A5052536069- Force Microscopy Techniques and Applications
- RNA and protein synthesis mechanisms
- Protein Structure and Dynamics
- Orbital Angular Momentum in Optics
- Mechanical and Optical Resonators
- Biochemical and Structural Characterization
- Advanced Fluorescence Microscopy Techniques
- Microfluidic and Capillary Electrophoresis Applications
- Bioinformatics and Genomic Networks
- Bacterial Genetics and Biotechnology
- Microfluidic and Bio-sensing Technologies
- Genetic Neurodegenerative Diseases
- Cellular Mechanics and Interactions
- RNA Research and Splicing
University of Zurich
2023
Zürcher Fachhochschule
2023
University of Cambridge
2019-2022
Google (United States)
2018
Abstract Accurate and stable site-specific attachment of DNA molecules to proteins is a requirement for many single-molecule force spectroscopy techniques. The most commonly used method still relies on maleimide chemistry involving cysteine residues in the protein interest. Studies have consequently often focused model that either no cysteines or with small number can be deleted so then introduced at specific sites. However, proteins, especially eukaryotes, contain too amenable this...
Nanohole optical tweezers have been used by several groups to trap and analyze proteins. In this work, we demonstrate that it is possible create high-performance double nanohole (DNH) substrates for trapping proteins without the need any top-down approaches (such as electron microscopy or focused-ion beam milling). Using polarization analysis, identify DNHs well determine their orientation then use them trapping. We are also able other hole configurations, such single, trimers clusters....
Label-free detection of single biomolecules in solution has been achieved using a variety experimental approaches over the past decade. Yet, our understanding magnitude optical contrast and its relationship with underlying atomic structure as well achievable measurement sensitivity precision remain poorly defined. Here, we use Fourier optics approach combined an structure-based molecular polarizability model to simulate mass photometry experiments from first principles. We find excellent...
Tandem-repeat proteins comprise small secondary structure motifs that stack to form one-dimensional arrays with distinctive mechanical properties are proposed direct their cellular functions. Here, we use single-molecule optical tweezers study the folding of consensus-designed tetratricopeptide repeats (CTPRs), superhelical short helix-turn-helix motifs. We find CTPRs display a spring-like response in which individual undergo rapid equilibrium fluctuations between partially folded and...
Abstract Label-free detection of single biomolecules in solution has been achieved using a variety experimental approaches over the past decade. Yet, our understanding magnitude optical contrast and its relationship to underlying atomic structure, as well achievable measurement sensitivity precision remain poorly defined. Here, we use Fourier optics approach combined with an structure-based molecular polarizability model simulate mass photometry experiments from first principles. We find...
Abstract Tandem-repeat proteins comprise small secondary structure motifs that stack to form one-dimensional arrays with distinctive mechanical properties are proposed direct their cellular functions. Here, we use single-molecule optical tweezers study the folding of consensus-designed tetratricopeptide repeats (CTPRs) — superhelical short helix-turn-helix motifs. We find CTPRs display a spring-like response in which individual undergo rapid equilibrium fluctuations between folded and...
Single-molecule force spectroscopy using optical tweezers continues to provide detailed insights into the behavior of nanoscale systems. Obtaining precise measurements their mechanical properties is highly dependent on accurate instrument calibration. Therefore, instrumental drift or inaccurate calibration may prevent reaching an accuracy at theoretical limit and lead incorrect conclusions. Commonly encountered sources error include inaccuracies in detector sensitivity trap stiffness...
ABSTRACT Accurate and stable site-specific attachment of DNA molecules to proteins is a requirement for many single-molecule force spectroscopy techniques. The most commonly used method still relies on maleimide chemistry involving cysteine residues in the protein interest. Studies have consequently often focused model that either no cysteines or with small number can be deleted so then introduced at specific sites. However, proteins, especially eukaryotes, contain too amenable this...