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

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.

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

Autorentext
Sharona Cohen is a trained physicist, specialized in optical systems, microscopy and spectroscopy. She acquired her PhD at the interdisciplinary chemical physics department at Weizmann Institute of Science.

Inhalt
Abstract.- Introduction.- Methods.- Results.- Discussion.- Summary and Future Plans.