Protein mass spectrometry:
Saved in:
| Format: | Book |
|---|---|
| Language: | English |
| Published: |
Amsterdam [u.a.]
Elsevier
2009
|
| Edition: | 1. ed. |
| Series: | Wilson and Wilson's Comprehensive analytical chemistry
52 |
| Subjects: | |
| Online Access: | Inhaltsverzeichnis |
| Physical Description: | XXXII, 518 S., [6] Bl. Ill., graph. Darst. |
| ISBN: | 9780444530554 044453055X |
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| 245 | 1 | 0 | |a Protein mass spectrometry |c ed. by Julian P. Whitelegge |
| 250 | |a 1. ed. | ||
| 264 | 1 | |a Amsterdam [u.a.] |b Elsevier |c 2009 | |
| 300 | |a XXXII, 518 S., [6] Bl. |b Ill., graph. Darst. | ||
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| 338 | |b nc |2 rdacarrier | ||
| 490 | 1 | |a Wilson and Wilson's Comprehensive analytical chemistry |v 52 | |
| 650 | 4 | |a Mass Spectrometry | |
| 650 | 4 | |a Mass spectrometry | |
| 650 | 4 | |a Proteins |x Spectra | |
| 650 | 4 | |a Proteins |x analysis | |
| 650 | 4 | |a Proteomics | |
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Record in the Search Index
| _version_ | 1804137928809512960 |
|---|---|
| adam_text | Contributors to Volume
52 xiii
Volumes in the Series
xix
Foreword
xxiii
Preface
xxix
Series Editor s Preface
xxxi
1.
An Introduction to the Basic Principles and Concepts of Mass Spectrometry
1
Kym F. Faull,
Alek
N.
Dooley, Frederic Halgand, Lorelei D. Shoemaker,
Andrew J. Norris, Christopher M. Ryan, Arthur Laganowsky, Jodie V. Johnson
and Jonathan E. Katz
1.
Opening Remarks
2
2.
The Instrument
4
3.
Vacuum Systems
4
4.
Definitions
5
5.
Resolution
6
6.
Mass Accuracy
8
7.
Isotopes
9
8.
Reconciling Theoretical and Measured Masses
Π
9.
Charge State Assignment
11
10.
The Need for Chromatography
12
11.
The Myth of Defining Elemental Compositions
13
12.
Desorption lonization: Laser Desorption
14
13.
Spray lonization: Electrospray lonization
16
14.
Mass Analyzers
19
15.
Time-of-Flight Mass Spectrometers
20
16.
Linear Quadrupole Mass Filters
22
17.
Quadrupole Ion Traps
23
18.
Linear Ion Traps
26
19.
Ion Cyclotron Cells and Fourier Transform Mass Spectrometry
27
20.
The Orbitrap
29
21.
Detectors
30
22.
Electron Multipliers
31
23.
Conversion Dynodes or High-Energy Dynodes
32
24.
Quantification
32
25.
Structural Elucidation by Mass Spectrometry
34
VII
viii Contents
26. Gas Phase Ion
Stabilities and Energetics of the Collisionally-Activated Dissociation
Process
35
27.
Collision-Induced Dissociation
36
28.
Electron Capture Dissociation
38
29.
Electron Transfer Dissociation
40
30.
Scan Modes in Tandem Mass Spectrometry
40
31.
Conclusions
43
Acknowledgements
44
References
44
2.
Characterization of Protein Higher Order Structure and Dynamics
with ESI MS
47
Wendell P. Griffith, Anirban Mohimen, Rinat R. Abzalimov and Igor A. Kaltashov
1.
Introduction
47
2.
Charge-State Distributions of Protein Ions in ESI MS and Large-Scale Conformational
Dynamics of Single Polypeptide Chains
48
3.
Conformational Dynamics in Multi-Component Systems: Assembly of Hemoglobin
Tetramers
51
4.
Charge-State Distribution and the Estimation of the Solvent-Exposed Surface Areas
of Proteins
55
5.
Limitations of the Use of Charge-State Distributions for Determining Protein
Conformational Heterogeneity
58
6.
Future Outlook
59
Acknowledgements
60
References
61
3.
Noncovalent Protein Interactions
63
Summer
L
Bernstein and Michael T. Bowers
1.
Introduction
63
2.
Instrumentation and Technical Development
64
3.
Protein Misfolding and Aggregation
67
4.
Ligand-Receptor Interactions
74
5.
Heterogeneous Complexes: TRAP
76
6.
Subunit
Exchange of Transthyretin
78
7.
Future Directions
78
8.
Conclusions
79
Acknowledgments
79
References
79
4.
Protein Analysis with Hydrogen-Deuterium Exchange Mass Spectrometry
83
Jennifer
L
Mitchell and John R.
Engen
1.
Introduction
83
2.
Experimental Protocol
88
3.
Illustrative Examples
96
4.
Conclusions
100
Acknowledgements
101
References
101
Contents
¡Χ
5.
Biochemical Reaction Kinetics Studied by Time-Resolved Electrospray
lonization Mass Spectrometry
103
Lars Konermann, Jingxi Pan and Derek J. Wilson
1.
Introduction
103
2.
Time-Resolved ESI-MS
105
3.
Selected Applications
109
4.
Conclusions and Outlook
120
Acknowledgements
121
References
121
6.
Thermodynamic Analysis of Protein Folding and Ligand Binding
by SUPREX
127
Michael
С
Fitzgerald, Liangjie Tang and Erin D. Hopper
1.
Introduction
127
2.
The SUPREX Protocol
128
3.
Evaluation of Thermodynamic Parameters
131
4.
Quantitative Analysis of Ligand Binding
136
5.
Unique Applications
141
6.
Conclusion
146
References
146
7.
Microsecond Time-Scale Hydroxyl Radical Profiling of Solvent-Accessible
Protein Residues
151
David M. Hambly and Michael L. Gross
1.
Introduction
151
2.
Reagents for Surface Mapping
153
3.
Fast Photochemical Oxidation of Proteins (FPOP)
163
Acknowledgement
172
References
172
8.
Intact Protein Mass Measurements and
Тор
-Down
Mass Spectrometry:
Application to Integral Membrane Proteins
179
Julian P. Whiteiegge
1.
Introduction
179
2.
Intact Protein Mass Measurements
180
3.
lonization
188
References
194
9.
Probing the Structure and Function of Integral Membrane Proteins
by Mass Spectrometry
197
Adam B. Weinglass
1.
Introduction
197
2.
Technical Aspects of Mass Spectrometry of Integral Membrane Proteins
198
3.
MS of Integral Membrane Proteins Provides Insight into Structure, Function and
Mechanism
199
Contents
4.
Conclusions
209
Acknowledgements
209
References
209
10.
Bottom-Up Mass Spectrometry Analysis of Integral Membrane Protein
Structure and Topology
213
Anna E.
Speers
and Christine
С
Wu
1.
Introduction
214
2.
IMP Structure and Characterization
214
3.
Mass Spectrometry Instrumentation
216
4.
General Considerations for Sample Preparation
218
5.
Localizing Glycosylation Sites
220
6.
Limited Proteolysis
222
7.
Residue-Specific Chemical Modification
226
8.
Photoaffinity Labeling of Binding-Site Residues
230
9.
Cross-Linking
233
10.
H/D Exchange
234
11.
Summary and Future Directions
236
Abbreviations
238
Acknowledgement
239
References
239
11.
Covalent Trapping of Protein Interactions in Complex Systems
245
Rasanjala Weerasekera, Tujin Shi and
Gerold Schmitt-Ulms
1.
Introduction
245
2.
Protein Crosslinking
247
3.
Interactome Methods
251
4.
Interface and Topology Mapping
259
5.
Future Directions
266
Abbreviations
268
Acknowledgements
268
References
268
12.
Phosphoproteomics
275
Martin R. Larsen and Phillip J. Robinson
1.
Introduction to Phosphoproteomics
275
2.
Strategies for Enrichment of Phosphorylated Peptides
277
3.
Mass Spectrometric Analysis of Phosphorylated Peptides
282
4.
Quantitative Phosphoproteomics
285
5.
Factors Affecting Phosphoproteomics
290
6.
Conclusion
292
Acknowledgements
293
References
293
13.
Analysis of Protein-Tyrosine Phosphorylation by Mass Spectrometry
297
Guoan Zhang, Chong-Feng Xu and Thomas A.
Neubert
1.
introduction
297
2.
Enrichment
299
Contents xi
3. Qualitative
Analysis
301
4. Quantitative
Analysis
305
5.
Future Directions
309
6.
Conclusions
310
Abbreviations
310
Acknowledgement
311
References
311
14.
Protein Histidine Phosphorylation
315
Xin-Lin Zu,
Paul G. Besant and Paul V. Attwood
1.
Introduction
316
2.
Chemistry of Phosphohistidine
317
3.
Protein Histidine Phosphorylation
318
4.
Detection of Histidine Phosphorylation
331
5.
Future Directions
339
6.
Conclusion
346
Acknowledgements
346
References
346
15.
O-GlcNAc Proteomics: Mass Spectrometric Analysis of O-GlcNAc
Modifications on Proteins
353
Robert J. Chalkley, Lance Wells and Keith Vosseller
1.
Introduction
354
2.
Challenges to Mapping Sites of O-GlcNAc Modification
358
3.
Early Efforts in O-GlcNAc Site-Mapping
360
4.
Enzymatic Tagging of O-GlcNAc to Facilitate Enrichment and Identification of
Modification Sites
361
5.
Chemoenzymatic Approaches in O-GlcNAc Proteomics
362
6.
Beta-Elimination/Michael Addition Strategies for O-GlcNAcylation Site-Mapping
363
7.
Direct Enrichment of Native O-GlcNAc Modified Proteins with WGA Lectin Weak
Affinity Chromatography (LWAC)
365
8.
Ion Trap MSVmS3 for O-GlcNAc Modified
Peptide
Identification
366
9.
Electron Capture Dissociation (ECD) for O-GlcNAc Site-Mapping
366
10.
Interpretation of O-GlcNAcylated
Peptide
Mass Spectrometry
368
11.
Conclusions
369
References
370
16.
Analysis of Deam
¡dation
in Proteins
375
Jason J. Cournoyer and Peter B. O Connor
1.
What is Deamidation?
376
2.
How Does Deamidation Occur?
377
3.
Biological Significance of Deamidation
380
4.
Non-MS Based Methods for Studying Dearnidation
385
5.
Mass Spectrometry Based Methods for Studying Deamidation
390
6.
Quantitation of Deamidation and Its Products
397
7.
Isotopie
Labeling Methods
399
8.
Summary
401
References
402
XII Contents
17.
Mass Spectrometry-Driven Approaches to Quantitative Proteomics and
Beyond
41Ί
Silke
Oeljeklaus, Jon Barbour, Helmut E. Meyer and
Bettina
Warscheid
1.
Why to Use Mass Spectrometry in Quantitative Proteomics
411
2.
MS-Based Approaches to Quantitative Proteomics
413
3.
Applications in Functional Proteomics
426
4.
How to Obtain Meaningful Data in MS-Based Quantitative Proteomics
437
5.
Perspectives
439
References
439
18.
Multiplexed Quantitative Proteomics Using Mass Spectrometry
449
Philip L. Ross, Xunming Chen,
Esteban Toro, Leticia
Britos, Lucy Shapiro and Darryl
Pappin
1.
introduction
449
2.
Isobaric N-Terminal
Peptide
Tagging
452
3.
Mass Spectrometry
457
4.
Quantitative Applications Using Isobaric Tagging
461
References
466
19.
Large-Scale Subcellular Localization of Proteins by Protein Correlation
Profiling
467
Leonard J. Foster
1.
Introduction
467
2.
Peptide
Correlation Profiling
468
3.
Other Quantitative Methods
473
4.
Software for
PCP
474
5.
Hardware Requirements for
PCP
475
6.
The Future for
PCP
and
Organelle
Proteomics
475
Acknowledgements
476
References
476
20.
Metabolic Labeling Approaches for the Relative Quantification
of Proteins
479
Edward L. Huttlin, Adrian D. Hegeman and Michael R. Sussman
1.
Introduction
480
2.
Selected Metabolic Labeling Strategies
483
3.
Practical Experimental Considerations
487
4.
Comparison of Full versus Partial Labeling
498
5.
Future Directions
507
References
509
Subject Index
515
|
| adam_txt |
Contributors to Volume
52 xiii
Volumes in the Series
xix
Foreword
xxiii
Preface
xxix
Series Editor's Preface
xxxi
1.
An Introduction to the Basic Principles and Concepts of Mass Spectrometry
1
Kym F. Faull,
Alek
N.
Dooley, Frederic Halgand, Lorelei D. Shoemaker,
Andrew J. Norris, Christopher M. Ryan, Arthur Laganowsky, Jodie V. Johnson
and Jonathan E. Katz
1.
Opening Remarks
2
2.
The Instrument
4
3.
Vacuum Systems
4
4.
Definitions
5
5.
Resolution
6
6.
Mass Accuracy
8
7.
Isotopes
9
8.
Reconciling Theoretical and Measured Masses
Π
9.
Charge State Assignment
11
10.
The Need for Chromatography
12
11.
The Myth of Defining Elemental Compositions
13
12.
Desorption lonization: Laser Desorption
14
13.
Spray lonization: Electrospray lonization
16
14.
Mass Analyzers
19
15.
Time-of-Flight Mass Spectrometers
20
16.
Linear Quadrupole Mass Filters
22
17.
Quadrupole Ion Traps
23
18.
Linear Ion Traps
26
19.
Ion Cyclotron Cells and Fourier Transform Mass Spectrometry
27
20.
The Orbitrap
29
21.
Detectors
30
22.
Electron Multipliers
31
23.
Conversion Dynodes or High-Energy Dynodes
32
24.
Quantification
32
25.
Structural Elucidation by Mass Spectrometry
34
VII
viii Contents
26. Gas Phase Ion
Stabilities and Energetics of the Collisionally-Activated Dissociation
Process
35
27.
Collision-Induced Dissociation
36
28.
Electron Capture Dissociation
38
29.
Electron Transfer Dissociation
40
30.
Scan Modes in Tandem Mass Spectrometry
40
31.
Conclusions
43
Acknowledgements
44
References
44
2.
Characterization of Protein Higher Order Structure and Dynamics
with ESI MS
47
Wendell P. Griffith, Anirban Mohimen, Rinat R. Abzalimov and Igor A. Kaltashov
1.
Introduction
47
2.
Charge-State Distributions of Protein Ions in ESI MS and Large-Scale Conformational
Dynamics of Single Polypeptide Chains
48
3.
Conformational Dynamics in Multi-Component Systems: Assembly of Hemoglobin
Tetramers
51
4.
Charge-State Distribution and the Estimation of the Solvent-Exposed Surface Areas
of Proteins
55
5.
Limitations of the Use of Charge-State Distributions for Determining Protein
Conformational Heterogeneity
58
6.
Future Outlook
59
Acknowledgements
60
References
61
3.
Noncovalent Protein Interactions
63
Summer
L
Bernstein and Michael T. Bowers
1.
Introduction
63
2.
Instrumentation and Technical Development
64
3.
Protein Misfolding and Aggregation
67
4.
Ligand-Receptor Interactions
74
5.
Heterogeneous Complexes: TRAP
76
6.
Subunit
Exchange of Transthyretin
78
7.
Future Directions
78
8.
Conclusions
79
Acknowledgments
79
References
79
4.
Protein Analysis with Hydrogen-Deuterium Exchange Mass Spectrometry
83
Jennifer
L
Mitchell and John R.
Engen
1.
Introduction
83
2.
Experimental Protocol
88
3.
Illustrative Examples
96
4.
Conclusions
100
Acknowledgements
101
References
101
Contents
¡Χ
5.
Biochemical Reaction Kinetics Studied by Time-Resolved Electrospray
lonization Mass Spectrometry
103
Lars Konermann, Jingxi Pan and Derek J. Wilson
1.
Introduction
103
2.
Time-Resolved ESI-MS
105
3.
Selected Applications
109
4.
Conclusions and Outlook
120
Acknowledgements
121
References
121
6.
Thermodynamic Analysis of Protein Folding and Ligand Binding
by SUPREX
127
Michael
С
Fitzgerald, Liangjie Tang and Erin D. Hopper
1.
Introduction
127
2.
The SUPREX Protocol
128
3.
Evaluation of Thermodynamic Parameters
131
4.
Quantitative Analysis of Ligand Binding
136
5.
Unique Applications
141
6.
Conclusion
146
References
146
7.
Microsecond Time-Scale Hydroxyl Radical Profiling of Solvent-Accessible
Protein Residues
151
David M. Hambly and Michael L. Gross
1.
Introduction
151
2.
Reagents for Surface Mapping
153
3.
Fast Photochemical Oxidation of Proteins (FPOP)
163
Acknowledgement
172
References
172
8.
Intact Protein Mass Measurements and
Тор
-Down
Mass Spectrometry:
Application to Integral Membrane Proteins
179
Julian P. Whiteiegge
1.
Introduction
179
2.
Intact Protein Mass Measurements
180
3.
lonization
188
References
194
9.
Probing the Structure and Function of Integral Membrane Proteins
by Mass Spectrometry
197
Adam B. Weinglass
1.
Introduction
197
2.
Technical Aspects of Mass Spectrometry of Integral Membrane Proteins
198
3.
MS of Integral Membrane Proteins Provides Insight into Structure, Function and
Mechanism
199
Contents
4.
Conclusions
209
Acknowledgements
209
References
209
10.
Bottom-Up Mass Spectrometry Analysis of Integral Membrane Protein
Structure and Topology
213
Anna E.
Speers
and Christine
С
Wu
1.
Introduction
214
2.
IMP Structure and Characterization
214
3.
Mass Spectrometry Instrumentation
216
4.
General Considerations for Sample Preparation
218
5.
Localizing Glycosylation Sites
220
6.
Limited Proteolysis
222
7.
Residue-Specific Chemical Modification
226
8.
Photoaffinity Labeling of Binding-Site Residues
230
9.
Cross-Linking
233
10.
H/D Exchange
234
11.
Summary and Future Directions
236
Abbreviations
238
Acknowledgement
239
References
239
11.
Covalent Trapping of Protein Interactions in Complex Systems
245
Rasanjala Weerasekera, Tujin Shi and
Gerold Schmitt-Ulms
1.
Introduction
245
2.
Protein Crosslinking
247
3.
Interactome Methods
251
4.
Interface and Topology Mapping
259
5.
Future Directions
266
Abbreviations
268
Acknowledgements
268
References
268
12.
Phosphoproteomics
275
Martin R. Larsen and Phillip J. Robinson
1.
Introduction to Phosphoproteomics
275
2.
Strategies for Enrichment of Phosphorylated Peptides
277
3.
Mass Spectrometric Analysis of Phosphorylated Peptides
282
4.
Quantitative Phosphoproteomics
285
5.
Factors Affecting Phosphoproteomics
290
6.
Conclusion
292
Acknowledgements
293
References
293
13.
Analysis of Protein-Tyrosine Phosphorylation by Mass Spectrometry
297
Guoan Zhang, Chong-Feng Xu and Thomas A.
Neubert
1.
introduction
297
2.
Enrichment
299
Contents xi
3. Qualitative
Analysis
301
4. Quantitative
Analysis
305
5.
Future Directions
309
6.
Conclusions
310
Abbreviations
310
Acknowledgement
311
References
311
14.
Protein Histidine Phosphorylation
315
Xin-Lin Zu,
Paul G. Besant and Paul V. Attwood
1.
Introduction
316
2.
Chemistry of Phosphohistidine
317
3.
Protein Histidine Phosphorylation
318
4.
Detection of Histidine Phosphorylation
331
5.
Future Directions
339
6.
Conclusion
346
Acknowledgements
346
References
346
15.
O-GlcNAc Proteomics: Mass Spectrometric Analysis of O-GlcNAc
Modifications on Proteins
353
Robert J. Chalkley, Lance Wells and Keith Vosseller
1.
Introduction
354
2.
Challenges to Mapping Sites of O-GlcNAc Modification
358
3.
Early Efforts in O-GlcNAc Site-Mapping
360
4.
Enzymatic Tagging of O-GlcNAc to Facilitate Enrichment and Identification of
Modification Sites
361
5.
Chemoenzymatic Approaches in O-GlcNAc Proteomics
362
6.
Beta-Elimination/Michael Addition Strategies for O-GlcNAcylation Site-Mapping
363
7.
Direct Enrichment of Native O-GlcNAc Modified Proteins with WGA Lectin Weak
Affinity Chromatography (LWAC)
365
8.
Ion Trap MSVmS3 for O-GlcNAc Modified
Peptide
Identification
366
9.
Electron Capture Dissociation (ECD) for O-GlcNAc Site-Mapping
366
10.
Interpretation of O-GlcNAcylated
Peptide
Mass Spectrometry
368
11.
Conclusions
369
References
370
16.
Analysis of Deam
¡dation
in Proteins
375
Jason J. Cournoyer and Peter B. O'Connor
1.
What is Deamidation?
376
2.
How Does Deamidation Occur?
377
3.
Biological Significance of Deamidation
380
4.
Non-MS Based Methods for Studying Dearnidation
385
5.
Mass Spectrometry Based Methods for Studying Deamidation
390
6.
Quantitation of Deamidation and Its Products
397
7.
Isotopie
Labeling Methods
399
8.
Summary
401
References
402
XII Contents
17.
Mass Spectrometry-Driven Approaches to Quantitative Proteomics and
Beyond
41Ί
Silke
Oeljeklaus, Jon Barbour, Helmut E. Meyer and
Bettina
Warscheid
1.
Why to Use Mass Spectrometry in Quantitative Proteomics
411
2.
MS-Based Approaches to Quantitative Proteomics
413
3.
Applications in Functional Proteomics
426
4.
How to Obtain Meaningful Data in MS-Based Quantitative Proteomics
437
5.
Perspectives
439
References
439
18.
Multiplexed Quantitative Proteomics Using Mass Spectrometry
449
Philip L. Ross, Xunming Chen,
Esteban Toro, Leticia
Britos, Lucy Shapiro and Darryl
Pappin
1.
introduction
449
2.
Isobaric N-Terminal
Peptide
Tagging
452
3.
Mass Spectrometry
457
4.
Quantitative Applications Using Isobaric Tagging
461
References
466
19.
Large-Scale Subcellular Localization of Proteins by Protein Correlation
Profiling
467
Leonard J. Foster
1.
Introduction
467
2.
Peptide
Correlation Profiling
468
3.
Other Quantitative Methods
473
4.
Software for
PCP
474
5.
Hardware Requirements for
PCP
475
6.
The Future for
PCP
and
Organelle
Proteomics
475
Acknowledgements
476
References
476
20.
Metabolic Labeling Approaches for the Relative Quantification
of Proteins
479
Edward L. Huttlin, Adrian D. Hegeman and Michael R. Sussman
1.
Introduction
480
2.
Selected Metabolic Labeling Strategies
483
3.
Practical Experimental Considerations
487
4.
Comparison of Full versus Partial Labeling
498
5.
Future Directions
507
References
509
Subject Index
515 |
| any_adam_object | 1 |
| any_adam_object_boolean | 1 |
| building | Verbundindex |
| bvnumber | BV035008898 |
| callnumber-first | Q - Science |
| callnumber-label | QD75 |
| callnumber-raw | QD75 |
| callnumber-search | QD75 |
| callnumber-sort | QD 275 |
| callnumber-subject | QD - Chemistry |
| classification_rvk | WC 4170 |
| ctrlnum | (OCoLC)260202125 (DE-599)BVBBV035008898 |
| dewey-full | 572.633 |
| dewey-hundreds | 500 - Natural sciences and mathematics |
| dewey-ones | 572 - Biochemistry |
| dewey-raw | 572.633 |
| dewey-search | 572.633 |
| dewey-sort | 3572.633 |
| dewey-tens | 570 - Biology |
| discipline | Biologie |
| discipline_str_mv | Biologie |
| edition | 1. ed. |
| format | Book |
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| genre | (DE-588)4143413-4 Aufsatzsammlung gnd-content |
| genre_facet | Aufsatzsammlung |
| id | DE-604.BV035008898 |
| illustrated | Illustrated |
| index_date | 2024-07-02T21:43:10Z |
| indexdate | 2024-07-09T21:20:05Z |
| institution | BVB |
| isbn | 9780444530554 044453055X |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-016678174 |
| oclc_num | 260202125 |
| open_access_boolean | |
| owner | DE-355 DE-BY-UBR DE-703 |
| owner_facet | DE-355 DE-BY-UBR DE-703 |
| physical | XXXII, 518 S., [6] Bl. Ill., graph. Darst. |
| publishDate | 2009 |
| publishDateSearch | 2009 |
| publishDateSort | 2009 |
| publisher | Elsevier |
| record_format | marc |
| series | Wilson and Wilson's Comprehensive analytical chemistry |
| series2 | Wilson and Wilson's Comprehensive analytical chemistry |
| spelling | Protein mass spectrometry ed. by Julian P. Whitelegge 1. ed. Amsterdam [u.a.] Elsevier 2009 XXXII, 518 S., [6] Bl. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Wilson and Wilson's Comprehensive analytical chemistry 52 Mass Spectrometry Mass spectrometry Proteins Spectra Proteins analysis Proteomics Proteine (DE-588)4076388-2 gnd rswk-swf Massenspektrometrie (DE-588)4037882-2 gnd rswk-swf (DE-588)4143413-4 Aufsatzsammlung gnd-content Proteine (DE-588)4076388-2 s Massenspektrometrie (DE-588)4037882-2 s b DE-604 Whitelegge, Julian P. Sonstige oth Wilson and Wilson's Comprehensive analytical chemistry 52 (DE-604)BV000900805 52 Digitalisierung UB Regensburg application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=016678174&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Protein mass spectrometry Wilson and Wilson's Comprehensive analytical chemistry Mass Spectrometry Mass spectrometry Proteins Spectra Proteins analysis Proteomics Proteine (DE-588)4076388-2 gnd Massenspektrometrie (DE-588)4037882-2 gnd |
| subject_GND | (DE-588)4076388-2 (DE-588)4037882-2 (DE-588)4143413-4 |
| title | Protein mass spectrometry |
| title_auth | Protein mass spectrometry |
| title_exact_search | Protein mass spectrometry |
| title_exact_search_txtP | Protein mass spectrometry |
| title_full | Protein mass spectrometry ed. by Julian P. Whitelegge |
| title_fullStr | Protein mass spectrometry ed. by Julian P. Whitelegge |
| title_full_unstemmed | Protein mass spectrometry ed. by Julian P. Whitelegge |
| title_short | Protein mass spectrometry |
| title_sort | protein mass spectrometry |
| topic | Mass Spectrometry Mass spectrometry Proteins Spectra Proteins analysis Proteomics Proteine (DE-588)4076388-2 gnd Massenspektrometrie (DE-588)4037882-2 gnd |
| topic_facet | Mass Spectrometry Mass spectrometry Proteins Spectra Proteins analysis Proteomics Proteine Massenspektrometrie Aufsatzsammlung |
| url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=016678174&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
| volume_link | (DE-604)BV000900805 |
| work_keys_str_mv | AT whiteleggejulianp proteinmassspectrometry |