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Part of the book series: Springer Theses ((Springer Theses))

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Abstract

The disulfide bond seemingly represents a case where photochemistry efficiently competes with energy dissipation by internal conversion. It is well-recognized that upon the absorption of light a disulfide bond will cleave leaving two free radicals [1]. This process has been observed to occur on a sub ps timescale [2]. Despite this photolability, the disulfide bond formed by the oxidation of two cysteine amino acids is an important factor in determining the tertiary structure of proteins along with hydrogen bonding and hydrophobic interactions [3]. For the disulfide bond to prevail, the radicals formed by the bond cleavage must be confined such as to allow for recombination and thereby reformation of the disulfide bond. In solution, the solvent shell surrounding radicals formed by the photocleavage of a disulfide bond has been argued to provide such confinement, but a quantum yield of 30

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Notes

  1. 1.

    The author did not take part in conducting the experiments.

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Correspondence to Thomas Scheby Kuhlman .

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Kuhlman, T.S. (2013). Dithiane. In: The Non-Ergodic Nature of Internal Conversion. Springer Theses. Springer, Heidelberg. https://doi.org/10.1007/978-3-319-00386-3_9

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