| Autor: |
Robkis, D. Miklos, Hoang, Eileen M., Po, Pengse, Deutsch, Carol J., Petersson, E. James |
| Zdroj: |
Biopolymers; Jan2021, Vol. 112 Issue 1, p1-11, 11p |
| Abstrakt: |
Thioamides, single atom oxygen‐to‐sulfur substitutions of canonical amide bonds, can be valuable probes for protein folding and protease studies. Here, we investigate the fluorescence quenching properties of thioamides incorporated into the side‐chains of amino acids. We synthesize and incorporate Fmoc‐protected, solid‐phase peptide synthesis building blocks for introducing Nε‐thioacetyl‐lysine and γ‐thioasparagine. Using rigid model peptides, we demonstrate the distance‐dependent fluorescence quenching of these thioamides. Furthermore, we describe attempts to incorporate of Nε‐thioacetyl‐lysine into proteins expressed in Escherichia coli using amber codon suppression. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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