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.

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.

Zusammenfassung

Inthis thesis single-molecule fluorescence resonance energy transfer(FRET)spectroscopy was used to study the folding of a protein that belongsto the large and important family of repeat proteins. Cohen showsthat the dynamics of the expanded conformations is likely to be veryfast, suggesting a spring-like motion of the whole chain. Thefindings shed new lighton the elasticity of structure in repeat proteins, which is relatedto their function in binding multiple and disparate partners. Thisconcise research summary provides useful insights for studentsbeginning a PhD in this or a related area, and researchers enteringthis field.

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