Analyzing biomolecular interactions by mass spectrometry:
Gespeichert in:
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Format: | Buch |
Sprache: | English |
Veröffentlicht: |
Weinheim
Wiley-VCH
2015
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Schlagworte: | |
Online-Zugang: | Inhaltsverzeichnis |
Beschreibung: | XXII, 378 S. Ill., graph. Darst. |
ISBN: | 9783527334643 9783527673391 |
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Datensatz im Suchindex
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adam_text | CONTENTS
LIST OF CONTRIBUTORS XIII
PREFACE XVII
ABBREVIATIONS XIX
1 INTRODUCTION TO MASS SPECTROMETRY, A TUTORIAL 1
WILFRIED M.A. NIESSEN AND DAVID FALCK
1.1 INTRODUCTION 1
1.2 FIGURES OF MERIT 1
1.2.1 INTRODUCTION 1
1.2.2 RESOLUTION 2
1.2.3 MASS ACCURACY 4
1.2.4 GENERAL DATA ACQUISITION IN MS 5
1.3 ANALYTE IONIZATION 6
1.3.1 INTRODUCTION 6
1.3.2 ELE CTROSPRAY IONIZATION 8
1.3.3 MATRIX-ASSISTED LASER DESORPTION IONIZATION 10
1.3.4 OTHER IONIZATION METHODS 10
1.3.5 SOLVENT AND SAMPLE COMPATIBILITY ISSUES 11
1.4 MASS ANALYZER BUILDING BLOCKS 12
1.4.1 INTRODUCTION 12
1.4.2 QUADRUPOLE MASS ANALYZER 13
1.4.3 ION-TRAP MASS ANALYZER 13
1.4.4 TIME-OF-FLIGHT MASS ANALYZER 15
1.4.5 FOURIER TRANSFORM ION CYCLOTRON RESONANCE MASS SPECTROMETER 16
1.4.6 ORBITRAP MASS ANALYZER 17
1.4.7 ION DETECTION 18
1.5 TANDEM MASS SPECTROMETRY 18
1.5.1 INTRODUCTION: TANDEM-IN-TIME AND TANDEM-IN-SPACE 18
1.5.2 ION DISSOCIATION TECHNIQUES 20
1.5.3 TANDEM QUADRUPOLE MS-MS INSTRUMENTS 21
1.5.4 ION-TRAP MS INSTRUMENTS 23
1.5.5 TANDEM TOF (TOF-TOF) INSTRUMENTS 23
1.5.6 HYBRID INSTRUMENTS (Q-TOF, Q-LIT, IT-TOF) 24
HTTP://D-NB.INFO/1058702823
VI
CONTENTS
1.5.7 MS-MS AND MSN IN FT-ICR-MS 26
1.5.8 ORBITRAP-BASED HYBRID SYSTEMS 27
1.5.9 LON-.MOBILITY SPECTROMETRY-MASS SPECTROMETRY 28
1.6 DATA INTERPRETATION AND ANALYTICAL STRATEGIES 30
1.6.1 DATA ACQUISITION IN MS REVISITED 30
1.6.2 QUANTITATIVE BIOANALYSIS AND RESIDUE ANALYSIS 31
1.6.3 IDENTIFICATION OF SMALL-MOLECULE KNOWN UNKNOWNS 32
1.6.4 IDENTIFICATION OF DRUG METABOLITES 33
1.6.5 PROTEIN MOLECULAR WEIGHT DETERMINATION 37
1.6.6 PEPTIDE FRAGMENTATION AND SEQUENCING 38
1.6.7 GENERAL PROTEOMICS STRATEGIES: TOP-DOWN, MIDDLE-DOWN,
BOTTOM-UP 39
1.7 CONCLUSION AND PERSPECTIVES 43
REFERENCES 43
PART I DIRECT MS BASED AFFINITY TECHNIQUES
55
2 STUDYING PROTEIN-PROTEIN INTERACTIONS BY COMBINING NATIVE MASS
SPECTROMETRY AND CHEMICAL CROSS-LINKING
57
MICHAL SHARON AND ANDREA SINZ
2.1 INTRODUCTION 57
2.2 PROTEIN ANALYSIS BY MASS SPECTROMETRY 58
2.3 NATIVE MS 59
2.3.1 INSTRUMENTATION FOR HIGH-MASS ION DETECTION 60
2.3.2 DEFINING THE EXACT MASS OF THE COMPOSING SUBUNITS 60
2.3.3 ANALYZING THE INTACT COMPLEX 61
2.4 CHEMICAL CROSS-LINKING MS 64
2.4.1 TYPES OF CROSS-LINKERS 64
2.4.2 MS/MS CLEAVABLE CROSS-LINKERS
66
2.4.3 DATA ANALYSIS
68
2.5 VALUE OF COMBINING NATIVE MS WITH CHEMICAL CROSS-LINKING MS
68
2.6 REGULATING THE GIANT 69
2.7 CAPTURING TRANSIENT INTERACTIONS 70
2.8 AN INTEGRATIVE APPROACH FOR OBTAINING LOW-RESOLUTION STRUCTURES
OF NATIVE PROTEIN COMPLEXES 72
2.9 FUTURE DIRECTIONS 73
REFERENCES 74
3 NATIVE MASS SPECTROMETRY APPROACHES USING ION MOBILITY-MASS
SPECTROMETRY
81
FREDERIK LERMYTE, ESTHER MARIE MARTIN, ALBERT KONIJNENBERG, FILIP
LEMIERE,
AND FRANK SOBOTT
3.1 INTRODUCTION 81
3.2 SAMPLE PREPARATION 82
3.3 ELECTROSPRAY IONIZATION 84
CONTENTS
VII
3.4 MASS ANALYZERS AND TANDEM MS APPROACHES
88
3.5 ION MOBILITY 90
3.6 DATA PROCESSING 95
3.7 CHALLENGES AND FUTURE PERSPECTIVES 98
REFERENCES 102
PART II LC-MS BASED WITH INDIRECT ASSAYS
109
4 METHODOLOGIES FOR EFFECT-DIRECTED ANALYSIS: ENVIRONMENTAL
APPLICATIONS, FOOD ANALYSIS, AND DRUG DISCOVERY
111
WILLEM JONKER, MARJA LAMOREE, CORINEJ. HOUTMAN, ANDJEROEN KOOL
4.1 INTRODUCTION 111
4.2 PRINCIPLE OF TRADITIONAL EFFECT-DIRECTED ANALYSIS 113
4.3 SAMPLE PREPARATION 113
4.3.1 ENVIRONMENTAL ANALYSIS 113
4.3.1.1 AQUEOUS SAMPLES 113
4.3.1.2 BIOLOGICAL SAMPLES 116
4.3.1.3 SEDIMENT, SOIL, SUSPENDED MATTER 120
4.3.2 FOOD ANALYSIS 121
4.3.2.1 CHROMATOGRAPHY-OLFACTOMETRY 122
4.3.2.2 FUNCTIONAL FOODS 123
4.3.3 DRUG DISCOVERY 124
4.3.3.1 COMBINATORIAL LIBRARIES AND NATURAL EXTRACTS 124
4.4 FRACTIONATION FOR BIOASSAY TESTING 126
4.4.1 ENVIRONMENTAL ANALYSIS 126
4.4.2 FOOD ANALYSIS 130
4.4.3 DRUG DISCOVERY 131
4.5 MISCELLANEOUS APPROACHES 133
4.6 BIOASSAY TESTING 136
4.6.1 ENVIRONMENTAL ANALYSIS 136
4.6.2 FOOD ANALYSIS 140
4.6.3 DRUG DISCOVERY 140
4.7 IDENTIFICATION AND CONFIRMATION PROCESS 141
4.7.1 INSTRUMENTATION 141
4.7.1.1 GAS CHROMATOGRAPHY-MASS SPECTROMETRY 141
4.7.1.2 LIQUID CHROMATOGRAPHY-MASS SPECTROMETRY 142
4.7.2 DATA ANALYSIS 143
4.7.2.1 DECONVOLUTION 144
4.7.2.2 DATABASE SPECTRUM SEARCHING 145
4.7.2.3 DATABASE SEARCHING ON MOLECULAR FORMULA 145
4.7.2.4 IN SILICO TOOLS 145
4.7.2.5 USE OF PHYSICOCHEMICAL PROPERTIES 146
4.7.2.6 APPLICATIONS IN NONTARGET SCREENING AND EDA 146
4.8 CONCLUSION AND PERSPECTIVES 148
REFERENCES 149
VIII
CONTENTS
5 MS BINDING ASSAYS
165
GEORG HOFNER AND KLAUS 71 WANNER
5.1 INTRODUCTION 165
5.2 MS BINDING ASSAYS - STRATEGY 167
5.2.1 ANALOGIES AND DIFFERENCES COMPARED TO RADIOLIGAND BINDING
ASSAYS 167
5.2.2 FUNDAMENTAL ASSAY CONSIDERATIONS 169
5.2.3 FUNDAMENTAL ANALYTICAL CONSIDERATIONS 170
5.3 APPLICATION OF MS BINDING ASSAYS 171
5.3.1 MS BINDING ASSAYS FOR THE GABA TRANSPORTER GAT1 171
5.3.1.1 GABA TRANSPORTERS 171
5.3.1.2 MS BINDING ASSAYS FOR GAT1 - GENERAL SETUP 172
5.3.1.3 MS BINDING ASSAYS FOR GAT1 - SPEEDING UP CHROMATOGRAPHY 177
5.3.1.4 MS BINDING ASSAYS FOR GAT1 WITH MALDI-MS/MS FOR
QUANTITATION 179
5.3.1.5 LIBRARY SCREENING BY MEANS OF MS BINDING ASSAYS 181
5.3.2 MS BINDING ASSAYS FOR THE SEROTONIN TRANSPORTER 183
5.3.2.1 SEROTONIN TRANSPORTER 183
5.3.2.2 MS BINDING ASSAYS FOR SERT - GENERAL SETUP 184
5.3.3 MS BINDING ASSAYS BASED ON THE QUANTITATION OF THE NONBOUND
MARKER 187
5.3.3.1 COMPETITIVE MS BINDING ASSAYS FOR DOPAMINE D1 AND D2
RECEPTORS 188
5.3.4 OTHER EXAMPLES FOLLOWING THE CONCEPT OF MS BINDING ASSAYS 189
5.4 SUMMARY AND PERSPECTIVES 191
ACKNOWLEDGMENTS 192
REFERENCES 192
6 METABOLIC PROFILING APPROACHES FOR THE IDENTIFICATION OF BIOACTIVE
METABOLITES IN PLANTS
199
EMILY PIPAN AND ANGELA I. CALDERDN
6.1 INTRODUCTION TO PLANT METABOLIC PROFILING 199
6.2 SAMPLE COLLECTION AND PROCESSING 200
6.3 HYPHENATED TECHNIQUES 203
6.3.1 LIQUID CHROMATOGRAPHY-MASS SPECTROMETRY 203
6.3.2 GAS CHROMATOGRAPHY-MASS SPECTROMETRY 206
6.3.3 CAPILLARY ELECTROPHORESIS-MASS SPECTROMETRY 207
6.4 MASS SPECTROMETRY 207
6.4.1 TIME OF FLIGHT 208
6.4.2 QUADRUPOLE MASS FILTER 208
6.4.3 ION TRAPS (ORBITRAP AND LINEAR QUADRUPOLE (LTQ)) 209
6.4.4 FOURIER TRANSFORM MASS SPECTROMETRY 210
6.4.5 ION MOBILITY MASS SPECTROMETRY 210
6.5 MASS SPECTROMETRIC IMAGING 210
6.5.1 MALDI-MS 211
CONTENTS
| IX
6.5.2 SIMS-MS 212
6.5.3 DESI-MS 212
6.5.4 LAESI-MS 213
6.5.5 LDI-MS AND OTHERS FOR IMAGING 213
6.6 DATA ANALYSIS 214
6.6.1 DATA PROCESSING 214
6.6.2 DATA ANALYSIS METHODS 214
6.6.3 DATABASES 215
6.7 FUTURE PERSPECTIVES 216
REFERENCES 216
7 ANTIVENOMICS: A PROTEOMICS TOOL FOR STUDYING THE IMMUNOREACTIVITY
OFANTIVENOMS
227
JUAN J. CALVETE, JOSE MARIA GUTIERREZ, LIBIA SANZ, DAVINIA PLA, AND
BRUNO LOMONTE
7.1 INTRODUCTION 227
7.2 CHALLENGE OF FIGHTING HUMAN ENVENOMING BY SNAKEBITES 227
7.3 TOOLBOX FOR STUDYING THE IMMUNOLOGICAL PROFILE OF ANTIVENOMS 228
7.4 FIRST-GENERATION ANTIVENOMICS 229
7.5 SNAKE VENOMICS 230
7.6 SECOND-GENERATION ANTIVENOMICS 232
7.7 CONCLUDING REMARKS 236
ACKNOWLEDGMENTS 236
REFERENCES 236
PART III DIRECT PRE-AND ON-COLUMN COUPLED TECHNIQUES
241
8 FRONTAL AND ZONAL AFFINITY CHROMATOGRAPHY COUPLED TO MASS
SPECTROMETRY
243
NAGENDRA S. SINGH, ZHENJING JIANG, AND RUIN MOADDEL
8.1 INTRODUCTION 243
8.2 FRONTAL AFFINITY CHROMATOGRAPHY 244
8.3 STAIRCASE METHOD 247
8.4 SIMULTANEOUS FRONTAL ANALYSIS OF A COMPLEX MIXTURE 249
8.5 MULTIPROTEIN STATIONARY PHASE 252
8.6 ZONAL CHROMATOGRAPHY 253
8.7 NONLINEAR CHROMATOGRAPHY 260
ACKNOWLEDGMENTS 265
REFERENCES 265
9 ONLINE AFFINITY ASSESSMENT AND IMMUNOAFFINITY SAMPLE PRETREATMENT
IN CAPILLARY ELECTROPHORESIS-MASS SPECTROMETRY
271
ROB HASELBERG AND GOVERT W. SOMSEN
9.1 INTRODUCTION 27I
9.2 CAPILLARY ELECTROPHORESIS 272
X
CONTENTS
9.3 AFFINITY CAPILLARY ELECTROPHORESIS 276
9.3.1 DYNAMIC EQUILIBRIUM ACE (FAST COMPLEXATION KINETICS) 276
9.3.2 PRE-EQUILIBRIUM ACE (SLOW COMPLEXATION KINETICS) 279
9.3.3 KINETIC ACE (INTERMEDIATE COMPLEXATION KINETICS) 280
9.4 IMMUNOAFFINITY CAPILLARY ELECTROPHORESIS 281
9.5 CAPILLARY ELECTROPHORESIS-MASS SPECTROMETRY 283
9.5.1 GENERAL REQUIREMENTS FOR EFFECTIVE CE-MS COUPLING 283
9.5.2 SPECIFIC REQUIREMENTS FOR ACE-MS AND IA-CE-MS 284
9.6 APPLICATION OF ACE-MS 286
9.7 APPLICATIONS OF IA-CE-MS 292
9.8 CONCLUSIONS 295
REFERENCES 296
10 LABEL-FREE BIOSENSOR AFFINITY ANALYSIS COUPLED TO MASS
SPECTROMETRY
299
DAVID BONNET, DORA MEHN, AND GERARDO R. MARCHESINI
10.1 INTRODUCTION TO MS-COUPLED BIOSENSOR PLATFORMS 299
10.2 STRATEGIES FOR COUPLING LABEL-FREE ANALYSIS WITH MASS
SPECTROMETRY 301
10.2.1 ON-CHIP APPROACHES 301
10.2.1.1 SPR-MALDI-MS 301
10.2.1.2 SPR-LDI-MS 304
10.2.2 OFF-CHIP CONFIGURATIONS 305
10.2.2.1 ESI-MS 305
10.2.2.2 IN PARALLEL APPROACH 305
10.2.3 CHIP CAPTURE AND RELEASE CHROMATOGRAPHY - ELECTROSPRAY-MS 306
10.3 NEW SENSOR AND MS PLATFORMS, OPPORTUNITIES FOR INTEGRATION 307
10.3.1 IMAGING NANOPLASMONICS 307
10.3.2 EVANESCENT WAVE SILICON WAVEGUIDES 308
10.3.3 NEW TRENDS IN MS MATRIX-FREE ION SOURCES 309
10.3.4 TAG-MASS 310
10.3.5 INTEGRATION 310
REFERENCES 310
PART IV DIRECT POST COLUMN COUPLED AFFINITY TECHNIQUES
317
11 HIGH-RESOLUTION SCREENING: POST-COLUMN CONTINUOUS-FLOW
BIOASSAYS
319
DAVID FALCK, WILFRIED M.A. NIESSEN, AND JEROEN KOOL
11.1 INTRODUCTION 319
11.1.1 VARIANTS OF ON-LINE POST-COLUMN ASSAYS USING MASS
SPECTROMETRY 321
11.1.1.1 MASS SPECTROMETRY AS READOUT FOR BIOLOGICAL ASSAYS 323
11.1.1.2 STRUCTURE ELUCIDATION BY MASS SPECTROMETRY 327
11.1.2 TARGETS AND ANALYTES 328
CONTENTS
XI
11.1.2.1 TARGETS 328
11.1.2.2 ANALYTES AND SAMPLES 330
11.2 THE HIGH-RESOLUTION SCREENING PLATFORM 330
11.2.1 SEPARATION 330
11.2.2 FLOW SPLITTING 334
11.2.3 BIOASSAY 336
11.2.4 MS DETECTION 340
11.3 DATA ANALYSIS 342
11.3.1 DIFFERENCES BETWEEN HRS AND HTS 342
11.3.1.1 INFLUENCE OF SHORTER INCUBATION TIMES 342
11.3.1.2 THE ASSAY SIGNAL 344
11.3.1.3 DILUTION CALCULATIONS 346
11.3.1.4 MS STRUCTURE ELUCIDATION 347
11.3.1.5 STRUCTURE-AFFINITY MATCHING 349
11.3.2 VALIDATION 350
11.4 CONCLUSIONS AND PERSPECTIVES 353
11.4.1 THE RELATION OF ON-LINE POST-COLUMN ASSAYS TO OTHER FORMATS 353
11.4.2 TRENDS IN HIGH-RESOLUTION SCREENING 354
11.4.3 CONCLUSIONS 357
REFERENCES 358
12 CONCLUSIONS
365
JEROEN KOOL
INDEX
373
|
any_adam_object | 1 |
author2 | Kool, Jeroen |
author2_role | edt |
author2_variant | j k jk |
author_GND | (DE-588)1068899042 |
author_facet | Kool, Jeroen |
building | Verbundindex |
bvnumber | BV042417332 |
classification_rvk | VG 9800 WC 2600 |
ctrlnum | (OCoLC)908620123 (DE-599)HBZHT018547996 |
dewey-full | 572.36 |
dewey-hundreds | 500 - Natural sciences and mathematics |
dewey-ones | 572 - Biochemistry |
dewey-raw | 572.36 |
dewey-search | 572.36 |
dewey-sort | 3572.36 |
dewey-tens | 570 - Biology |
discipline | Chemie / Pharmazie Biologie |
format | Book |
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genre | (DE-588)4143413-4 Aufsatzsammlung gnd-content |
genre_facet | Aufsatzsammlung |
id | DE-604.BV042417332 |
illustrated | Illustrated |
indexdate | 2024-07-10T01:21:01Z |
institution | BVB |
isbn | 9783527334643 9783527673391 |
language | English |
oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-027852800 |
oclc_num | 908620123 |
open_access_boolean | |
owner | DE-11 DE-703 DE-19 DE-BY-UBM |
owner_facet | DE-11 DE-703 DE-19 DE-BY-UBM |
physical | XXII, 378 S. Ill., graph. Darst. |
publishDate | 2015 |
publishDateSearch | 2015 |
publishDateSort | 2015 |
publisher | Wiley-VCH |
record_format | marc |
spelling | Analyzing biomolecular interactions by mass spectrometry ed. by Jeroen Kool ... Weinheim Wiley-VCH 2015 XXII, 378 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Wechselwirkung (DE-588)4064937-4 gnd rswk-swf Massenspektrometrie (DE-588)4037882-2 gnd rswk-swf Biomolekül (DE-588)4135124-1 gnd rswk-swf Analytische Chemie Massenspektrometrie (DE-588)4143413-4 Aufsatzsammlung gnd-content Biomolekül (DE-588)4135124-1 s Wechselwirkung (DE-588)4064937-4 s Massenspektrometrie (DE-588)4037882-2 s DE-604 Kool, Jeroen (DE-588)1068899042 edt Erscheint auch als Online-Ausgabe, EPUB 978-3-527-67341-4 Erscheint auch als Online-Ausgabe, MOBI 978-3-527-67340-7 Erscheint auch als Online-Ausgabe, PDF 978-3-527-67342-1 DNB Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=027852800&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
spellingShingle | Analyzing biomolecular interactions by mass spectrometry Wechselwirkung (DE-588)4064937-4 gnd Massenspektrometrie (DE-588)4037882-2 gnd Biomolekül (DE-588)4135124-1 gnd |
subject_GND | (DE-588)4064937-4 (DE-588)4037882-2 (DE-588)4135124-1 (DE-588)4143413-4 |
title | Analyzing biomolecular interactions by mass spectrometry |
title_auth | Analyzing biomolecular interactions by mass spectrometry |
title_exact_search | Analyzing biomolecular interactions by mass spectrometry |
title_full | Analyzing biomolecular interactions by mass spectrometry ed. by Jeroen Kool ... |
title_fullStr | Analyzing biomolecular interactions by mass spectrometry ed. by Jeroen Kool ... |
title_full_unstemmed | Analyzing biomolecular interactions by mass spectrometry ed. by Jeroen Kool ... |
title_short | Analyzing biomolecular interactions by mass spectrometry |
title_sort | analyzing biomolecular interactions by mass spectrometry |
topic | Wechselwirkung (DE-588)4064937-4 gnd Massenspektrometrie (DE-588)4037882-2 gnd Biomolekül (DE-588)4135124-1 gnd |
topic_facet | Wechselwirkung Massenspektrometrie Biomolekül Aufsatzsammlung |
url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=027852800&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
work_keys_str_mv | AT kooljeroen analyzingbiomolecularinteractionsbymassspectrometry |