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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.
List of contents
Abstract.- Introduction.- Methods.- Results.- Discussion.- Summary and Future Plans.
About the author
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.
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.
