Single-molecule fluorescence spectroscopy of the folding of a repeat protein /

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Bibliographic Details
Author / Creator:Cohen, Sharona, author.
Imprint:Cham : Springer, [2015]
©2016
Description:1 online resource
Language:English
Series:Springer theses
Springer theses.
Subject:
Format: E-Resource Book
URL for this record:http://pi.lib.uchicago.edu/1001/cat/bib/11249053
Hidden Bibliographic Details
ISBN:9783319095585
3319095587
9783319095578
3319095579
Notes:"Doctoral thesis accepted by Weizmann Institute of Science, Rehovot, Israel."
Includes bibliographical references.
Online resource, title from PDF title page (Ebsco, viewed on October 29, 2015).
Summary: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.
Other form:Print version: Cohen, Sharona. Single-molecule fluorescence spectroscopy of the folding of a repeat protein. Cham : Springer, [2015] 3319095579 9783319095578
Standard no.:10.1007/978-3-319-09558-5
Table of Contents:
  • Abstract
  • Introduction
  • Methods
  • Results
  • Discussion
  • Summary and Future Plans.