Analytical Techniques for the Elucidation of Protein Function (eBook, ePUB)

Redaktion: Suetake, Isao; Hojo, Hironobu; Sharma, Rohit K.

• Format: ePub

Produktbeschreibung

ANALYTICAL TECHNIQUES FOR THE ELUCIDATION OF PROTEIN FUNCTION An essential aid for scientists seeking alternative techniques for investigating proteins Proteins are the building blocks of living organisms, and they play an enormous range of fundamental roles in sustaining and shaping life. The critical determinant of a protein's function is its structure, and the analysis of protein structures has therefore become a significant component of biological research. In recent years, longstanding analytical techniques such as X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy have been supplemented by a number of new methods which promise to revolutionize the study of proteins and their functions. Analytical Techniques for the Elucidation of Protein Function serves as an introduction to these techniques, which are especially crucial for analyzing intrinsically disordered regions and post-translational modifications. These have revolutionized the study of proteins in recent years, and conventional methods for analyzing protein structures are no longer sufficient to work through their ramifications. This book therefore brings greater awareness of techniques which promise to produce the very cutting edge of protein research. Analytical Techniques for the Elucidation of Protein Function readers will find: * A discussion of techniques including electron paramagnetic resonance (ESR) spectroscopy, neutron scattering, Raman imaging, and more * Both theoretical background and practical applications for each technique * Contributions from leading international researchers into protein structure and function This practically focused text is a valuable reference for protein and peptide analysis and synthesis researchers, as well as for graduate and advanced undergraduate students in the life sciences.

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Produktdetails

• Verlag: John Wiley & Sons
• Seitenzahl: 240
• Erscheinungstermin: 4. Januar 2023
• Englisch
• ISBN-13: 9781119886341
• Artikelnr.: 67287866

Autorenporträt

Isao Suetake, Ph.D, is Professor at Nakamura Gakuen University, Japan. He has published widely on the molecular mechanisms of epigenetics. Rohit K. Sharma, Ph.D, is Assistant Professor in the Department of Chemistry, Panjab University, India. His research focuses on peptide/protein conjugated nanostructures in drug delivery and related areas. Hironobu Hojo, Ph.D, is Professor at the Institute for Protein Research, Osaka University, Japan. He has published widely on the chemical synthesis of proteins and related subjects.

Inhaltsangabe

Preface ix

Editor's Biographies xi

List of Contributors xiii

1 EPR Spectroscopy 1

1.1 Outline of EPR Spectroscopy 2
Hiroyuki Mino

1.1.1 Overview 2

1.2 Biological Applications of EPR 13
Isao Suetake, Risa Mutoh, Yuichi Mishima, Masatomo So, and Hironobu Hojo

1.2.1 Proteins and Their Structures: Domain and Intrinsically Disordered Region 13

1.2.2 Introduction of Spin Probes on Proteins 14

1.2.3 Measurement of Constant Wave (CW)-EPR Spectrum 19

1.2.4 Application of CW-EPR to Protein (Clock Protein, Amyloid Proteins, and HP1) 21

1.2.4.1 Clock Proteins 22

1.2.4.2 Amyloid Proteins (Aß Peptide, ß 2 -microglobulin, alpha-synuclein, Tau, and Prion) 23

1.2.4.3 Heterochromatin Protein 1 (HP1) 26

1.2.5 Measurement of Longer Distance between Spin-spin (HP1, Tau, alpha-synuclein) 29

1.2.6 Biophysical Functions of Protein Dynamics 31

1.2.7 Summary/Conclusion 31

2 Introduction to Incoherent Neutron Scattering: A Powerful Technique to Investigate the Dynamics of Bio-macromolecules 39
Tatsuhito Matsuo and Judith Peters

2.1 Introduction 39

2.2 Basic Theory and Dynamical Information Obtained from iNS 42

2.2.1 Basic Principle of iNS Experiments 42

2.2.2 Incoherent Scattering Function 45

2.2.3 Dynamical Information Obtained by iNS 51

2.2.3.1 Elastic Incoherent Neutron Scattering (EINS) 52

2.2.3.2 Quasi-elastic Neutron Scattering (QENS) 53

2.3 Examples of Biological Applications of iNS 58

2.3.1 Dynamical Modulation of Proteins Caused by a Disease-causing Point Mutation 58

2.3.2 Dynamical Differences between Amyloid Polymorphic Fibrils Showing Different Levels of Cytotoxicity 59

2.3.3 New Theoretical Framework to Describe the Dynamical Behavior of Lipid Molecules 60

2.3.4 Separation of Dynamics of Protein-detergent Complexes 61

2.3.5 Hydration Water Mobility around Proteins 62

2.4 Summary 63

3 Elucidation of Protein Function Using Raman Spectroscopy 69
Saima Malik, Maitrayee U. Trivedi, Gurpreet K. Soni, and Rohit K. Sharma

3.1 Introduction 69

3.2 Basic Principle and Working of Raman Spectroscopy 71

3.2.1 Theory and Frequencies of Raman Spectroscopy 71

3.2.2 Instrumentation 73

3.3 Advances in Raman Spectroscopy Techniques 74

3.3.1 Resonance Raman Spectroscopy for Protein Analysis 74

3.3.1.1 Ultraviolet Resonance Raman Spectroscopy 75

3.3.1.2 Time-resolved Resonance Raman Spectroscopy 76

3.3.2 Surface-enhanced Raman Spectroscopy (SERS) 77

3.3.3 Tip-enhanced Raman Spectroscopy 80

3.3.4 Polarized Raman Spectroscopy 83

3.3.5 Raman Crystallography 85

3.3.6 2D-COS Raman Spectroscopy 88

3.4 Applications 91

3.5 Conclusion 92

4 Fundamental Principles of Impedance Spectroscopy and its Biological Applications 101
Yusuke Tsutsui

4.1 Introduction 101

4.1.1 Basic Concept of Impedance Spectroscopy 101

4.1.2 Description of Impedance for Capacitors and Inductors 105

4.1.3 Nyquist Plot 106

4.1.4 Debye Model 108

4.1.5 Constant Phase and Warburg Element to Model Distorted and Diffusive Components 111

4.2 Biological Applications of Impedance Spectroscopy 113

4.2.1 Detection of DNA Hybridization and Photodamage 113

4.2.2 Detection and Analysis of Proteins 115

4.3 Conclusion 119

5 Mass Spectrometry Imaging 125
Shuichi Shimma

5.1 Introduction 125

5.2 Workflow of MSI 126