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荧光蛋白中脯氨酸类似物对脯氨酸的残基特异换：骨架的“分子手术”如何影响折叠和稳定性
JoVE Journal
Bioengenharia
This content is Free Access.
JoVE Journal Bioengenharia
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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荧光蛋白中脯氨酸类似物对脯氨酸的残基特异换：骨架的“分子手术”如何影响折叠和稳定性

DOI:
10.3791/63320-v

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10:31 min

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February 03, 2022

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

Capítulos

  • 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

Summary

Tadução automática

Tadução automática

为了克服经典定点诱变的局限性，将具有特定修饰的脯氨酸类似物掺入几种荧光蛋白中。我们展示了氟替代氢或脯氨酸残基中的单双键（“分子手术”）如何影响基本的蛋白质特性，包括它们的折叠和与光的相互作用。

Tags

Keywords: Proline AnalogNon-canonical Amino AcidProtein FoldingProtein StabilityMolecular SurgeryFluorescent ProteinSite-directed MutagenesisRibosomal Protein TranslationProtein EngineeringE. Coli CultureNMM MediumOptical DensityCell SuspensionCentrifugationAmino Acid DepletionAmpicillin

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