| Description |
1 online resource (262 p.) |
| Contents |
Intro -- Title page -- Copyright -- Table of Contents -- Preface -- Editor's Biographies -- List of Contributors -- 1 EPR Spectroscopy -- 1.1 Outline of EPR Spectroscopy -- 1.1.1 Overview -- 1.2 Biological Applications of EPR -- 1.2.1 Proteins and Their Structures: Domain and Intrinsically Disordered Region -- 1.2.2 Introduction of Spin Probes on Proteins -- 1.2.3 Measurement of Constant Wave (CW)-EPR Spectrum -- 1.2.4 Application of CW-EPR to Protein (Clock Protein, Amyloid Proteins, and HP1) -- 1.2.4.1 Clock Proteins |
|
1.2.4.2 Amyloid Proteins (Aß Peptide, ß2-microglobulin, a-synuclein, Tau, and Prion) -- 1.2.4.3 Heterochromatin Protein 1 (HP1) -- 1.2.5 Measurement of Longer Distance between Spin-spin (HP1, Tau, a-synuclein) -- 1.2.6 Biophysical Functions of Protein Dynamics -- 1.2.7 Summary/Conclusion -- 2 Introduction to Incoherent Neutron Scattering: A Powerful Technique to Investigate the Dynamics of Bio-macromolecules -- 2.1 Introduction -- 2.2 Basic Theory and Dynamical Information Obtained from iNS -- 2.2.1 Basic Principle of iNS Experiments -- 2.2.2 Incoherent Scattering Function |
|
2.2.3 Dynamical Information Obtained by iNS -- 2.2.3.1 Elastic Incoherent Neutron Scattering (EINS) -- 2.2.3.2 Quasi-elastic Neutron Scattering (QENS) -- 2.3 Examples of Biological Applications of iNS -- 2.3.1 Dynamical Modulation of Proteins Caused by a Disease-causing Point Mutation -- 2.3.2 Dynamical Differences between Amyloid Polymorphic Fibrils Showing Different Levels of Cytotoxicity -- 2.3.3 New Theoretical Framework to Describe the Dynamical Behavior of Lipid Molecules -- 2.3.4 Separation of Dynamics of Protein-detergent Complexes -- 2.3.5 Hydration Water Mobility around Proteins |
|
2.4 Summary -- 3 Elucidation of Protein Function Using Raman Spectroscopy -- 3.1 Introduction -- 3.2 Basic Principle and Working of Raman Spectroscopy -- 3.2.1 Theory and Frequencies of Raman Spectroscopy -- 3.2.2 Instrumentation -- 3.3 Advances in Raman Spectroscopy Techniques -- 3.3.1 Resonance Raman Spectroscopy for Protein Analysis -- 3.3.1.1 Ultraviolet Resonance Raman Spectroscopy -- 3.3.1.2 Time-resolved Resonance Raman Spectroscopy -- 3.3.2 Surface-enhanced Raman Spectroscopy (SERS) -- 3.3.3 Tip-enhanced Raman Spectroscopy -- 3.3.4 Polarized Raman Spectroscopy |
|
3.3.5 Raman Crystallography -- 3.3.6 2D-COS Raman Spectroscopy -- 3.4 Applications -- 3.5 Conclusion -- 4 Fundamental Principles of Impedance Spectroscopy and its Biological Applications -- 4.1 Introduction -- 4.1.1 Basic Concept of Impedance Spectroscopy -- 4.1.2 Description of Impedance for Capacitors and Inductors -- 4.1.3 Nyquist Plot -- 4.1.4 Debye Model -- 4.1.5 Constant Phase and Warburg Element to Model Distorted and Diffusive Components -- 4.2 Biological Applications of Impedance Spectroscopy -- 4.2.1 Detection of DNA Hybridization and Photodamage |
| Notes |
Description based upon print version of record |
|
4.2.2 Detection and Analysis of Proteins |
| Form |
Electronic book
|
| Author |
Sharma, Rohit K
|
|
Hojo, Hironobu
|
| ISBN |
9781119886341 |
|
1119886341 |
|
