Investigation of nanoscopic dynamics and potentials by interferometric scattering microscopy. (2018)
- Record Type:
- Book
- Title:
- Investigation of nanoscopic dynamics and potentials by interferometric scattering microscopy. (2018)
- Main Title:
- Investigation of nanoscopic dynamics and potentials by interferometric scattering microscopy
- Further Information:
- Note: Jaime Ortega Arroyo.
- Authors:
- Arroyo, Jaime Ortega
- Contents:
- Intro; Supervisor's Foreword; Abstract; Parts of this thesis have been published in the following journal articles:; Acknowledgements; Contents; List of Figures; 1 Introduction; References; 2 Non-fluorescent Single-Molecule Approaches to Optical Microscopy; 2.1 Introduction; 2.2 Single-Particle Tracking; 2.3 Scattering Detection: An Alternative to Fluorescence; 2.4 Interferometric Scattering; 2.4.1 Confocal Detection; 2.4.2 Non-scanned Wide-Field Detection; 2.4.3 Confocal Beam Scanning Wide-Field Detection; 2.5 Applications; 2.5.1 Lateral Single-Particle Tracking 2.5.2 Axial Localisation via Interferometry2.5.3 Label-Free Imaging; 2.6 Conclusion and Outlook; References; 3 Experimental Methods; 3.1 Experimental Optics and Hardware; 3.1.1 Interferometric Scattering Channel; 3.1.2 Focus Control Feedback Channel; 3.1.3 Single-Molecule Fluorescence Channel; 3.1.4 Sample Stage Stabilisation; 3.1.5 Camera Characterisation; 3.1.6 Operation and Synchronisation of the Acousto-Optic Beam Deflector; 3.1.7 Data Acquisition; 3.2 Experimental iSCAT Microscopy; 3.2.1 Image Processing; 3.2.2 Spot Detection; 3.2.3 Localisation; 3.2.4 Trajectory Linking 3.2.5 Assessment of Localisation Precision3.2.6 Self-referencing; References; 4 Anomalous Diffusion Due to Interleaflet Coupling and Molecular Pinning; 4.1 Introduction; 4.2 Experimental Methods; 4.2.1 Materials; 4.2.2 Vesicle Preparation; 4.2.3 Substrate Preparation; 4.2.4 Supported Lipid Bilayer Formation; 4.2.5 Instrument Setup Parameters;Intro; Supervisor's Foreword; Abstract; Parts of this thesis have been published in the following journal articles:; Acknowledgements; Contents; List of Figures; 1 Introduction; References; 2 Non-fluorescent Single-Molecule Approaches to Optical Microscopy; 2.1 Introduction; 2.2 Single-Particle Tracking; 2.3 Scattering Detection: An Alternative to Fluorescence; 2.4 Interferometric Scattering; 2.4.1 Confocal Detection; 2.4.2 Non-scanned Wide-Field Detection; 2.4.3 Confocal Beam Scanning Wide-Field Detection; 2.5 Applications; 2.5.1 Lateral Single-Particle Tracking 2.5.2 Axial Localisation via Interferometry2.5.3 Label-Free Imaging; 2.6 Conclusion and Outlook; References; 3 Experimental Methods; 3.1 Experimental Optics and Hardware; 3.1.1 Interferometric Scattering Channel; 3.1.2 Focus Control Feedback Channel; 3.1.3 Single-Molecule Fluorescence Channel; 3.1.4 Sample Stage Stabilisation; 3.1.5 Camera Characterisation; 3.1.6 Operation and Synchronisation of the Acousto-Optic Beam Deflector; 3.1.7 Data Acquisition; 3.2 Experimental iSCAT Microscopy; 3.2.1 Image Processing; 3.2.2 Spot Detection; 3.2.3 Localisation; 3.2.4 Trajectory Linking 3.2.5 Assessment of Localisation Precision3.2.6 Self-referencing; References; 4 Anomalous Diffusion Due to Interleaflet Coupling and Molecular Pinning; 4.1 Introduction; 4.2 Experimental Methods; 4.2.1 Materials; 4.2.2 Vesicle Preparation; 4.2.3 Substrate Preparation; 4.2.4 Supported Lipid Bilayer Formation; 4.2.5 Instrument Setup Parameters; 4.3 Experimental Results; 4.3.1 GM1 Undergoes Anomalous Diffusion in Supported Lipid Bilayers; 4.3.2 Transient Confinement Causes Anomalous Diffusion; 4.3.3 Concentration Dependent Dynamics of Transient Binding 4.3.4 Recovery of Brownian Motion upon Tuning Substrate Interactions and Interleaflet Coupling4.4 Discussion; 4.4.1 Importance of Simultaneous Localisation Precision and Time Resolution; 4.4.2 Thermal and Optical Force Considerations; 4.4.3 Membrane Defects, Labelling Artefacts, and CTxB Induced Aggregation Do Not Cause Transient Binding; 4.4.4 Transient Binding Requires Substrate Interaction and Interleaflet Coupling; 4.4.5 Multiple CTxB-GM1 Interactions Result in Ring-Like Structures; 4.4.6 A Model of Transient Binding: Molecular Pinning; 4.5 Conclusion and Outlook; References 5 Structural Dynamics of Myosin 5a5.1 Introduction; 5.2 Experimental Methods; 5.2.1 Sample Preparation; 5.2.2 Experimental Setup; 5.3 Experimental Results; 5.3.1 N-Terminus Labelling Does Not Perturb the Kinetics of Myosin 5a; 5.3.2 During Myosin Movement the Motor Domain Undergoes a Transition Between Two Distinct States; 5.3.3 The Labelled Motor Domain Moves in Three Dimensions; 5.3.4 A Conformational Change in the Motor Domain Accompanies the Power Stroke; 5.3.5 Myosin Steps via a Single, Spatially-Constrained Transient State … (more)
- Publisher Details:
- Cham, Switzerland : Springer
- Publication Date:
- 2018
- Extent:
- 1 online resource (xxxvi, 142 pages), illustrations (some color)
- Subjects:
- 570.28/2
Chemistry
Microscopy
Interferometry
NATURE -- Reference
SCIENCE -- Life Sciences -- Biology
SCIENCE -- Life Sciences -- General
Interferometry
Microscopy
Science -- Chemistry -- Organic
Science -- Life Sciences -- Biology -- Molecular Biology
Science -- Molecular Physics
Organic chemistry
Cellular biology (cytology)
Atomic & molecular physics
Chemistry, Physical organic
Chemistry, Organic
Cytology
Science -- Chemistry -- Physical & Theoretical
Physical chemistry
Electronic books - Languages:
- English
- ISBNs:
- 9783319770956
3319770950 - Related ISBNs:
- 9783319770949
3319770942 - Notes:
- Note: Includes bibliographical references.
Note: Online resource; title from PDF title page (SpringerLink, viewed March 21, 2018). - Access Rights:
- Legal Deposit; Only available on premises controlled by the deposit library and to one user at any one time; The Legal Deposit Libraries (Non-Print Works) Regulations (UK).
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- Restricted: Printing from this resource is governed by The Legal Deposit Libraries (Non-Print Works) Regulations (UK) and UK copyright law currently in force.
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- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library HMNTS - ELD.DS.371166
- Ingest File:
- 01_357.xml