AI Article Synopsis
- Thioamides can replace parts of peptide backbones, altering hydrogen bonding and protein behavior, and can also aid in studying energy and electron transfer.
- This paper discusses the semi-synthesis of the B1 domain of protein G (GB1) using thioamide modifications at either end of the protein.
- The thioamide is added to a peptide fragment through solid-phase synthesis and then combined with a recombinantly expressed protein fragment using a method called native chemical ligation, with provided protocols and examples for research in structural biology and protein misfolding.
Article Abstract
The thioamide is a versatile replacement of the peptide backbone with altered hydrogen bonding and conformational preferences, as well the ability participate in energy and electron transfer processes. Semi-synthetic incorporation of a thioamide into a protein can be used to study protein folding or protein/protein interactions using these properties. Semi-synthesis also provides the opportunity to study the role of thioamides in natural proteins. Here we outline the semi-synthesis of a model protein, the B1 domain of protein G (GB1) with a thioamide at the N-terminus or the C-terminus. The thioamide is synthetically incorporated into a fragment by solid-phase peptide synthesis, whereas the remainder of the protein is recombinantly expressed. Then, the two fragments are joined by native chemical ligation. The explicit protocol for GB1 synthesis is accompanied by examples of applications with GB1 and other proteins in structural biology and protein misfolding studies.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8617429 | PMC |
| http://dx.doi.org/10.1016/bs.mie.2021.04.011 | DOI Listing |
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