Overview
- Nominated as an Outstanding Ph.D. thesis by Weizmann Institute of Science, Rehovot, Israel
- First optical characterization of elasticity of a repeat protein
- Comprehensive single-molecule FRET experiments probe both dynamics and structure during equilibrium folding
- Includes supplementary material: sn.pub/extras
Part of the book series: Springer Theses (Springer Theses)
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Table of contents (5 chapters)
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Front Matter
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Back Matter
Keywords
About this book
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.
Authors and Affiliations
About the author
Bibliographic Information
Book Title: Single-Molecule Fluorescence Spectroscopy of the Folding of a Repeat Protein
Authors: Sharona Cohen
Series Title: Springer Theses
DOI: https://doi.org/10.1007/978-3-319-09558-5
Publisher: Springer Cham
eBook Packages: Chemistry and Materials Science, Chemistry and Material Science (R0)
Copyright Information: Springer International Publishing Switzerland 2016
Hardcover ISBN: 978-3-319-09557-8Published: 02 November 2015
Softcover ISBN: 978-3-319-37236-5Published: 23 August 2016
eBook ISBN: 978-3-319-09558-5Published: 17 October 2015
Series ISSN: 2190-5053
Series E-ISSN: 2190-5061
Edition Number: 1
Number of Pages: XIII, 59
Topics: Bioorganic Chemistry, Spectroscopy/Spectrometry, Biological and Medical Physics, Biophysics