Single Molecule Fluorescence Spectroscopy of the Folding of a Repeat Protein: 2016

Series: Springer Theses

Sold by Ingram

This product may not be approved for your region.
Hardback
  • Free Shipping

    On orders of AED 100 or more. Standard delivery within 5-15 days.
  • Free Reserve & Collect

    Reserve & Collect from Magrudy's or partner stores accross the UAE.
  • Cash On Delivery

    Pay when your order arrives.
  • Free returns

    See more about our return policy.
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.