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Utilizing single-molecule fluorescence resonance energy transfer (FRET) spectroscopy, the research investigates protein folding within a significant family of repeat proteins. The study reveals that the dynamics of expanded conformations exhibit rapid, spring-like motion, enhancing understanding of the structural elasticity crucial for binding various partners. This concise thesis offers valuable insights for PhD students and researchers entering the field, highlighting the functional implications of repeat protein behavior.
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Single-Molecule Fluorescence Spectroscopy of the Folding of a Repeat Protein, Sharona Cohen
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- Pubblicato
- 2016
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