ReviewMolecules (Basel, Switzerland)2013
Semi-synthesis of labeled proteins for spectroscopic applications.
Review in Molecules (Basel, Switzerland), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed.
- Exploiting Protein N-Terminus for Site-Specific Bioconjugation.Molecules (Basel, Switzerland) · 2021Review
- Characterizing Aciniform Silk Repetitive Domain Backbone Dynamics and Hydrodynamic Modularity.International journal of molecular sciences · 2016Article
- Beyond new chemical entities: advancing drug development based on functional versatility of antibodies.Human vaccines & immunotherapeutics · 2014Article
- Optical control and study of biological processes at the single-cell level in a live organism.Reports on progress in physics. Physical Society (Great Britain) · 2013Review
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Since the introduction of SPPS by Merrifield in the 60s, peptide chemists have considered the possibility of preparing large proteins. The introduction of native chemical ligation in the 90s and then of expressed protein ligation have opened the way to the preparation of synthetic proteins without size limitations. This review focuses on semi-synthetic strategies useful to prepare proteins decorated with spectroscopic probes, like fluorescent labels and stable isotopes, and their biophysical applications. We show that expressed protein ligation, combining the advantages of organic chemistry with the easy and size limitless recombinant protein expression, is an excellent strategy for the chemical synthesis of labeled proteins, enabling a single protein to be functionalized at one or even more distinct positions with different probes.
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