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Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How “Molecular Surgery” of the Backbone Affects Folding and Stability
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Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How “Molecular Surgery” of the Backbone Affects Folding and Stability
Bölümler
- 00:04Introduction
- 01:39Production of Recombinant Wild-Type Fluorescent Proteins and Selective Pressure Incorporation to Produce Fluorescent Proteins with Proline Analogs
- 04:08Fluorescence Emission of Protein Variants
- 05:00Denaturation and Refolding of EGFP Variants
- 06:38Results: Effect of Atomic Substitutions in Variants of GFP
- 09:17Conclusion
To overcome the limitations of classical site-directed mutagenesis, proline analogs with specific modifications were incorporated into several fluorescent proteins. We show how the replacement of hydrogen by fluorine or of the single by double bonds in proline residues ("molecular surgery") affects fundamental protein properties, including their folding and interaction with light.
