The Experts below are selected from a list of 168 Experts worldwide ranked by ideXlab platform
Christian Hoppmann - One of the best experts on this subject based on the ideXlab platform.
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light switchable hemithioindigo hemistilbene containing peptides ultrafast spectroscopy of the z e isomerization of the chromophore and the structural dynamics of the peptide moiety
Journal of Physical Chemistry B, 2012Co-Authors: Nadja Regner, Teja T Herzog, Karin Haiser, Christian Hoppmann, Michael Beyermann, Jorg Sauermann, Martin Engelhard, Thorben Cordes, K RuckbraunAbstract:Two hemithioindigo–hemistilbene (HTI) derivatives, designed to operate as structural switches in peptides, as well as two HTI peptides are characterized by ultrafast spectroscopy in the visible and the infrared. The two HTI switches follow the reaction scheme published for other HTI compounds with a picosecond excited state reaction (τ1 ≈ 6 ps) and isomerization from Z to E with τ2 = 13 and 51 ps. As compared to the isolated chromophores, the isomerization reaction is slowed down in the Chromopeptides to τ2 = 24 and 69 ps. For the smaller peptide containing 6 amino acids, the structural changes of the peptide moiety observed via the IR spectrum in the amide I band follow the isomerization of the molecular switch closely. In the larger cyclic Chromopeptide, containing 20 amino acids and mimicking a β-hairpin structure in the Z-form of the chromophore, the peptide moiety also changes its structure during isomerization of the chromophore. However, the IR spectrum at the end of the observation period of 3 ns ...
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Light-Switchable Hemithioindigo–Hemistilbene-Containing Peptides: Ultrafast Spectroscopy of the Z → E Isomerization of the Chromophore and the Structural Dynamics of the Peptide Moiety B
The Journal of Physical Chemistry, 2012Co-Authors: Nadja Regner, Teja T Herzog, Karin Haiser, Christian Hoppmann, Michael Beyermann, Jorg Sauermann, Martin Engelhard, Thorben Cordes, K. Rück-braun, Wolfgang ZinthAbstract:Two hemithioindigo–hemistilbene (HTI) derivatives, designed to operate as structural switches in peptides, as well as two HTI peptides are characterized by ultrafast spectroscopy in the visible and the infrared. The two HTI switches follow the reaction scheme published for other HTI compounds with a picosecond excited state reaction (τ₁ ≈ 6 ps) and isomerization from Z to E with τ₂ = 13 and 51 ps. As compared to the isolated chromophores, the isomerization reaction is slowed down in the Chromopeptides to τ₂ = 24 and 69 ps. For the smaller peptide containing 6 amino acids, the structural changes of the peptide moiety observed via the IR spectrum in the amide I band follow the isomerization of the molecular switch closely. In the larger cyclic Chromopeptide, containing 20 amino acids and mimicking a β-hairpin structure in the Z-form of the chromophore, the peptide moiety also changes its structure during isomerization of the chromophore. However, the IR spectrum at the end of the observation period of 3 ns deviates significantly from the stationary difference spectrum. These signatures indicate that strong additional structural changes, e.g., breaking of interchain hydrogen bonds, also occur on longer time scales.
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Light-Switchable Hemithioindigo–Hemistilbene-Containing Peptides: Ultrafast Spectroscopy of the Z → E Isomerization of the Chromophore and the Structural Dynamics of the Peptide Moiety
2012Co-Authors: Nadja Regner, Teja T Herzog, Karin Haiser, Christian Hoppmann, Michael Beyermann, Jorg Sauermann, Martin Engelhard, Thorben Cordes, K. Rück-braun, Wolfgang ZinthAbstract:Two hemithioindigo–hemistilbene (HTI) derivatives, designed to operate as structural switches in peptides, as well as two HTI peptides are characterized by ultrafast spectroscopy in the visible and the infrared. The two HTI switches follow the reaction scheme published for other HTI compounds with a picosecond excited state reaction (τ1 ≈ 6 ps) and isomerization from Z to E with τ2 = 13 and 51 ps. As compared to the isolated chromophores, the isomerization reaction is slowed down in the Chromopeptides to τ2 = 24 and 69 ps. For the smaller peptide containing 6 amino acids, the structural changes of the peptide moiety observed via the IR spectrum in the amide I band follow the isomerization of the molecular switch closely. In the larger cyclic Chromopeptide, containing 20 amino acids and mimicking a β-hairpin structure in the Z-form of the chromophore, the peptide moiety also changes its structure during isomerization of the chromophore. However, the IR spectrum at the end of the observation period of 3 ns deviates significantly from the stationary difference spectrum. These signatures indicate that strong additional structural changes, e.g., breaking of interchain hydrogen bonds, also occur on longer time scales
Nadja Regner - One of the best experts on this subject based on the ideXlab platform.
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light switchable hemithioindigo hemistilbene containing peptides ultrafast spectroscopy of the z e isomerization of the chromophore and the structural dynamics of the peptide moiety
Journal of Physical Chemistry B, 2012Co-Authors: Nadja Regner, Teja T Herzog, Karin Haiser, Christian Hoppmann, Michael Beyermann, Jorg Sauermann, Martin Engelhard, Thorben Cordes, K RuckbraunAbstract:Two hemithioindigo–hemistilbene (HTI) derivatives, designed to operate as structural switches in peptides, as well as two HTI peptides are characterized by ultrafast spectroscopy in the visible and the infrared. The two HTI switches follow the reaction scheme published for other HTI compounds with a picosecond excited state reaction (τ1 ≈ 6 ps) and isomerization from Z to E with τ2 = 13 and 51 ps. As compared to the isolated chromophores, the isomerization reaction is slowed down in the Chromopeptides to τ2 = 24 and 69 ps. For the smaller peptide containing 6 amino acids, the structural changes of the peptide moiety observed via the IR spectrum in the amide I band follow the isomerization of the molecular switch closely. In the larger cyclic Chromopeptide, containing 20 amino acids and mimicking a β-hairpin structure in the Z-form of the chromophore, the peptide moiety also changes its structure during isomerization of the chromophore. However, the IR spectrum at the end of the observation period of 3 ns ...
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Light-Switchable Hemithioindigo–Hemistilbene-Containing Peptides: Ultrafast Spectroscopy of the Z → E Isomerization of the Chromophore and the Structural Dynamics of the Peptide Moiety B
The Journal of Physical Chemistry, 2012Co-Authors: Nadja Regner, Teja T Herzog, Karin Haiser, Christian Hoppmann, Michael Beyermann, Jorg Sauermann, Martin Engelhard, Thorben Cordes, K. Rück-braun, Wolfgang ZinthAbstract:Two hemithioindigo–hemistilbene (HTI) derivatives, designed to operate as structural switches in peptides, as well as two HTI peptides are characterized by ultrafast spectroscopy in the visible and the infrared. The two HTI switches follow the reaction scheme published for other HTI compounds with a picosecond excited state reaction (τ₁ ≈ 6 ps) and isomerization from Z to E with τ₂ = 13 and 51 ps. As compared to the isolated chromophores, the isomerization reaction is slowed down in the Chromopeptides to τ₂ = 24 and 69 ps. For the smaller peptide containing 6 amino acids, the structural changes of the peptide moiety observed via the IR spectrum in the amide I band follow the isomerization of the molecular switch closely. In the larger cyclic Chromopeptide, containing 20 amino acids and mimicking a β-hairpin structure in the Z-form of the chromophore, the peptide moiety also changes its structure during isomerization of the chromophore. However, the IR spectrum at the end of the observation period of 3 ns deviates significantly from the stationary difference spectrum. These signatures indicate that strong additional structural changes, e.g., breaking of interchain hydrogen bonds, also occur on longer time scales.
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Light-Switchable Hemithioindigo–Hemistilbene-Containing Peptides: Ultrafast Spectroscopy of the Z → E Isomerization of the Chromophore and the Structural Dynamics of the Peptide Moiety
2012Co-Authors: Nadja Regner, Teja T Herzog, Karin Haiser, Christian Hoppmann, Michael Beyermann, Jorg Sauermann, Martin Engelhard, Thorben Cordes, K. Rück-braun, Wolfgang ZinthAbstract:Two hemithioindigo–hemistilbene (HTI) derivatives, designed to operate as structural switches in peptides, as well as two HTI peptides are characterized by ultrafast spectroscopy in the visible and the infrared. The two HTI switches follow the reaction scheme published for other HTI compounds with a picosecond excited state reaction (τ1 ≈ 6 ps) and isomerization from Z to E with τ2 = 13 and 51 ps. As compared to the isolated chromophores, the isomerization reaction is slowed down in the Chromopeptides to τ2 = 24 and 69 ps. For the smaller peptide containing 6 amino acids, the structural changes of the peptide moiety observed via the IR spectrum in the amide I band follow the isomerization of the molecular switch closely. In the larger cyclic Chromopeptide, containing 20 amino acids and mimicking a β-hairpin structure in the Z-form of the chromophore, the peptide moiety also changes its structure during isomerization of the chromophore. However, the IR spectrum at the end of the observation period of 3 ns deviates significantly from the stationary difference spectrum. These signatures indicate that strong additional structural changes, e.g., breaking of interchain hydrogen bonds, also occur on longer time scales
Wolfgang Zinth - One of the best experts on this subject based on the ideXlab platform.
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Light-Switchable Hemithioindigo–Hemistilbene-Containing Peptides: Ultrafast Spectroscopy of the Z → E Isomerization of the Chromophore and the Structural Dynamics of the Peptide Moiety B
The Journal of Physical Chemistry, 2012Co-Authors: Nadja Regner, Teja T Herzog, Karin Haiser, Christian Hoppmann, Michael Beyermann, Jorg Sauermann, Martin Engelhard, Thorben Cordes, K. Rück-braun, Wolfgang ZinthAbstract:Two hemithioindigo–hemistilbene (HTI) derivatives, designed to operate as structural switches in peptides, as well as two HTI peptides are characterized by ultrafast spectroscopy in the visible and the infrared. The two HTI switches follow the reaction scheme published for other HTI compounds with a picosecond excited state reaction (τ₁ ≈ 6 ps) and isomerization from Z to E with τ₂ = 13 and 51 ps. As compared to the isolated chromophores, the isomerization reaction is slowed down in the Chromopeptides to τ₂ = 24 and 69 ps. For the smaller peptide containing 6 amino acids, the structural changes of the peptide moiety observed via the IR spectrum in the amide I band follow the isomerization of the molecular switch closely. In the larger cyclic Chromopeptide, containing 20 amino acids and mimicking a β-hairpin structure in the Z-form of the chromophore, the peptide moiety also changes its structure during isomerization of the chromophore. However, the IR spectrum at the end of the observation period of 3 ns deviates significantly from the stationary difference spectrum. These signatures indicate that strong additional structural changes, e.g., breaking of interchain hydrogen bonds, also occur on longer time scales.
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Light-Switchable Hemithioindigo–Hemistilbene-Containing Peptides: Ultrafast Spectroscopy of the Z → E Isomerization of the Chromophore and the Structural Dynamics of the Peptide Moiety
2012Co-Authors: Nadja Regner, Teja T Herzog, Karin Haiser, Christian Hoppmann, Michael Beyermann, Jorg Sauermann, Martin Engelhard, Thorben Cordes, K. Rück-braun, Wolfgang ZinthAbstract:Two hemithioindigo–hemistilbene (HTI) derivatives, designed to operate as structural switches in peptides, as well as two HTI peptides are characterized by ultrafast spectroscopy in the visible and the infrared. The two HTI switches follow the reaction scheme published for other HTI compounds with a picosecond excited state reaction (τ1 ≈ 6 ps) and isomerization from Z to E with τ2 = 13 and 51 ps. As compared to the isolated chromophores, the isomerization reaction is slowed down in the Chromopeptides to τ2 = 24 and 69 ps. For the smaller peptide containing 6 amino acids, the structural changes of the peptide moiety observed via the IR spectrum in the amide I band follow the isomerization of the molecular switch closely. In the larger cyclic Chromopeptide, containing 20 amino acids and mimicking a β-hairpin structure in the Z-form of the chromophore, the peptide moiety also changes its structure during isomerization of the chromophore. However, the IR spectrum at the end of the observation period of 3 ns deviates significantly from the stationary difference spectrum. These signatures indicate that strong additional structural changes, e.g., breaking of interchain hydrogen bonds, also occur on longer time scales
Karin Haiser - One of the best experts on this subject based on the ideXlab platform.
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light switchable hemithioindigo hemistilbene containing peptides ultrafast spectroscopy of the z e isomerization of the chromophore and the structural dynamics of the peptide moiety
Journal of Physical Chemistry B, 2012Co-Authors: Nadja Regner, Teja T Herzog, Karin Haiser, Christian Hoppmann, Michael Beyermann, Jorg Sauermann, Martin Engelhard, Thorben Cordes, K RuckbraunAbstract:Two hemithioindigo–hemistilbene (HTI) derivatives, designed to operate as structural switches in peptides, as well as two HTI peptides are characterized by ultrafast spectroscopy in the visible and the infrared. The two HTI switches follow the reaction scheme published for other HTI compounds with a picosecond excited state reaction (τ1 ≈ 6 ps) and isomerization from Z to E with τ2 = 13 and 51 ps. As compared to the isolated chromophores, the isomerization reaction is slowed down in the Chromopeptides to τ2 = 24 and 69 ps. For the smaller peptide containing 6 amino acids, the structural changes of the peptide moiety observed via the IR spectrum in the amide I band follow the isomerization of the molecular switch closely. In the larger cyclic Chromopeptide, containing 20 amino acids and mimicking a β-hairpin structure in the Z-form of the chromophore, the peptide moiety also changes its structure during isomerization of the chromophore. However, the IR spectrum at the end of the observation period of 3 ns ...
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Light-Switchable Hemithioindigo–Hemistilbene-Containing Peptides: Ultrafast Spectroscopy of the Z → E Isomerization of the Chromophore and the Structural Dynamics of the Peptide Moiety B
The Journal of Physical Chemistry, 2012Co-Authors: Nadja Regner, Teja T Herzog, Karin Haiser, Christian Hoppmann, Michael Beyermann, Jorg Sauermann, Martin Engelhard, Thorben Cordes, K. Rück-braun, Wolfgang ZinthAbstract:Two hemithioindigo–hemistilbene (HTI) derivatives, designed to operate as structural switches in peptides, as well as two HTI peptides are characterized by ultrafast spectroscopy in the visible and the infrared. The two HTI switches follow the reaction scheme published for other HTI compounds with a picosecond excited state reaction (τ₁ ≈ 6 ps) and isomerization from Z to E with τ₂ = 13 and 51 ps. As compared to the isolated chromophores, the isomerization reaction is slowed down in the Chromopeptides to τ₂ = 24 and 69 ps. For the smaller peptide containing 6 amino acids, the structural changes of the peptide moiety observed via the IR spectrum in the amide I band follow the isomerization of the molecular switch closely. In the larger cyclic Chromopeptide, containing 20 amino acids and mimicking a β-hairpin structure in the Z-form of the chromophore, the peptide moiety also changes its structure during isomerization of the chromophore. However, the IR spectrum at the end of the observation period of 3 ns deviates significantly from the stationary difference spectrum. These signatures indicate that strong additional structural changes, e.g., breaking of interchain hydrogen bonds, also occur on longer time scales.
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Light-Switchable Hemithioindigo–Hemistilbene-Containing Peptides: Ultrafast Spectroscopy of the Z → E Isomerization of the Chromophore and the Structural Dynamics of the Peptide Moiety
2012Co-Authors: Nadja Regner, Teja T Herzog, Karin Haiser, Christian Hoppmann, Michael Beyermann, Jorg Sauermann, Martin Engelhard, Thorben Cordes, K. Rück-braun, Wolfgang ZinthAbstract:Two hemithioindigo–hemistilbene (HTI) derivatives, designed to operate as structural switches in peptides, as well as two HTI peptides are characterized by ultrafast spectroscopy in the visible and the infrared. The two HTI switches follow the reaction scheme published for other HTI compounds with a picosecond excited state reaction (τ1 ≈ 6 ps) and isomerization from Z to E with τ2 = 13 and 51 ps. As compared to the isolated chromophores, the isomerization reaction is slowed down in the Chromopeptides to τ2 = 24 and 69 ps. For the smaller peptide containing 6 amino acids, the structural changes of the peptide moiety observed via the IR spectrum in the amide I band follow the isomerization of the molecular switch closely. In the larger cyclic Chromopeptide, containing 20 amino acids and mimicking a β-hairpin structure in the Z-form of the chromophore, the peptide moiety also changes its structure during isomerization of the chromophore. However, the IR spectrum at the end of the observation period of 3 ns deviates significantly from the stationary difference spectrum. These signatures indicate that strong additional structural changes, e.g., breaking of interchain hydrogen bonds, also occur on longer time scales
Teja T Herzog - One of the best experts on this subject based on the ideXlab platform.
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light switchable hemithioindigo hemistilbene containing peptides ultrafast spectroscopy of the z e isomerization of the chromophore and the structural dynamics of the peptide moiety
Journal of Physical Chemistry B, 2012Co-Authors: Nadja Regner, Teja T Herzog, Karin Haiser, Christian Hoppmann, Michael Beyermann, Jorg Sauermann, Martin Engelhard, Thorben Cordes, K RuckbraunAbstract:Two hemithioindigo–hemistilbene (HTI) derivatives, designed to operate as structural switches in peptides, as well as two HTI peptides are characterized by ultrafast spectroscopy in the visible and the infrared. The two HTI switches follow the reaction scheme published for other HTI compounds with a picosecond excited state reaction (τ1 ≈ 6 ps) and isomerization from Z to E with τ2 = 13 and 51 ps. As compared to the isolated chromophores, the isomerization reaction is slowed down in the Chromopeptides to τ2 = 24 and 69 ps. For the smaller peptide containing 6 amino acids, the structural changes of the peptide moiety observed via the IR spectrum in the amide I band follow the isomerization of the molecular switch closely. In the larger cyclic Chromopeptide, containing 20 amino acids and mimicking a β-hairpin structure in the Z-form of the chromophore, the peptide moiety also changes its structure during isomerization of the chromophore. However, the IR spectrum at the end of the observation period of 3 ns ...
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Light-Switchable Hemithioindigo–Hemistilbene-Containing Peptides: Ultrafast Spectroscopy of the Z → E Isomerization of the Chromophore and the Structural Dynamics of the Peptide Moiety B
The Journal of Physical Chemistry, 2012Co-Authors: Nadja Regner, Teja T Herzog, Karin Haiser, Christian Hoppmann, Michael Beyermann, Jorg Sauermann, Martin Engelhard, Thorben Cordes, K. Rück-braun, Wolfgang ZinthAbstract:Two hemithioindigo–hemistilbene (HTI) derivatives, designed to operate as structural switches in peptides, as well as two HTI peptides are characterized by ultrafast spectroscopy in the visible and the infrared. The two HTI switches follow the reaction scheme published for other HTI compounds with a picosecond excited state reaction (τ₁ ≈ 6 ps) and isomerization from Z to E with τ₂ = 13 and 51 ps. As compared to the isolated chromophores, the isomerization reaction is slowed down in the Chromopeptides to τ₂ = 24 and 69 ps. For the smaller peptide containing 6 amino acids, the structural changes of the peptide moiety observed via the IR spectrum in the amide I band follow the isomerization of the molecular switch closely. In the larger cyclic Chromopeptide, containing 20 amino acids and mimicking a β-hairpin structure in the Z-form of the chromophore, the peptide moiety also changes its structure during isomerization of the chromophore. However, the IR spectrum at the end of the observation period of 3 ns deviates significantly from the stationary difference spectrum. These signatures indicate that strong additional structural changes, e.g., breaking of interchain hydrogen bonds, also occur on longer time scales.
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Light-Switchable Hemithioindigo–Hemistilbene-Containing Peptides: Ultrafast Spectroscopy of the Z → E Isomerization of the Chromophore and the Structural Dynamics of the Peptide Moiety
2012Co-Authors: Nadja Regner, Teja T Herzog, Karin Haiser, Christian Hoppmann, Michael Beyermann, Jorg Sauermann, Martin Engelhard, Thorben Cordes, K. Rück-braun, Wolfgang ZinthAbstract:Two hemithioindigo–hemistilbene (HTI) derivatives, designed to operate as structural switches in peptides, as well as two HTI peptides are characterized by ultrafast spectroscopy in the visible and the infrared. The two HTI switches follow the reaction scheme published for other HTI compounds with a picosecond excited state reaction (τ1 ≈ 6 ps) and isomerization from Z to E with τ2 = 13 and 51 ps. As compared to the isolated chromophores, the isomerization reaction is slowed down in the Chromopeptides to τ2 = 24 and 69 ps. For the smaller peptide containing 6 amino acids, the structural changes of the peptide moiety observed via the IR spectrum in the amide I band follow the isomerization of the molecular switch closely. In the larger cyclic Chromopeptide, containing 20 amino acids and mimicking a β-hairpin structure in the Z-form of the chromophore, the peptide moiety also changes its structure during isomerization of the chromophore. However, the IR spectrum at the end of the observation period of 3 ns deviates significantly from the stationary difference spectrum. These signatures indicate that strong additional structural changes, e.g., breaking of interchain hydrogen bonds, also occur on longer time scales