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Rezensionsexemplar
Alexander Mehlich
Transition paths of protein-folding probed with optical tweezers
Establishing transition path analysis techniques in single-molecule force spectroscopy based on simulation and experiments performed on natural and artificial proteins
Protein-folding is one of the greatest challenges in science today. From a physicist‘s perspective, nature solves this ‚protein-folding problem‘ by providing a multidimensional energy landscape which efficiently guides a loose peptide towards a distinct 3D structure which is solely predefined by its unique amino acid sequence.
A powerful method to directly study the folding mechanism of proteins is single-molecule force spectroscopy. With a variety of sophisticated analysis tools it is possible to derive transition state positions and barrier heights, up to entire one-dimensional projections of the folding energy landscapes of proteins, from single-molecule trajectories. Recent technological advances to improve temporal and spatial resolution opened doors to directly accessing protein-folding transition paths.
This book addresses three key questions associated with the ‚physics of protein-folding‘:
1. What does energy landscape roughness mean?
2. How and what can we learn from studying transition paths?
3. Are natural and artificial proteins mechanically different?
In addition to new findings, this work includes a comprehensive overview of state-of-the-art analysis methods for single-molecule force spectroscopy data. Notably, the provided level of detail empowers the reader to reproduce all crucial lines of thought.
A powerful method to directly study the folding mechanism of proteins is single-molecule force spectroscopy. With a variety of sophisticated analysis tools it is possible to derive transition state positions and barrier heights, up to entire one-dimensional projections of the folding energy landscapes of proteins, from single-molecule trajectories. Recent technological advances to improve temporal and spatial resolution opened doors to directly accessing protein-folding transition paths.
This book addresses three key questions associated with the ‚physics of protein-folding‘:
1. What does energy landscape roughness mean?
2. How and what can we learn from studying transition paths?
3. Are natural and artificial proteins mechanically different?
In addition to new findings, this work includes a comprehensive overview of state-of-the-art analysis methods for single-molecule force spectroscopy data. Notably, the provided level of detail empowers the reader to reproduce all crucial lines of thought.
Schlagwörter: transition paths; protein folding; single molecule mechanics; force spectroscopy; de novo protein design; energy landscape roughness; friction
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