Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

2.8K Views

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10:31 min

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February 3rd, 2022

DOI :

10.3791/63320-v

February 3rd, 2022

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Tuyet Mai Thi To¹, Vladimir Kubyshkin², Franz-Josef Schmitt³, Nediljko Budisa¹^,², Thomas Friedrich¹

¹Institute of Chemistry, Technische Universität Berlin, ²Department of Chemistry, University of Manitoba, ³Institute of Physics, Martin-Luther-Universität Halle-Wittenberg

Summary

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Proline Analogs

Molecular Surgery

Site directed Mutagenesis

Protein Folding

Stability

Ribosomally synthesized Proteins

Non canonical Amino Acids

Protein Properties

Biotechnological Engineering

Chapters in this video

0:04

Introduction

1:39

Production of Recombinant Wild-Type Fluorescent Proteins and Selective Pressure Incorporation to Produce Fluorescent Proteins with Proline Analogs

4:08

Fluorescence Emission of Protein Variants

5:00

Denaturation and Refolding of EGFP Variants

6:38

Results: Effect of Atomic Substitutions in Variants of GFP

9:17

Conclusion

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