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

• Κύριος συγγραφέας: Cohen, Sharona (Συγγραφέας)
• Συγγραφή απο Οργανισμό/Αρχή: SpringerLink (Online service)
• Μορφή: Ηλεκτρονική πηγή Ηλ. βιβλίο
• Γλώσσα: English
• Έκδοση: Cham : Springer International Publishing : Imprint: Springer, 2016.
• Έκδοση: 1st ed. 2016.
• Σειρά: Springer Theses, Recognizing Outstanding Ph.D. Research,
• Θέματα: Chemistry.; Spectroscopy.; Bioorganic chemistry.; Biophysics.; Biological physics.; Bioorganic Chemistry.; Spectroscopy/Spectrometry.; Biophysics and Biological Physics.
• Φυσική περιγραφή: XIII, 59 p. 28 illus. in color. online resource.
• ISBN: 9783319095585
• ISSN: 2190-5053

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.