Giới Thiệu Về Huỳnh Quang: Lý Thuyết và Ứng Dụng

Trường đại học

University of Hawaii at Manoa

Chuyên ngành

Biochemistry

Người đăng

Ẩn danh

Thể loại

thesis

2014

305
0
0

Phí lưu trữ

75 Point

Mục lục chi tiết

Preface

1. CHAPTER 1: Introduction

1.1. What Is Fluorescence and How Is It Used?

1.2. A Nano-History of Fluorescence

1.3. Excited State Lifetime

1.4. And the Rest

1.5. General Fluorescence Texts

2. CHAPTER 2: Absorption of Light

2.1. Electromagnetic Radiation: Characterization

2.2. Relevant Wavelength Range

2.3. Absorption of Light by Molecules

2.4. Franck–Condon Principle

2.5. Effect of Conjugation on Absorption

2.6. Effects of Molecular Environment on Absorption

2.7. Beer–Lambert Law

2.8. Departures from Beer–Lambert Law

3. CHAPTER 3: Instrumentation

3.1. Photon Counting versus Analog Detection

4. CHAPTER 4: Emission and Excitation Spectra

4.1. Why Do We Want Emission Spectra?

4.2. Correcting Emission Spectra

4.3. Correcting for Background

4.4. Correcting for Instrumental Parameters

4.5. Spectral Center of Mass

4.6. Advanced Scanning Methods

5. CHAPTER 5: Polarization and Anisotropy

5.1. Some Applications of Polarization/Anisotropy

5.2. Protein/Ligand Interactions

5.3. Fluorescence Polarization Immunoassay

5.4. Numerical Aperture Effects

5.5. Effect of Scattering

5.6. Rayleigh Scatter and Rayleigh Ghosts

5.7. Scattering of the Fluorescence

5.8. Depolarization via FRET

6. CHAPTER 6: Time-Resolved Fluorescence

6.1. Excited State Lifetimes

6.2. Time Correlated Single Photon Counting

6.3. Frequency Domain Instrumentation

6.4. Time Domain versus Frequency Domain

6.5. Anisotropy Decay/Dynamic Polarization

7. CHAPTER 7: Quantum Yields and Quenching

7.1. Determination of QYs

7.2. Kasha–Vavilov Rule

7.3. Collisional or Dynamic Quenching

7.4. Quenching and Membrane Systems

8. CHAPTER 8: Förster Resonance Energy Transfer

8.1. How Do We Determine the Efficiency of Energy Transfer (E)?

8.2. Steady-State Intensity

8.3. Time-Resolved Method: Decrease in the Lifetime of the Donor

8.4. The Orientation Factor

8.5. How Do We Determine κ2?

8.6. Homo-Transfer of Electronic Excitation Energy

8.7. Examples of FRET Applications

9. CHAPTER 9: Brief Overview of Fluorescence Microscopy

9.1. Introduction of Fluorophores into Living Cells

9.2. Fluorescence Microscopy Approaches

9.3. Total Internal Reflection Fluorescence

9.4. Multi-Photon Excitation

9.5. Fluorescence Fluctuation Spectroscopy (FFS)

9.6. Fluorescence Recovery after Photobleaching (FRAP)

9.7. Fluorescence Lifetime Imaging Microscopy (FLIM)

9.8. Super-Resolution Techniques

9.9. Single-Molecule Fluorescence

9.10. Where Do Fluorophores Come From?

9.11. How Does One Choose a Fluorophore?

9.12. Labeling Proteins In Vitro

9.12.1. Amine Reactive Probes

9.12.2. Thiol Reactive Probes

9.12.3. Separation of Labeled Protein from Unreacted Probe

9.12.4. Determination of the Extent of Labeling

9.13. Membrane Probes

9.14. Additional Comments on Membrane Systems

9.15. Nucleic Acid Probes and Nucleotide/Nucleoside Analogs

9.16. Voltage-Sensitive Dyes

11. CHAPTER 11: Intrinsic Protein Fluorescence

11.1. Electronic Energy Transfer in Proteins

11.2. Use of Site-Directed Mutagenesis

11.3. Protein Unfolding/Refolding

11.4. Intrinsic Fluorescence Spectra/Intensity

11.5. Protein–Protein and Protein–DNA Interactions

11.6. Phasors and Protein Fluorescence

Appendix: Rogue’s Gallery of Fluorescence Artifacts and Errors