Reviews in fluorescence 2015. (2016)
- Record Type:
- Book
- Title:
- Reviews in fluorescence 2015. (2016)
- Main Title:
- Reviews in fluorescence 2015
- Further Information:
- Note: Chris D. Geddes, editor.
- Editors:
- Geddes, Chris D
- Contents:
- Preface; Contents; Chapter 1: Studying Protein Misfolding and Aggregation by Fluorescence Spectroscopy; 1.1 A Brief Introduction to Protein Misfolding and Aggregation; 1.2 Experimental Techniques to Study Protein Aggregation; 1.3 Fluorescence Spectroscopy and Protein Aggregation; 1.4 Fluorescence Techniques to Study Protein Oligomers and Amyloids During Protein Aggregation; 1.4.1 Fluorescence Intensity, Spectrum and Lifetime; 1.4.1.1 Intrinsic Fluorophores; 1.4.1.2 Extrinsic Fluorophores; 1.4.2 Fluorescence Polarization (Anisotropy); 1.4.3 Fluorescence Quenching. 1.4.4 Fluorescence Resonance Energy Transfer (FRET)1.4.5 Single-Molecule Fluorescence Studies; 1.4.6 Fluorescence Correlation Spectroscopy (FCS); 1.5 Case Studies from our Laboratory at IISER Mohali; 1.5.1 Lysozyme Aggregation; 1.5.2 Serum Albumin Aggregation; 1.5.3 Conformational Property of kappa-Casein -- A Model Intrinsically Disordered Protein; 1.6 Conclusions and Future Directions; References; Chapter 2: Time-Dependent Spectral Shifts in Tryptophan Fluorescence: Bridging Experiments with Molecular Dynamics Simulations; 2.1 Introduction. 2.2 Relationship Between Spectral Shifts and Electronic Energy Levels2.3 Effect of the Electric Field on the Electronic Energy Levels; 2.4 Nonlinear Stark Effect; 2.5 Hybrid QM-MD Versus Classical MD; 2.6 Direct-Response Versus Linear-Response Method; 2.7 Separation of Contributions from Different Motions; 2.8 Dielectric Relaxation of Bulk Solvent; 2.9 Relaxation of WaterPreface; Contents; Chapter 1: Studying Protein Misfolding and Aggregation by Fluorescence Spectroscopy; 1.1 A Brief Introduction to Protein Misfolding and Aggregation; 1.2 Experimental Techniques to Study Protein Aggregation; 1.3 Fluorescence Spectroscopy and Protein Aggregation; 1.4 Fluorescence Techniques to Study Protein Oligomers and Amyloids During Protein Aggregation; 1.4.1 Fluorescence Intensity, Spectrum and Lifetime; 1.4.1.1 Intrinsic Fluorophores; 1.4.1.2 Extrinsic Fluorophores; 1.4.2 Fluorescence Polarization (Anisotropy); 1.4.3 Fluorescence Quenching. 1.4.4 Fluorescence Resonance Energy Transfer (FRET)1.4.5 Single-Molecule Fluorescence Studies; 1.4.6 Fluorescence Correlation Spectroscopy (FCS); 1.5 Case Studies from our Laboratory at IISER Mohali; 1.5.1 Lysozyme Aggregation; 1.5.2 Serum Albumin Aggregation; 1.5.3 Conformational Property of kappa-Casein -- A Model Intrinsically Disordered Protein; 1.6 Conclusions and Future Directions; References; Chapter 2: Time-Dependent Spectral Shifts in Tryptophan Fluorescence: Bridging Experiments with Molecular Dynamics Simulations; 2.1 Introduction. 2.2 Relationship Between Spectral Shifts and Electronic Energy Levels2.3 Effect of the Electric Field on the Electronic Energy Levels; 2.4 Nonlinear Stark Effect; 2.5 Hybrid QM-MD Versus Classical MD; 2.6 Direct-Response Versus Linear-Response Method; 2.7 Separation of Contributions from Different Motions; 2.8 Dielectric Relaxation of Bulk Solvent; 2.9 Relaxation of Water Molecules Near Protein Surface and Inside Protein; 2.10 Separation of Relaxation Modes by Their Time Scales; 2.11 Conclusions; References; Chapter 3: Directional Fluorescence Based on Surface Plasmon-Coupling. 3.1 Introduction3.2 Properties of SPCE; 3.2.1 Directional Emission; 3.2.2 Background Suppression; 3.2.3 P-Polarized Emission; 3.2.4 Distance-Determined Coupling; 3.3 The Strategies for Improving SPCE; 3.3.1 Enlarging the Optical Window; 3.3.2 Improving the Applicability and Sensitivity; 3.3.3 Obtaining Controllable Coupling with Spatial Resolution; 3.4 SPCE Optical Imaging; 3.4.1 SPCE Imaging System Based on Microscope Technique; 3.4.2 Point Spread Function of SPCE Microscope; 3.4.3 Present Researches Utilizing Optical Imaging; 3.5 The Applications of SPCE in Analysis; 3.5.1 DNA Sensing. 3.5.2 Aptamers-Based Protein Sensing3.5.3 Immunological Detection; 3.5.4 Other Fluorescence Analysis; 3.6 Conclusions; References; Chapter 4: Fluorescence Analysis of Thermoresponsive Polymers; 4.1 Introduction; 4.2 Stimuli-Responsive Polymers; 4.2.1 Thermoresponsive Polymers; 4.2.2 Poly(N-IsoPropylAcrylamide), PNIPAm; 4.3 Polymer Characterisation by Fluorescence; 4.4 Thermoresponsive Polymer Characterization; 4.4.1 Water Sorption; 4.4.2 Physicochemical Parameters by Solvatochromism; 4.4.3 Physicochemical Parameters by Fluorescence. … (more)
- Publisher Details:
- Cham : Springer
- Publication Date:
- 2016
- Extent:
- 1 online resource (viii, 380 pages), illustrations (some color)
- Subjects:
- 535/.352
Medicine
Fluorescence
Biotechnology
Analytical biochemistry
Chemistry, Physical organic
SCIENCE -- Physics -- Optics & Light
Fluorescence
Science -- Biotechnology
Science -- Chemistry -- Analytic
Science -- Chemistry -- Physical & Theoretical
Biotechnology
Analytical chemistry
Physical chemistry
Medical -- General
Medical research
Electronic books - Languages:
- English
- ISBNs:
- 9783319246093
3319246097
3319246070
9783319246079 - Related ISBNs:
- 9783319246079
- Notes:
- Note: Online resource; title from PDF title page (SpringerLink, viewed January 4, 2016).
- 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).
- Access Usage:
- Restricted: Printing from this resource is governed by The Legal Deposit Libraries (Non-Print Works) Regulations (UK) and UK copyright law currently in force.
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library HMNTS - ELD.DS.326704
- Ingest File:
- 03_014.xml