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Single-Molecule Fluorescence Spectroscopy of the Folding of a Repeat Protein

  • Sharona Cohen

Part of the Springer Theses book series (Springer Theses)

Table of contents

  1. Front Matter
    Pages i-xiii
  2. Sharona Cohen
    Pages 1-11
  3. Sharona Cohen
    Pages 13-22
  4. Sharona Cohen
    Pages 23-50
  5. Sharona Cohen
    Pages 51-56
  6. Sharona Cohen
    Pages 57-58
  7. Back Matter
    Pages 59-59

About this book

Introduction

In this thesis single-molecule fluorescence resonance energy transfer (FRET) spectroscopy was used to study the folding of a protein that belongs to the large and important family of repeat proteins. Cohen shows that the dynamics of the expanded conformations is likely to be very fast, suggesting a spring-like motion of the whole chain. The findings shed new light on the elasticity of structure in repeat proteins, which is related to their function in binding multiple and disparate partners. This concise research summary provides useful insights for students beginning a PhD in this or a related area, and researchers entering this field.


Keywords

CTPR with Three Repeats (CTPR3) Consensus TPR (CTPR) Fluorescent Correlation Spectroscopy (FCS) Förster Resonance Energy Transfer (FRET) Repeat Proteins Single Molecule FRET (SM-FRET) Tetratrico Peptide Repeat (TPR)

Authors and affiliations

  • Sharona Cohen
    • 1
  1. 1.Chemical Physics DepartmentWeizmann Institute of ScienceRehovotIsrael

Bibliographic information

  • DOI https://doi.org/10.1007/978-3-319-09558-5
  • Copyright Information Springer International Publishing Switzerland 2016
  • Publisher Name Springer, Cham
  • eBook Packages Chemistry and Materials Science
  • Print ISBN 978-3-319-09557-8
  • Online ISBN 978-3-319-09558-5
  • Series Print ISSN 2190-5053
  • Series Online ISSN 2190-5061
  • Buy this book on publisher's site
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