposomes on a L1 sensor chip at increasing concentrations of peptide. B) Peptide concentration dependency of TH-(1-43) (black) and THp-(1-43) (red) when bound to POPS liposomes. RUs were measured as a function of peptide concentration. S0.5 values were extracted from the hyperbolic, single-rectangular, two-parameter curve fitting and resulted in S0.5 of 53.3 ± 9.2 µM and 48.2 ± 7.4 µM for TH-(1-43) and THp-(1-43), respectively. C) Far-UV CD spectra of 40 µM TH-(1-43) (black lines) or THp-(1-43) (red lines) without (solid lines) or with (dotted lines) POPS liposomes (0.6 mM phospholipid). Samples were prepared in 10 mM Na-Hepes, 150 mM NaCl, pH 7.4, and spectra were recorded at 25 °C.
    Figure Legend Snippet: A) Representative sensorgrams for the interaction of TH-(1-43) with POPS liposomes on a L1 sensor chip at increasing concentrations of peptide. B) Peptide concentration dependency of TH-(1-43) (black) and THp-(1-43) (red) when bound to POPS liposomes. RUs were measured as a function of peptide concentration. S0.5 values were extracted from the hyperbolic, single-rectangular, two-parameter curve fitting and resulted in S0.5 of 53.3 ± 9.2 µM and 48.2 ± 7.4 µM for TH-(1-43) and THp-(1-43), respectively. C) Far-UV CD spectra of 40 µM TH-(1-43) (black lines) or THp-(1-43) (red lines) without (solid lines) or with (dotted lines) POPS liposomes (0.6 mM phospholipid). Samples were prepared in 10 mM Na-Hepes, 150 mM NaCl, pH 7.4, and spectra were recorded at 25 °C.

    Techniques Used: Concentration Assay

    TH-(1-43)/POPS is presented in panels A and B, and THp-(1-43)/POPS is presented in panels C and D. Panels A and C show the peptide – coloured as a continuous gradient going from blue (N-terminal) to red (C-terminal) – together with most of the peptideinteracting leaflet of the POPS bilayer, the orange spheres representing the head group phosphorus atoms. Panels B and D provide close-ups of the most important hydrogen bond interactions (dashed lines) in each case, where the relevant TH residues are displayed as ball-and-stick models and the POPS lipids as sticks. Water and ions have been removed for clarity.
    Figure Legend Snippet: TH-(1-43)/POPS is presented in panels A and B, and THp-(1-43)/POPS is presented in panels C and D. Panels A and C show the peptide – coloured as a continuous gradient going from blue (N-terminal) to red (C-terminal) – together with most of the peptideinteracting leaflet of the POPS bilayer, the orange spheres representing the head group phosphorus atoms. Panels B and D provide close-ups of the most important hydrogen bond interactions (dashed lines) in each case, where the relevant TH residues are displayed as ball-and-stick models and the POPS lipids as sticks. Water and ions have been removed for clarity.

    Techniques Used:

    The energies are computed using 1000 frames extracted from the last 100 ns of each peptide/membrane simulation (systems D and E in Table 1). ΔGdecomp = ΔG’ – ΔGnon-polar. The black bars represent the energies derived for each residue in TH-(1-43), and the grey bars are the THp-(1-43) equivalents. A) Sorted by amino acid sequence; B) Sorted in ascending order according to the TH-(1-43) decomposition energies.
    Figure Legend Snippet: The energies are computed using 1000 frames extracted from the last 100 ns of each peptide/membrane simulation (systems D and E in Table 1). ΔGdecomp = ΔG’ – ΔGnon-polar. The black bars represent the energies derived for each residue in TH-(1-43), and the grey bars are the THp-(1-43) equivalents. A) Sorted by amino acid sequence; B) Sorted in ascending order according to the TH-(1-43) decomposition energies.

    Techniques Used: Derivative Assay, Sequencing



    Similar Products

    th-(1-43  (Accelrys)
    90
    Accelrys th-(1-43
    B factors (Panel A) were calculated from the aqueous simulations for <t>TH-(1-43)</t> (black line) and THp-(1-43) (red line) and from the peptide/membrane simulations for TH-(1-43) (blue line) and THp-(1-43) (green line), and are represented as a function of residue number. Panel B: Representative structure of THp-(1-43) which shows the intrapeptide sidechain-sidechain hydrogen bonds with occupancies >25% (dashed lines) in the aqueous simulation. The peptide is coloured as a continuous gradient going from blue (N-terminal) to red (C-terminal). The last 100 ns of each simulation were used for both analyses.
    Th (1 43, supplied by Accelrys, 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/th-(1-43/th++1+43/pmc03872242-162-10-24
    Average 90 stars, based on 1 article reviews
    th-(1-43 - by Bioz Stars, 2026-09
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    B factors (Panel A) were calculated from the aqueous simulations for TH-(1-43) (black line) and THp-(1-43) (red line) and from the peptide/membrane simulations for TH-(1-43) (blue line) and THp-(1-43) (green line), and are represented as a function of residue number. Panel B: Representative structure of THp-(1-43) which shows the intrapeptide sidechain-sidechain hydrogen bonds with occupancies >25% (dashed lines) in the aqueous simulation. The peptide is coloured as a continuous gradient going from blue (N-terminal) to red (C-terminal). The last 100 ns of each simulation were used for both analyses.

    Journal: Journal of molecular biology

    Article Title: The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes

    doi: 10.1016/j.jmb.2013.09.012

    Figure Lengend Snippet: B factors (Panel A) were calculated from the aqueous simulations for TH-(1-43) (black line) and THp-(1-43) (red line) and from the peptide/membrane simulations for TH-(1-43) (blue line) and THp-(1-43) (green line), and are represented as a function of residue number. Panel B: Representative structure of THp-(1-43) which shows the intrapeptide sidechain-sidechain hydrogen bonds with occupancies >25% (dashed lines) in the aqueous simulation. The peptide is coloured as a continuous gradient going from blue (N-terminal) to red (C-terminal). The last 100 ns of each simulation were used for both analyses.

    Article Snippet: TH peptides in water and with the POPS membrane The peptides TH-(1-43) and THp-(1-43) were built as random coils with the protein builder in Accelrys Discovery Studio 36 and simulated for 100 ns in explicit octahedral-shaped water boxes.

    Techniques:

    A) Representative sensorgrams for the interaction of TH-(1-43) with POPS liposomes on a L1 sensor chip at increasing concentrations of peptide. B) Peptide concentration dependency of TH-(1-43) (black) and THp-(1-43) (red) when bound to POPS liposomes. RUs were measured as a function of peptide concentration. S0.5 values were extracted from the hyperbolic, single-rectangular, two-parameter curve fitting and resulted in S0.5 of 53.3 ± 9.2 µM and 48.2 ± 7.4 µM for TH-(1-43) and THp-(1-43), respectively. C) Far-UV CD spectra of 40 µM TH-(1-43) (black lines) or THp-(1-43) (red lines) without (solid lines) or with (dotted lines) POPS liposomes (0.6 mM phospholipid). Samples were prepared in 10 mM Na-Hepes, 150 mM NaCl, pH 7.4, and spectra were recorded at 25 °C.

    Journal: Journal of molecular biology

    Article Title: The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes

    doi: 10.1016/j.jmb.2013.09.012

    Figure Lengend Snippet: A) Representative sensorgrams for the interaction of TH-(1-43) with POPS liposomes on a L1 sensor chip at increasing concentrations of peptide. B) Peptide concentration dependency of TH-(1-43) (black) and THp-(1-43) (red) when bound to POPS liposomes. RUs were measured as a function of peptide concentration. S0.5 values were extracted from the hyperbolic, single-rectangular, two-parameter curve fitting and resulted in S0.5 of 53.3 ± 9.2 µM and 48.2 ± 7.4 µM for TH-(1-43) and THp-(1-43), respectively. C) Far-UV CD spectra of 40 µM TH-(1-43) (black lines) or THp-(1-43) (red lines) without (solid lines) or with (dotted lines) POPS liposomes (0.6 mM phospholipid). Samples were prepared in 10 mM Na-Hepes, 150 mM NaCl, pH 7.4, and spectra were recorded at 25 °C.

    Article Snippet: TH peptides in water and with the POPS membrane The peptides TH-(1-43) and THp-(1-43) were built as random coils with the protein builder in Accelrys Discovery Studio 36 and simulated for 100 ns in explicit octahedral-shaped water boxes.

    Techniques: Concentration Assay

    TH-(1-43)/POPS is presented in panels A and B, and THp-(1-43)/POPS is presented in panels C and D. Panels A and C show the peptide – coloured as a continuous gradient going from blue (N-terminal) to red (C-terminal) – together with most of the peptideinteracting leaflet of the POPS bilayer, the orange spheres representing the head group phosphorus atoms. Panels B and D provide close-ups of the most important hydrogen bond interactions (dashed lines) in each case, where the relevant TH residues are displayed as ball-and-stick models and the POPS lipids as sticks. Water and ions have been removed for clarity.

    Journal: Journal of molecular biology

    Article Title: The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes

    doi: 10.1016/j.jmb.2013.09.012

    Figure Lengend Snippet: TH-(1-43)/POPS is presented in panels A and B, and THp-(1-43)/POPS is presented in panels C and D. Panels A and C show the peptide – coloured as a continuous gradient going from blue (N-terminal) to red (C-terminal) – together with most of the peptideinteracting leaflet of the POPS bilayer, the orange spheres representing the head group phosphorus atoms. Panels B and D provide close-ups of the most important hydrogen bond interactions (dashed lines) in each case, where the relevant TH residues are displayed as ball-and-stick models and the POPS lipids as sticks. Water and ions have been removed for clarity.

    Article Snippet: TH peptides in water and with the POPS membrane The peptides TH-(1-43) and THp-(1-43) were built as random coils with the protein builder in Accelrys Discovery Studio 36 and simulated for 100 ns in explicit octahedral-shaped water boxes.

    Techniques:

    The energies are computed using 1000 frames extracted from the last 100 ns of each peptide/membrane simulation (systems D and E in Table 1). ΔGdecomp = ΔG’ – ΔGnon-polar. The black bars represent the energies derived for each residue in TH-(1-43), and the grey bars are the THp-(1-43) equivalents. A) Sorted by amino acid sequence; B) Sorted in ascending order according to the TH-(1-43) decomposition energies.

    Journal: Journal of molecular biology

    Article Title: The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes

    doi: 10.1016/j.jmb.2013.09.012

    Figure Lengend Snippet: The energies are computed using 1000 frames extracted from the last 100 ns of each peptide/membrane simulation (systems D and E in Table 1). ΔGdecomp = ΔG’ – ΔGnon-polar. The black bars represent the energies derived for each residue in TH-(1-43), and the grey bars are the THp-(1-43) equivalents. A) Sorted by amino acid sequence; B) Sorted in ascending order according to the TH-(1-43) decomposition energies.

    Article Snippet: TH peptides in water and with the POPS membrane The peptides TH-(1-43) and THp-(1-43) were built as random coils with the protein builder in Accelrys Discovery Studio 36 and simulated for 100 ns in explicit octahedral-shaped water boxes.

    Techniques: Derivative Assay, Sequencing