Mass spectrometry of protein interactions:
Gespeichert in:
| Format: | Buch |
|---|---|
| Sprache: | English |
| Veröffentlicht: |
Hoboken, NJ
Wiley
2007
|
| Schriftenreihe: | Wiley-Interscience series on mass spectrometry
|
| Schlagworte: | |
| Online-Zugang: | Inhaltsverzeichnis |
| Beschreibung: | XII, 137 S. Ill., graph. Darst. |
| ISBN: | 0471793736 9780471793731 |
Internformat
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| 245 | 1 | 0 | |a Mass spectrometry of protein interactions |c ed. by Kevin M. Downard |
| 264 | 1 | |a Hoboken, NJ |b Wiley |c 2007 | |
| 300 | |a XII, 137 S. |b Ill., graph. Darst. | ||
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| 490 | 0 | |a Wiley-Interscience series on mass spectrometry | |
| 650 | 4 | |a Protein-protein interactions | |
| 650 | 4 | |a Mass spectrometry | |
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| 650 | 4 | |a Mass Spectrometry |x methods | |
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| adam_text | CONTENTS
Preface ix
Contributors xi
1 Direct Characterization of Protein Complexes by Electrospray
Ionization Mass Spectrometry and Ion Mobility Analysis 1
Joseph A. Loo and Catherine S. Kaddis
1.1 Introduction, 2
1.1.1 Historical Perspective of ESI MS for Measuring Protein
Complexes, 3
1.1.2 Types of Interactions that Are Probed by ESI MS, 6
1.2 Critical Aspects of the Experimental Procedure, 8
1.2.1 Instrumental Parameters, 8
1.2.1.1 Electrospray Ionization Source, 9
1.2.1.2 Atmosphere/Vacuum Interface and Pressure, 9
1.2.1.3 Mass Spectrometry Analyzers, 10
1.2.1.4 Ion Mobility Analyzers, 12
1.2.2 Sample Preparation, 15
1.3 Solution Phase Equilibria and Gas Phase Dissociation, 16
1.3.1 Measuring Solution Dissociation Constants, 16
1.3.2 Tandem Mass Spectrometry of Protein Complexes, 16
1.4 Conclusions, 18
Acknowledgments, 19
References, 19
V
vi CONTENTS
2 Softly, Softly—Detection of Protein Complexes
by Matrix Assisted Laser Desorption Ionization
Mass Spectrometry 25
Kevin M. Downard
2.1 Introduction, 25
2.2 First Glimpses and the First Shot Phenomenon, 28
2.3 Matrix and Solution Criteria to Preserve Protein Complexes, 30
2.4 Laser Fluence, Wavelength, and Ion Extraction, 32
2.5 Preservation of Protein Complexes on Conventional MALDI
Targets, 35
2.6 Affinity Targets and Surfaces Coupled to MALDI, 37
2.7 Conclusions, 39
References, 39
3 Probing Protein Interactions Using Hydrogen Deuterium
Exchange Mass Spectrometry 45
David D. Weis, Suma Kaveti, Yan Wu, and John R. Engen
3.1 Introduction, 46
3.2 Hydrogen Exchange Background, 46
3.3 General HX MS Method, 47
3.3.1 Location Information Provided by HX MS, 49
3.3.2 Revealing Interactions by Comparison, 50
3.4 Interactions of Proteins, 50
3.5 Examples, 52
3.5.1 Conformational Changes of Proteins During Binding, 52
3.5.2 Protein Protein Interactions, 52
3.5.3 Protein Peptide Interactions, 54
3.5.4 Protein Small Molecule Interactions, 55
3.6 Conclusions, 57
Acknowledgements, 57
References, 57
4 Limited Proteolysis Mass Spectrometry of Protein Complexes 63
Maria Monti and Piero Pucci
4.1 Introduction, 63
4.2 Limited Proteolysis Analysis, 64
4.3 Experimental Design, 67
4.4 Probing Protein Protein Interactions, 69
4.5 Probing Protein Nucleic Acid Interactions, 72
4.6 Probing Protein Ligand Interactions, 74
CONTENTS vii
4.7 Probing Amyloid Fibril Core, 76
4.8 Conclusions, 78
References, 78
5 Chemical Cross Linking and Mass Spectrometry
for Investigation of Protein Protein Interactions 83
Andrea Sinz
5.1 Introduction, 84
5.2 Cross Linking Strategies, 85
5.2.1 Bottom Up Approach, 85
5.2.2 Top Down Approach, 88
5.3 Functional Groups of Cross Linking Reagents:
Reactivities, 89
5.3.1 Amine Reactive Cross Linkers, 89
5.3.2 Sulfhydryl Reactive Cross Linkers, 91
5.3.3 Photoreactive Cross Linkers, 91
5.4 Cross Linker Design, 92
5.4.1 Homobifunctional Cross Linkers, 92
5.4.2 Heterobifunctional Cross Linkers, 93
5.4.3 Zero Length Cross Linkers, 93
5.4.4 Trifunctional Cross Linkers, 93
5.5 Mass Spectrometric Analysis of Cross Linked Products, 94
5.5.1 Bottom Up Analysis by MALDI MS, 94
5.5.2 Bottom Up Analysis by ESI MS (LC/MS), 94
5.5.3 Bottom Up and Top Down Analysis
by ESI FTICR MS, 95
5.6 Identification of Cross Linked Products, 97
5.7 Computer Software for Data Analysis, 99
5.8 Conclusions and Perspectives, 99
Abbreviations, 100
Acknowledgments, 100
References, 101
6 Genesis and Application of Radical Probe Mass Spectrometry
(RP MS) to Study Protein Interactions 109
Simin D. Maleknia and Kevin M. Downard
6.1 Genesis of Radical Probe Mass Spectrometry, 110
6.2 The Reactive Residue Side Chains, 111
6.3 Conditions Important to Radical Probe Mass Spectrometry
Experiments, 115
viii CONTENTS
6.4 Generation of Radicals on Millisecond Timescales, 117
6.5 Applications of RP MS to Studies of Protein Interactions, 119
6.5.1 Intramolecular Interactions, 120
6.5.2 Intermolecular Interactions: Protein Peptide and
Protein Protein Complexes, 122
6.6 Onset of Oxidative Damage and Its Implications for Protein
Interactions, 126
6.7 Application of Radical Oxidation to Study Protein
Assemblies, 128
6.8 Modeling Protein Complexes with Data from
RP MS Experiments, 129
6.9 Conclusions, 130
References, 131
Index 135
|
| adam_txt |
CONTENTS
Preface ix
Contributors xi
1 Direct Characterization of Protein Complexes by Electrospray
Ionization Mass Spectrometry and Ion Mobility Analysis 1
Joseph A. Loo and Catherine S. Kaddis
1.1 Introduction, 2
1.1.1 Historical Perspective of ESI MS for Measuring Protein
Complexes, 3
1.1.2 Types of Interactions that Are Probed by ESI MS, 6
1.2 Critical Aspects of the Experimental Procedure, 8
1.2.1 Instrumental Parameters, 8
1.2.1.1 Electrospray Ionization Source, 9
1.2.1.2 Atmosphere/Vacuum Interface and Pressure, 9
1.2.1.3 Mass Spectrometry Analyzers, 10
1.2.1.4 Ion Mobility Analyzers, 12
1.2.2 Sample Preparation, 15
1.3 Solution Phase Equilibria and Gas Phase Dissociation, 16
1.3.1 Measuring Solution Dissociation Constants, 16
1.3.2 Tandem Mass Spectrometry of Protein Complexes, 16
1.4 Conclusions, 18
Acknowledgments, 19
References, 19
V
vi CONTENTS
2 Softly, Softly—Detection of Protein Complexes
by Matrix Assisted Laser Desorption Ionization
Mass Spectrometry 25
Kevin M. Downard
2.1 Introduction, 25
2.2 First Glimpses and the First Shot Phenomenon, 28
2.3 Matrix and Solution Criteria to Preserve Protein Complexes, 30
2.4 Laser Fluence, Wavelength, and Ion Extraction, 32
2.5 Preservation of Protein Complexes on Conventional MALDI
Targets, 35
2.6 Affinity Targets and Surfaces Coupled to MALDI, 37
2.7 Conclusions, 39
References, 39
3 Probing Protein Interactions Using Hydrogen Deuterium
Exchange Mass Spectrometry 45
David D. Weis, Suma Kaveti, Yan Wu, and John R. Engen
3.1 Introduction, 46
3.2 Hydrogen Exchange Background, 46
3.3 General HX MS Method, 47
3.3.1 Location Information Provided by HX MS, 49
3.3.2 Revealing Interactions by Comparison, 50
3.4 Interactions of Proteins, 50
3.5 Examples, 52
3.5.1 Conformational Changes of Proteins During Binding, 52
3.5.2 Protein Protein Interactions, 52
3.5.3 Protein Peptide Interactions, 54
3.5.4 Protein Small Molecule Interactions, 55
3.6 Conclusions, 57
Acknowledgements, 57
References, 57
4 Limited Proteolysis Mass Spectrometry of Protein Complexes 63
Maria Monti and Piero Pucci
4.1 Introduction, 63
4.2 Limited Proteolysis Analysis, 64
4.3 Experimental Design, 67
4.4 Probing Protein Protein Interactions, 69
4.5 Probing Protein Nucleic Acid Interactions, 72
4.6 Probing Protein Ligand Interactions, 74
CONTENTS vii
4.7 Probing Amyloid Fibril Core, 76
4.8 Conclusions, 78
References, 78
5 Chemical Cross Linking and Mass Spectrometry
for Investigation of Protein Protein Interactions 83
Andrea Sinz
5.1 Introduction, 84
5.2 Cross Linking Strategies, 85
5.2.1 Bottom Up Approach, 85
5.2.2 Top Down Approach, 88
5.3 Functional Groups of Cross Linking Reagents:
Reactivities, 89
5.3.1 Amine Reactive Cross Linkers, 89
5.3.2 Sulfhydryl Reactive Cross Linkers, 91
5.3.3 Photoreactive Cross Linkers, 91
5.4 Cross Linker Design, 92
5.4.1 Homobifunctional Cross Linkers, 92
5.4.2 Heterobifunctional Cross Linkers, 93
5.4.3 Zero Length Cross Linkers, 93
5.4.4 Trifunctional Cross Linkers, 93
5.5 Mass Spectrometric Analysis of Cross Linked Products, 94
5.5.1 Bottom Up Analysis by MALDI MS, 94
5.5.2 Bottom Up Analysis by ESI MS (LC/MS), 94
5.5.3 Bottom Up and Top Down Analysis
by ESI FTICR MS, 95
5.6 Identification of Cross Linked Products, 97
5.7 Computer Software for Data Analysis, 99
5.8 Conclusions and Perspectives, 99
Abbreviations, 100
Acknowledgments, 100
References, 101
6 Genesis and Application of Radical Probe Mass Spectrometry
(RP MS) to Study Protein Interactions 109
Simin D. Maleknia and Kevin M. Downard
6.1 Genesis of Radical Probe Mass Spectrometry, 110
6.2 The Reactive Residue Side Chains, 111
6.3 Conditions Important to Radical Probe Mass Spectrometry
Experiments, 115
viii CONTENTS
6.4 Generation of Radicals on Millisecond Timescales, 117
6.5 Applications of RP MS to Studies of Protein Interactions, 119
6.5.1 Intramolecular Interactions, 120
6.5.2 Intermolecular Interactions: Protein Peptide and
Protein Protein Complexes, 122
6.6 Onset of Oxidative Damage and Its Implications for Protein
Interactions, 126
6.7 Application of Radical Oxidation to Study Protein
Assemblies, 128
6.8 Modeling Protein Complexes with Data from
RP MS Experiments, 129
6.9 Conclusions, 130
References, 131
Index 135 |
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| index_date | 2024-07-02T16:43:03Z |
| indexdate | 2024-07-09T20:53:36Z |
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| language | English |
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| physical | XII, 137 S. Ill., graph. Darst. |
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| spelling | Mass spectrometry of protein interactions ed. by Kevin M. Downard Hoboken, NJ Wiley 2007 XII, 137 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Wiley-Interscience series on mass spectrometry Protein-protein interactions Mass spectrometry Proteins analysis Mass Spectrometry methods Proteins metabolism Massenspektrometrie (DE-588)4037882-2 gnd rswk-swf Proteine (DE-588)4076388-2 gnd rswk-swf (DE-588)4143413-4 Aufsatzsammlung gnd-content Proteine (DE-588)4076388-2 s Massenspektrometrie (DE-588)4037882-2 s DE-604 Downard, Kevin M. Sonstige oth HBZ Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=015472458&sequence=000008&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Mass spectrometry of protein interactions Protein-protein interactions Mass spectrometry Proteins analysis Mass Spectrometry methods Proteins metabolism Massenspektrometrie (DE-588)4037882-2 gnd Proteine (DE-588)4076388-2 gnd |
| subject_GND | (DE-588)4037882-2 (DE-588)4076388-2 (DE-588)4143413-4 |
| title | Mass spectrometry of protein interactions |
| title_auth | Mass spectrometry of protein interactions |
| title_exact_search | Mass spectrometry of protein interactions |
| title_exact_search_txtP | Mass spectrometry of protein interactions |
| title_full | Mass spectrometry of protein interactions ed. by Kevin M. Downard |
| title_fullStr | Mass spectrometry of protein interactions ed. by Kevin M. Downard |
| title_full_unstemmed | Mass spectrometry of protein interactions ed. by Kevin M. Downard |
| title_short | Mass spectrometry of protein interactions |
| title_sort | mass spectrometry of protein interactions |
| topic | Protein-protein interactions Mass spectrometry Proteins analysis Mass Spectrometry methods Proteins metabolism Massenspektrometrie (DE-588)4037882-2 gnd Proteine (DE-588)4076388-2 gnd |
| topic_facet | Protein-protein interactions Mass spectrometry Proteins analysis Mass Spectrometry methods Proteins metabolism Massenspektrometrie Proteine Aufsatzsammlung |
| url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=015472458&sequence=000008&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
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