Picosecond dynamics in water-soluble azobenzene-peptides

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Title: Picosecond dynamics in water-soluble azobenzene-peptides
Authors: Satzger, H.1, Root, C.1, Renner, C.2, Behrendt, R.2, Moroder, L.2, Wachtveitl, J.3, Zinth, W. wolfgang.zinth@physik.uni-muenchen.de
Source: Chemical Physics Letters. Sep2004, Vol. 396 Issue 1-3, p191-197. 7p.
Subjects: Absorption, Peptides, Heat, Mechanics (Physics)
Abstract: Ultrafast absorption changes are recorded for water-soluble cyclic azobenzene peptides containing the photoswitch (4-aminomethyl)-phenyl-azobenzoic acid (AMPB) and a bioactive peptide motif. They can be separated into the fast reactions in the AMPB chromophore and the slower response of the peptide moiety. While the fastest reactions display similar time constants as observed for AMPB peptides dissolved in DMSO the slower reaction dynamics assigned to vibrational cooling and motions of the peptide moiety are faster in water by a factor of up to two. The changes in the reaction times are explained by solvent heat capacity and viscosity. [Copyright &y& Elsevier]
Copyright of Chemical Physics Letters is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Picosecond dynamics in water-soluble azobenzene-peptides
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  Data: <searchLink fieldCode="JN" term="%22Chemical+Physics+Letters%22">Chemical Physics Letters</searchLink>. Sep2004, Vol. 396 Issue 1-3, p191-197. 7p.
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  Data: Ultrafast absorption changes are recorded for water-soluble cyclic azobenzene peptides containing the photoswitch (4-aminomethyl)-phenyl-azobenzoic acid (AMPB) and a bioactive peptide motif. They can be separated into the fast reactions in the AMPB chromophore and the slower response of the peptide moiety. While the fastest reactions display similar time constants as observed for AMPB peptides dissolved in DMSO the slower reaction dynamics assigned to vibrational cooling and motions of the peptide moiety are faster in water by a factor of up to two. The changes in the reaction times are explained by solvent heat capacity and viscosity. [Copyright &y& Elsevier]
– Name: AbstractSuppliedCopyright
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  Data: <i>Copyright of Chemical Physics Letters is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1016/j.cplett.2004.08.024
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        Text: English
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              Text: Sep2004
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