Proteome research: mass spectrometry:
Gespeichert in:
Format: | Buch |
---|---|
Sprache: | English |
Veröffentlicht: |
Berlin [u.a.]
Springer
2001
|
Schriftenreihe: | Principles and practice
|
Schlagworte: | |
Online-Zugang: | Inhaltsverzeichnis |
Beschreibung: | XXI, 274 S. graph. Darst. |
ISBN: | 3540672559 3540672567 |
Internformat
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245 | 1 | 0 | |a Proteome research: mass spectrometry |c Peter James [ed.] |
264 | 1 | |a Berlin [u.a.] |b Springer |c 2001 | |
300 | |a XXI, 274 S. |b graph. Darst. | ||
336 | |b txt |2 rdacontent | ||
337 | |b n |2 rdamedia | ||
338 | |b nc |2 rdacarrier | ||
490 | 0 | |a Principles and practice | |
650 | 7 | |a Espectrometria de massas |2 larpcal | |
650 | 7 | |a Proteínas |2 larpcal | |
650 | 4 | |a Protéines - Analyse | |
650 | 7 | |a Protéines - Analyse |2 ram | |
650 | 4 | |a Spectrométrie de masse | |
650 | 7 | |a Spectroscopie de masse |2 ram | |
650 | 4 | |a Mass Spectrometry | |
650 | 4 | |a Mass spectrometry | |
650 | 4 | |a Proteins |x Analysis | |
650 | 4 | |a Proteome |x analysis | |
650 | 0 | 7 | |a Massenspektrometrie |0 (DE-588)4037882-2 |2 gnd |9 rswk-swf |
650 | 0 | 7 | |a Proteomanalyse |0 (DE-588)4596545-6 |2 gnd |9 rswk-swf |
689 | 0 | 0 | |a Proteomanalyse |0 (DE-588)4596545-6 |D s |
689 | 0 | 1 | |a Massenspektrometrie |0 (DE-588)4037882-2 |D s |
689 | 0 | |5 DE-604 | |
700 | 1 | |a James, Peter |e Sonstige |4 oth | |
856 | 4 | 2 | |m DNB Datenaustausch |q application/pdf |u http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=009074200&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |3 Inhaltsverzeichnis |
943 | 1 | |a oai:aleph.bib-bvb.de:BVB01-009074200 |
Datensatz im Suchindex
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adam_text |
CONTENTS
1
MASS
SPECTROMETRY
AND
THE
PROTEOME
P
ETER
J
AMES
1.1
THE
INDUSTRIALISATION
OF
BIOLOGY
.
1
1.2
THE
PROTEOME
.
2
1.2.1
MRNA
AND
PROTEIN
.
2
1.2.2
VISUALISING
THE
PROTEOME:
TWO-DIMENSIONAL
GEL
ELECTROPHORESIS
.
2
1.3
MASS
SPECTROMETRY
AND
PROTEOMICS
.
3
1.3.1
GENERAL
REQUIREMENTS
.
3
1.3.2
SENSITIVITY
.
3
1.3.3
SAMPLE
HANDLING
.
5
1.3.4
HIGH-THROUGHPUT
PROTEIN
IDENTIFICATION
.
5
1.3.5
QUANTIFICATION
.
5
1.3.6
POST-TRANSLATIONAL
MODIFICATIONS
.
6
1.4
AIMS
OF
THE
BOOK
.
6
REFERENCES
.
8
2
BASICS
OF
TRIPLE-STAGE
QUADRUPOLE/ION-TRAP
MASS
SPECTROMETRY:
PRECURSOR,
PRODUCT
AND
NEUTRAL-LOSS
SCANNING.
ELECTROSPRAY
IONISATION
AND
NANOSPRAY
IONISATION
D
AVID
A
RNOTT
2.1
INTRODUCTION
.
11
2.2
FUNDAMENTAL
PRINCIPLES
.
12
2.2.1
MASS
ANALYSIS
.
12
2.2.2
COLLISION-INDUCED
DISSOCIATION
.
15
2.2.3
ELECTROSPRAY
IONISATION
.
16
2.3
TRIPLE-QUADRUPOLE
MS
.
17
2.3.1
INSTRUMENT
OVERVIEW
.
17
2.3.2
PRODUCT-ION
SCANS
.
18
2.3.3
PRECURSOR-ION
SCANS
.
21
2.3.4
NEUTRAL-LOSS
SCANS
.
23
2.4
ION-TRAP
MS
.
24
2.4.1
INSTRUMENT
OVERVIEW
.
24
2.4.2
FULL
MASS-RANGE
AND
HIGH-RESOLUTION
SCANS
.
25
2.4.3
PRODUCT-ION
SCANS
.
26
X
CONTENTS
2.4.4
MS'
1
.
27
2.5
VIRTUES
OF
TSQ
AND
ION-TRAP
INSTRUMENTS
.
28
REFERENCES
.
29
3
THE
BASICS
OF
MATRIX-ASSISTED
LASER
DESORPTION,
IONISATION
TIME-OF-FLIGHT
MASS
SPECTROMETRY
AND
POST-SOURCE
DECAY
ANALYSIS
B
ERNHARD
S
PENGLER
3.1
INTRODUCTION
.
33
3.2
PRINCIPLES
OF
MALDI
.
35
3.2.1
ION
FORMATION
BY
MALDI
.
36
3.2.2
SAMPLE
PREPARATION
.
39
3.2.3
INSTRUMENTATION
.
40
3.2.3.1
ION
SOURCE
.
40
3.2.3.2
MASS
ANALYSER
.
40
3.2.3.3
ION
DETECTOR
.
41
3.2.3.4
DELAYED
ION
EXTRACTION
.
42
3.3
PRINCIPLES
OF
MALDI-PSD
MASS
ANALYSIS
.
43
3.3.1
MECHANISMS
FOR
ION
ACTIVATION
.
43
3.3.2
INSTRUMENTATION
FOR
MALDI-PSD
.
46
3.3.2.1
ION
SOURCE
.
46
3.3.2.2
ION
GATE
.
47
3.3.2.3
MASS
ANALYSER
.
47
3.3.3
INTERPRETATION
OF
PSD
MASS
SPECTRA
.
48
3.3.4
IMPROVING
SPECTRAL
INFORMATION
.
50
3.4
CONCLUSION
.
50
REFERENCES
.
51
4
DATA-CONTROLLED
MICRO-SCALE
LIQUID
CHROMATOGRAPHY
-
TANDEM
MASS
SPECTROMETRY
OF
PEPTIDES
AND
PROTEINS:
STRATEGIES
FOR
IMPROVED
SENSITIVITY,
EFFICIENCY
AND
EFFECTIVENESS
D
OUGLAS
C.
S
TAHL
AND
T
ERRY
D.
L
EE
4.1
INTRODUCTION
.
55
4.2
THE
ES
PROCESS
.
56
4.3
MICRO-ES
EMITTER
DESIGN
.
57
4.3.1
EMITTER
CONSTRUCTION
.
57
4.4
HIGH-VOLTAGE
CONNECTION
.
58
4.5
CAPILLARY
COLUMNS
.
60
4.5.1
COLUMN
CONSTRUCTION
.
60
4.6
GRADIENT-DELIVERY
SYSTEMS
.
62
4.6.1
FLOW
SPLITTING
.
62
4.7
SAMPLE
LOADING
.
63
4.8
VARIABLE-FLOW
CHROMATOGRAPHY
AND
PEAK
PARKING
.
65
4.8.1
VARIABLE-FLOW
CHROMATOGRAPHY
.
65
CONTENTS
XI
4.8.2
PEAK
PARKING
.
67
4.8.3
AUTOMATION
.
68
4.9
DATA-CONTROLLED
ANALYSIS
.
69
4.9.1
ANALYSING
PEPTIDE
MODIFICATIONS
.
70
4.9.2
SOFTWARE
INTEGRATION
.
71
4.10
CONCLUSION
.
72
ACKNOWLEDGEMENTS
.
72
REFERENCES
.
73
5
SOLID-PHASE
EXTRACTION-CAPILLARY
ZONE
ELECTROPHORESIS-MASS
SPECTROMETRY
ANALYSIS
OF
LOW-ABUNDANCE
PROTEINS
D
ANIEL
F
IGEYS
AND
R
UEDI
A
EBERSOLD
5.1
INTRODUCTION
.
75
5.2
FABRICATION
OF
THE
SPE-CZE
SYSTEM
.
76
5.2.1
GENERAL
DESIGN
.
76
5.3
PROCEDURE
FOR
THE
SPE-CZE-MS/MS
EXPERIMENT
.
79
5.3.1
PRE-SATURATION
.
79
5.3.2
SAMPLE
LOADING
.
79
5.3.3
SAMPLE
ELUTION
AND
SEPARATION
.
79
5.3.3.1
SOLID-PHASE
EXTRACTION-CAPILLARY
ZONE
ELECTROPHORESIS
.
79
5.3.3.2
SPE
AND
TRANSIENT
ISOTACHOPHORESIS
.
81
5.3.4
SAMPLE
OVERLOADING
.
81
5.3.5
MS
AND
DATA
PROCESSING
.
82
5.4
SYSTEM
OPTIMISATION
AND
VARIATIONS
OF
THE
BASIC
METHOD
.
84
5.4.1
EXTRACTION
MATERIALS
FOR
THE
SPE
CARTRIDGE
.
84
5.4.2
SURFACE
CHEMISTRY
FOR
CAPILLARY
TUBING
.
87
5.4.3
SEPARATION
.
88
5.4.4
PEAK-PARKING
MODE
.
92
5.4.4.1
INSTRUMENT-CONTROL
PROCEDURES
.
93
5.4.4.2
ANALYSIS
OF
PROTEIN
WITH
THE
PEAK-PARKING
MODE
.
94
5.5
CONCLUSION
.
94
APPENDIX:
PROTOCOLS
.
96
1
SPE-CZE
(QUICK
GUIDE)
.
96
2
SPE-CZE-TRANSIENT
ISOTACHOPHORESIS
(QUICK
GUIDE)
.
96
3
COATING
OF
CAPILLARIES:
GENERAL
COMMENTS
.
96
4
Y-METHACRYLOPROPYL
TRIMETHOXYSILANE
COATING
.
97
5
MAPTAC
COATING
WITH
SI-O-SI
ATTACHMENTS
.
97
6
MAPTAC
COATING
WITH
SI-C
ATTACHMENTS
.
98
REFERENCES
.
98
6
PROTEIN
IDENTIFICATION
BY
PEPTIDE-MASS
FINGERPRINTING
P
AOLA
D
AINESE
AND
P
ETER
J
AMES
6.1
INTRODUCTION
.
103
6.1.1
PROTEIN
IDENTIFICATION
USING
PROTEOLYTIC
MASSES
.
103
XII
CONTENTS
6.2
DATABASE
SEARCHING
AND
SCORING
SCHEMES
.
105
6.3
STRENGTHS
AND
LIMITATIONS
OF
THE
METHOD
.
106
6.3.1
MASS
ACCURACY
AND
AUTOMATION
.
107
6.3.2
MULTIPLE
PROTEINS
IN
A
SAMPLE
.
108
6.3.3
PROTEIN
MODIFICATIONS
.
109
6.3.4
REMOVING
POST-TRANSLATIONAL
MODIFICATIONS
FOR
SEARCHING
.
110
6.3.5
RELATIVE
EFFECTIVENESS
OF
DIFFERENT
DIGESTERS
.
110
6.3.6
PRACTICAL
LIMITATIONS
OF
DIGESTION
.
ILL
6.4
EXTENSIONS
OF
THE
METHOD
.
112
6.4.1
ORTHOGONAL
DATA
.
112
6.4.2
CROSS-SPECIES
IDENTIFICATION
.
113
6.4.3
CHEMICAL
MODIFICATIONS
.
114
6.4.4
ITERATIVE
SEARCHING
.
114
6.5
SEQUENCE
TAGGING
.
116
6.5.1
RAGGED
TERMINI
.
116
6.5.2
ENZYMATIC-LADDER
SEQUENCING
.
117
6.5.3
CHEMICAL-LADDER
SEQUENCING
.
117
6.6
CONCLUSION
.
119
REFERENCES
.
121
7
PROTEIN
IDENTIFICATION
BY
SEQUEST
D
AVID
L.
T
ABB
,
J
IMMY
K.
E
NG
,
AND
J
OHN
R.
Y
ATES
III
7.1
INTRODUCTION
TO
SEQUEST
AND
PROTEIN
IDENTIFICATION
.
125
7.1.1
PEPTIDE
MS
AND
THE
COLLISION-INDUCED
DISSOCIATION
PROCESS
.
126
7.1.2
INTERPRETATION
OF
TANDEM
MASS
SPECTRA
.
126
7.2
DESCRIPTION
OF
THE
ALGORITHM
.
128
7.2.1
SPECTRUM
PRE-PROCESSING
.
128
7.2.2
SELECTION
OF
CANDIDATE
SEQUENCES
FROM
A
DATABASE
.
128
7.2.3
PREPARATION
FOR
SPECTRUM
COMPARISON
.
129
7.2.4
CROSS-CORRELATION
.
129
7.3
INTERPRETATION
OF
SEQUEST
SCORES
.
130
7.3.1
INTERPRETATION
OF
A
SPECTRUM
'
S
SEQUEST
RESULTS
.
130
7.3.2
INTERPRETATION
OF
AN
ENTIRE
LC/MS/MS
ANALYSIS
.
132
7.3.3
INTERPRETATION
OF
MULTIPLE
LC/MS/MS
ANALYSES
.
132
7.4
EXTENSIONS
OF
FUNCTIONALITY
.
135
7.4.1
COMPREHENSIVE
MODIFICATION
ANALYSIS
.
135
7.4.2
PERFORMANCE
IMPROVEMENTS
.
136
7.4.2.1
CONTAMINANT
FILTERING
.
136
7.4.2.2
SPECTRAL-QUALITY
FILTERING
.
137
7.4.2.3
HIGH-PERFORMANCE
COMPUTING
USING
A
PARALLEL
CLUSTER
.
138
7.5
APPLICATIONS
OF
SEQUEST
.
140
7.5.1
COMPLEX-MIXTURE
ANALYSIS
.
140
7.5.2
SUBTRACTIVE
ANALYSIS
.
140
CONTENTS
XIII
7.5.3
CASE
STUDIES
FROM
IN-GEL
DIGEST
ANALYSIS
.
141
7.6
CONCLUSION
.
142
REFERENCES
.
142
8
INTERPRETING
PEPTIDE
TANDEM
MASS-SPECTROMETRY
FRAGMENTATION
SPECTRA
W
ERNER
S
TAUDENMANN
AND
P
ETER
J
AMES
8.1
INTRODUCTION
TO
PEPTIDE
TANDEM
MASS
SPECTROMETRY
.
143
8.1.1
PEPTIDE
IONISATION
.
143
8.1.2
PEPTIDE
FRAGMENTATION
.
144
8.1.3
MECHANISM
OF
AMIDE-BOND
CLEAVAGE
.
146
8.1.4
SEQUENCE-DEPENDANT
FRAGMENTATION
TYPES
.
148
8.1.4.1
IMMONIUM
IONS
.
148
8.1.4.2
INTERNAL
CLEAVAGE
.
148
8.1.4.3
PREFERENTIAL
CLEAVAGE
C-TERMINAL
TO
ASP .
149
8.1.4.4
LOW-ENERGY
PRODUCTION
OF
A-TYPE
IONS
.
150
8.1.4.5
LOSS
OF
C-TERMINAL
AMINO
ACIDS
.
150
8.1.4.6
AMINO
ACID-SPECIFIC
MASS
LOSSES
.
150
8.2
MANUAL
INTERPRETATION
OF
PEPTIDE
MS/MS
SPECTRA
.
152
8.2.1
GENERAL
CONSIDERATIONS
.
152
8.2.2
AN
APPROACH
TO
MANUAL
INTERPRETATION
.
153
8.2.2.1
INTERPRETATION
CHECKLIST
.
153
8.2.3
INTERPRETING
A
SIMPLE
MS/MS
SPECTRUM
OF
A
TRYPTIC
PEPTIDE
.
155
8.2.4
THE
IMPORTANCE
OF
CHARGE
LOCATION
.
157
8.3
AIDS
TO
SPECTRAL
INTERPRETATION
AND
THE
AVOIDANCE
OF
PITFALLS
.
159
8.3.1
DISTINGUISHING
BETWEEN
RESIDUES
WITH
CLOSELY
RELATED
MASSES
.
159
8.3.2
ISOTOPIC
LABELLING
OF
ION
SERIES
.
160
8.3.3
A
CAUTIONARY
TALE
.
161
8.4
MANUAL
INTERPRETATION
AND
DATABASE
SEARCHING
.
161
8.5
CONCLUSION
.
164
ACKNOWLEDGEMENTS
.
164
REFERENCES
.
165
9
AUTOMATED
INTERPRETATION
OF
PEPTIDE
TANDEM
MASS
SPECTRA
AND
HOMOLOGY
SEARCHING
R
ICHARD
S.
J
OHNSON
9.1
DATABASE-SEARCHING
PROGRAMS
FOR
INEXACT
PEPTIDE
MATCHES
.
167
9.2
ALGORITHMS
FOR
AUTOMATED
INTERPRETATION
OF
PEPTIDE
TANDEM
MASS
SPECTRA
.
168
9.2.1
BRUTE-FORCE
METHOD
.
168
9.2.2
SUB-SEQUENCING
APPROACH
.
168
XIV
CONTENTS
9.2.3
GRAPHICAL
DISPLAY
TO
ASSIST
MANUAL
INTERPRETATION
.
169
9.2.4
GRAPH-THEORY
APPROACH
.
169
9.3
AMBIGUITIES ASSOCIATED
WITH
SEQUENCE
DETERMINATIONS
FROM
MS/MS
SPECTRA
.
172
9.3.1
ISOMERIC
AND
ISOBARIC
AMINO
ACID
RESIDUES
.
172
9.3.2
AMINO
ACID
RESIDUES
THAT
ARE
ISOBARIC
WITH
DIPEPTIDE
RESIDUES
.
173
9.3.3
MISSING
FRAGMENTATION
.
173
9.3.4
UNKNOWN
AND
UNUSUAL
FRAGMENTATION
REACTIONS
AND
ARTEFACTS
.
173
9.3.5
INHERENT
AMBIGUITY
DUE
TO
SPECTRUM
COMPLEXITY
.
174
9.4
USING
AMBIGUOUS
PEPTIDE
SEQUENCES
DERIVED
FROM
TANDEM
MASS
SPECTRA
.
174
9.4.1
AUTOMATED
VALIDATION
OF
DATABASE
MATCHES
.
174
9.4.2
USE
OF
A
HOMOLOGY-BASED
SEARCH
PROGRAM
THAT
HAS
BEEN
MODIFIED
TO
HANDLE
SEQUENCE
AMBIGUITIES
.
176
9.4.2.1
IDENTIFYING
PEPTIDES
DERIVED
FROM
NON-CONSENSUS
CLEAVAGES
OR
FROM
CHEMICAL
ARTEFACTS
.
176
9.4.2.2
DATABASE
SEQUENCE
ERRORS
AND
HOMOLOGOUS
PROTEINS
.
178
9.5
RESOLVING
SEQUENCE
AMBIGUITIES
.
178
9.5.1
HIGHER
MASS-ACCURACY
MEASUREMENTS
OF
FRAGMENT
IONS
AND
PEPTIDE
MOLECULAR
WEIGHTS
.
179
9.5.2
DEUTERIUM
INCORPORATION
.
179
9.5.3
CHEMICAL
MODIFICATIONS
.
180
9.5.4
C-TERMINAL
,8
O
LABELLING
.
180
9.5.5
MULTIPLE
STAGES
OF
MS/MS
.
180
9.5.6
COMPARISON
WITH
SYNTHETIC
PEPTIDES
.
182
9.6
CONCLUSION
.
182
ACKNOWLEDGEMENTS
.
182
REFERENCES
.
183
10
SPECIFIC
DETECTION
AND
ANALYSIS
OF
PHOSPHORYLATED
PEPTIDES
BY
MASS
SPECTROMETRY
M
ANFREDO
Q
UADRONI
10.1
INTRODUCTION
.
187
10.1.1
EXPERIMENTAL
APPROACHES
TO
THE
STUDY
OF
PHOSPHORYLATION
SITES
IN
PROTEINS
.
188
10.2
SPECIFIC
DETECTION
OF
PHOSPHOPEPTIDES
IN
COMPLEX
PEPTIDE
MIXTURES
.
189
10.2.1
ISOLATION
OF
PHOSPHOPEPTIDES
PRIOR
TO
MS
ANALYSIS
.
189
10.2.2
ENZYMATIC
REMOVAL
OF
THE
PHOSPHATE
GROUP
.
190
10.2.3
PHOSPHOPEPTIDE
DETECTION
BY
SELECTIVE
MS
SCANNING
METHODS
.
190
10.2.4
PHOSPHOPEPTIDE
DETECTION
BY
SELECTIVE
MS
SCANNING
METHODS
AFTER
SPECIFIC
CHEMICAL
MODIFICATIONS
.
192
CONTENTS
XV
10.3
PHOSPHORYLATION-SITE
ANALYSIS
BY
MS/MS
.
196
10.3.1
PHOSPHORYLATION-SITE
ANALYSIS
OF
NATIVE
PHOSPHOPEPTIDES
.
196
10.3.2
PHOSPHORYLATION-SITE
ANALYSIS
AFTER
CHEMICAL
MODIFICATION
OF
THE
PHOSPHOAMINO-ACID
SIDE
CHAINS
.
197
10.4
DATA
ANALYSIS
.
199
10.5
CONCLUSION
.
202
APPENDIX
.
203
1
IMAC
CHROMATOGRAPHY
FOR
THE
ISOLATION
OF
PHOSPHORYLATED
PEPTIDES
.
203
1.1
COLUMN
PACKING
.
203
1.2
IMAC
SEPARATION
.
203
2
CHEMICAL
MODIFICATION
OF
PHOSPHOPEPTIDES
FOR
MS
.
204
2.1
SYNTHESIS
OF
2
[4-PYRIDYL]
ETHANETHIOL
.
204
2.2
CONVERSION
OF
PHOSPHOSERINE
TO
S-PYRYDYLETHYLCYSTEINE
.
204
REFERENCES
.
204
11
GLYCOPROTEOMICS:
HIGH-THROUGHPUT
SEQUENCING
OF
OLIGOSACCHARIDE
MODIFICATIONS
TO
PROTEINS
P
AULINE
M.
R
UDD
,
C
RISTINA
C
OLOMINAS
,
L
OUISE
R
OYLE
,
N
EIL
M
URPHY
,
E
DMUND
H
ART
,
A
NTHONY
H.
M
ERRY
,
H
OLGER
F.
H
EBERSTREIT
,
AND
R
AYMOND
A.
D
WEK
11.1
BEYOND
THE
GENOME
AND
THE
PROTEOME
LIES
THE
GLYCOME
.
207
11.1.1
THE
IMPORTANCE
OF
GLYCOSYLATION
IN
PROTEOMICS
.
207
11.1.2
HIGH-THROUGHPUT
ANALYSIS
OF
HETEROGENEOUS
GLYCANS
REQUIRES
NEW
ANALYTICAL
STRATEGIES
.
208
11.2
A
RAPID
AND
ROBUST
STRATEGY
FOR
N
AND
O-GLYCAN
ANALYSIS
.
209
11.2.1
RELEASE
OF
N
AND
O-LINKED
GLYCANS
FROM
GLYCOPROTEINS
.
209
11.2.1.1
CHEMICAL
RELEASE
OF
N
AND
O-GLYCANS
FROM
GLYCOPROTEINS
USING
ANHYDROUS
HYDRAZINE
.
209
11.2.1.2
ENZYMATIC
RELEASE
AND
ANALYSIS
OF
N-LINKED
OLIGOSACCHARIDES
FROM
PROTEIN
BANDS
ON
SODIUM
DODECYL
SULPHATE
POLYACRYLAMIDE-GEL
ELECTROPHORESIS
GELS
.
209
11.2.1.3
ADVANTAGES
OF
THE
"
IN-GEL
"
RELEASE
METHOD
.
212
11.2.2
LABELLING
THE
GLYCAN
POOL
.
213
11.2.3
RESOLVING
RELEASED
GLYCAN
POOLS
AND
ASSIGNING
STRUCTURE
BY
HPLC
.
214
11.2.3.1
WEAK
ANION-EXCHANGE
CHROMATOGRAPHY
.
214
11.2.3.2
NORMAL-PHASE
HPLC
.
215
11.2.3.3
REVERSE-PHASE
HPLC
.
216
11.2.4
SIMULTANEOUS
SEQUENCING
OF
OLIGOSACCHARIDES
USING
ENZYME
ARRAYS
.
216
11.2.5
ANALYSIS
OF
THE
NP-HPLC
RESULTS
.
219
11.3
APPLICATIONS
OF
THIS
TECHNOLOGY
.
221
11.3.1
IGG
GLYCOSYLATION
AND
DISEASE
.
221
XVI
CONTENTS
11.3.2
POTENTIAL
ROLES
FOR
THE
GLYCANS
ATTACHED
TO
CD59
.
222
11.3.3
THE
THREE-DIMENSIONAL
STRUCTURE
OF
THE
PROTEIN
INFLUENCES
GLYCAN
PROCESSING
.
225
11.3.4
SIMULTANEOUS
ANALYSIS
OF
THE
N-GLYCAN
POOL
FROM
RAT
CD48
EXPRESSED
IN
CHO
CELLS
REVEALS
EXTENSIVE
HETEROGENEITY
.
225
11.3.5
ANALYSIS
OF
THE
O-GLYCANS
FROM
HUMAN
NEUTROPHIL
GELATINASE
B
SUGGESTS
THAT
THEY
MAY
PRODUCE
AN
EXTENDED
AND
RIGID
REGION
OF
THE
PEPTIDE
.
226
11.4
CONCLUSION
.
226
REFERENCES
.
226
12
PROTEOMICS
DATABASES
H
ANNO
L
ANGEN
AND
P
ETER
B
ERNDT
12.1
INTRODUCTION
.
229
12.2
PROTEIN
AND
NUCLEOTIDE-SEQUENCE
DATABASES
.
230
12.2.1
SWISS-PROT
.
230
12.2.2
TREMBL
.
232
12.2.3
GENBANK
.
232
12.2.4
PIR
.
233
12.2.5
OWL
.
233
12.2.6
EST
DATABASES
.
233
12.3
TWO-DIMENSIONAL
GEL
PROTEIN
DATABASES
.
234
12.3.1
SWISS
2D
POLYACRYLAMIDE-GEL
ELECTROPHORESIS
.
234
12.3.2
DANISH
CENTRE
FOR
HUMAN
GENOME
RESEARCH
2D-PAGE
DATABASES
.
239
12.3.3
ARGONNE
PROTEIN-MAPPING
GROUP
SERVER
.
240
12.3.4
SIENA
2D-PAGE
.
240
12.3.5
HEART
2D-PAGE
.
241
12.3.6
HSC
2D-PAGE
.
241
12.3.7
NATIONAL
INSTITUTES
FOR
MENTAL
HEALTH/NATIONAL
CANCER
INSTITUTE
PROTEIN-DISEASE
DATABASE
AND
THE
NATIONAL
CANCER
INSTITUTE/
FREDERICK
CANCER
RESEARCH
AND
DEVELOPMENT
CENTER
LABORATORY
OF
MATHEMATICAL
BIOLOGY
IMAGE
PROCESSING
.
241
12.3.8
YEAST-PROTEOME
DATABASE
.
242
12.3.9
MITODAT
.
242
12.3.10
LARGE-SCALE
BIOLOGY
.
242
12.3.11
UCSF2D-PAGE
.
242
12.3.12
ECO2DBASE
.
243
12.3.13
EMBRYONIC
STEM
CELLS
.
243
12.3.14
HUMAN
COLON-CARCINOMA
PROTEIN
DATABASE
.
243
12.3.15
YEAST
2D-PAGE
.
243
12.3.16
HAEMOPHILUS
2DE
PROTEIN
DATABASE
.
244
12.4
PROTEOMICS-DATABASE
DESIGN
.
244
12.4.1
THE
DATABASE
SCHEMA
.
245
CONTENTS
XVII
12.4.1.1
GENERAL
REMARKS
.
245
12.4.1.2
SAMPLE
AND
GEL
TRACKING
.
245
12.4.1.3
SPOT
LOCATION
AND
QUANTIFICATION
DATA
.
247
12.4.1.4
MASS-SPECTROMETRIC
DATA
.
248
12.4.1.5
PROTEIN
IDENTIFICATIONS
.
249
12.4.2
DATABASE
INTERFACE
.
249
12.4.2.1
BROWSER
.
250
12.4.2.2
COMMUNICATORS
.
251
12.4.2.3
EDITOR
.
251
12.4.2.4
AGENTS
.
251
12.4.3
DATABASE
TASKS
.
252
12.4.3.1
MAPPING
OF
PROTEOMES
.
252
12.4.3.2
PROTEIN-EXPRESSION
ANALYSIS
.
252
12.4.3.3
INTEGRATED
GENOMIC
ANALYSIS
.
252
12.4.3.4
PROTEIN
MODIFICATIONS
.
253
REFERENCES
.
253
13
QUO
VADIS
P
ETER
J
AMES
13.1
INTRODUCTION
.
259
13.2
PLUG-AND-PLAY
MS
.
260
13.3
RECENT
ADVANCES
IN
MS
INSTRUMENTATION
.
261
13.3.1
SENSITIVITY
AND
DUTY
CYCLES
.
261
13.3.2
MINIATURISATION
.
262
13.4
FOURIER-TRANSFORM
ION-CYCLOTRON
RESONANCE
MASS
SPECTROMETRY
.
262
13.4.1
THE
ADVANTAGES
OF
FT-ICR
MS
.
262
13.4.1.1
EXTREME
SENSITIVITY
AND
RESOLUTION
.
262
13.4.1.2
NON-DESTRUCTIVE
MEASUREMENT
.
263
13.4.2
THE
DISADVANTAGES
OF
FT-ICR
MS
.
264
13.4.2.1
HIGH
VACUUM
.
264
13.4.2.2
DUTY
CYCLE
.
264
13.5
FUTURE
DIRECTIONS
.
265
13.5.1
BYPASSING
PROTEOLYSIS:
FRAGMENTING
WHOLE
PROTEINS
IN
THE
MASS
SPECTROMETER
.
265
13.5.1.1
FRAGMENTATION
METHODS
.
265
13.5.1.2
PROTEIN
IDENTIFICATION
.
265
13.5.2
AN
ALTERNATIVE
TO
2D-PAGE?
MS
AS
THE
SECOND
DIMENSION
.
266
13.5.3
MOLECULAR-INTERACTION
MAPPING
.
266
13.6
CONCLUSION
.
267
REFERENCES
.
268
SUBJECT
INDEX
.
271 |
any_adam_object | 1 |
building | Verbundindex |
bvnumber | BV013308530 |
callnumber-first | Q - Science |
callnumber-label | QP551 |
callnumber-raw | QP551 |
callnumber-search | QP551 |
callnumber-sort | QP 3551 |
callnumber-subject | QP - Physiology |
classification_rvk | VG 9800 WC 4170 |
classification_tum | CHE 820f CHE 254f BIO 220f |
ctrlnum | (OCoLC)43945333 (DE-599)BVBBV013308530 |
dewey-full | 572/.636 |
dewey-hundreds | 500 - Natural sciences and mathematics |
dewey-ones | 572 - Biochemistry |
dewey-raw | 572/.636 |
dewey-search | 572/.636 |
dewey-sort | 3572 3636 |
dewey-tens | 570 - Biology |
discipline | Chemie / Pharmazie Biologie Chemie |
format | Book |
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id | DE-604.BV013308530 |
illustrated | Illustrated |
indexdate | 2024-11-22T17:13:15Z |
institution | BVB |
isbn | 3540672559 3540672567 |
language | English |
oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-009074200 |
oclc_num | 43945333 |
open_access_boolean | |
owner | DE-355 DE-BY-UBR DE-M49 DE-BY-TUM DE-20 DE-526 DE-B768 |
owner_facet | DE-355 DE-BY-UBR DE-M49 DE-BY-TUM DE-20 DE-526 DE-B768 |
physical | XXI, 274 S. graph. Darst. |
publishDate | 2001 |
publishDateSearch | 2001 |
publishDateSort | 2001 |
publisher | Springer |
record_format | marc |
series2 | Principles and practice |
spelling | Proteome research: mass spectrometry Peter James [ed.] Berlin [u.a.] Springer 2001 XXI, 274 S. graph. Darst. txt rdacontent n rdamedia nc rdacarrier Principles and practice Espectrometria de massas larpcal Proteínas larpcal Protéines - Analyse Protéines - Analyse ram Spectrométrie de masse Spectroscopie de masse ram Mass Spectrometry Mass spectrometry Proteins Analysis Proteome analysis Massenspektrometrie (DE-588)4037882-2 gnd rswk-swf Proteomanalyse (DE-588)4596545-6 gnd rswk-swf Proteomanalyse (DE-588)4596545-6 s Massenspektrometrie (DE-588)4037882-2 s DE-604 James, Peter Sonstige oth DNB Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=009074200&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
spellingShingle | Proteome research: mass spectrometry Espectrometria de massas larpcal Proteínas larpcal Protéines - Analyse Protéines - Analyse ram Spectrométrie de masse Spectroscopie de masse ram Mass Spectrometry Mass spectrometry Proteins Analysis Proteome analysis Massenspektrometrie (DE-588)4037882-2 gnd Proteomanalyse (DE-588)4596545-6 gnd |
subject_GND | (DE-588)4037882-2 (DE-588)4596545-6 |
title | Proteome research: mass spectrometry |
title_auth | Proteome research: mass spectrometry |
title_exact_search | Proteome research: mass spectrometry |
title_full | Proteome research: mass spectrometry Peter James [ed.] |
title_fullStr | Proteome research: mass spectrometry Peter James [ed.] |
title_full_unstemmed | Proteome research: mass spectrometry Peter James [ed.] |
title_short | Proteome research: mass spectrometry |
title_sort | proteome research mass spectrometry |
topic | Espectrometria de massas larpcal Proteínas larpcal Protéines - Analyse Protéines - Analyse ram Spectrométrie de masse Spectroscopie de masse ram Mass Spectrometry Mass spectrometry Proteins Analysis Proteome analysis Massenspektrometrie (DE-588)4037882-2 gnd Proteomanalyse (DE-588)4596545-6 gnd |
topic_facet | Espectrometria de massas Proteínas Protéines - Analyse Spectrométrie de masse Spectroscopie de masse Mass Spectrometry Mass spectrometry Proteins Analysis Proteome analysis Massenspektrometrie Proteomanalyse |
url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=009074200&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
work_keys_str_mv | AT jamespeter proteomeresearchmassspectrometry |