Intrinsic Reactivities of Amino Acids towards Photoalkylation with Benzophenone − A Study Preliminary to Photolabelling of the Transmembrane Protein Glycophorin A
✍ Scribed by Eckart Deseke; Yoichi Nakatani; Guy Ourisson
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 505 KB
- Volume
- 1998
- Category
- Article
- ISSN
- 1434-193X
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✦ Synopsis
A systematic study of the photoalkylation of amino acids by α-coupling products. Methionine was shown to be favoured both in the sense of reactivity as well as product stability. benzophenone, a standard photosensitive probe of biomolecules, was performed addressing for the first time chemo-, Preliminary to a project directed towards the elucidation of the topography of glycophorin A in membranes, the present regio-, and stereoselectivities. The high reactivity of the capto-dative substituted α-carbon, particularly in glycine, model experiments focussed on the ten amino acids that constitute the transmembrane part of this protein. could be demonstrated as well as the chemical lability of the