Peptides: chemistry and biology:
Gespeichert in:
| Vorheriger Titel: | Sewald, Norbert Peptides |
|---|---|
| Hauptverfasser: | , |
| Format: | Buch |
| Sprache: | English |
| Veröffentlicht: |
Weinheim
WILEY-VCH
2009
|
| Ausgabe: | 2., rev. and updated ed. |
| Schlagworte: | |
| Online-Zugang: | Inhaltstext Inhaltsverzeichnis |
| Beschreibung: | Früher mit der Nummer 9783527304059. - Literaturangaben |
| Beschreibung: | XVI, 578 S. Ill., graph. Darst. |
| ISBN: | 9783527318674 |
Internformat
MARC
| LEADER | 00000nam a2200000 c 4500 | ||
|---|---|---|---|
| 001 | BV035386905 | ||
| 003 | DE-604 | ||
| 005 | 20201215 | ||
| 007 | t | ||
| 008 | 090323s2009 ad|| |||| 00||| eng d | ||
| 015 | |a 09,N01,1367 |2 dnb | ||
| 016 | 7 | |a 99167653X |2 DE-101 | |
| 020 | |a 9783527318674 |c Pb. : EUR 99.00 (freier Pr.), sfr 158.00 (freier Pr.) |9 978-3-527-31867-4 | ||
| 024 | 3 | |a 9783527318674 | |
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| 100 | 1 | |a Sewald, Norbert |d 1961- |e Verfasser |0 (DE-588)120773473 |4 aut | |
| 245 | 1 | 0 | |a Peptides: chemistry and biology |c Norbert Sewald and Hans-Dieter Jakubke |
| 250 | |a 2., rev. and updated ed. | ||
| 264 | 1 | |a Weinheim |b WILEY-VCH |c 2009 | |
| 300 | |a XVI, 578 S. |b Ill., graph. Darst. | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b n |2 rdamedia | ||
| 338 | |b nc |2 rdacarrier | ||
| 500 | |a Früher mit der Nummer 9783527304059. - Literaturangaben | ||
| 650 | 4 | |a Peptide | |
| 650 | 4 | |a Peptides | |
| 650 | 0 | 7 | |a Chemie |0 (DE-588)4009816-3 |2 gnd |9 rswk-swf |
| 650 | 0 | 7 | |a Biologie |0 (DE-588)4006851-1 |2 gnd |9 rswk-swf |
| 650 | 0 | 7 | |a Peptide |0 (DE-588)4045125-2 |2 gnd |9 rswk-swf |
| 689 | 0 | 0 | |a Peptide |0 (DE-588)4045125-2 |D s |
| 689 | 0 | 1 | |a Chemie |0 (DE-588)4009816-3 |D s |
| 689 | 0 | |8 1\p |5 DE-604 | |
| 689 | 1 | 0 | |a Peptide |0 (DE-588)4045125-2 |D s |
| 689 | 1 | 1 | |a Biologie |0 (DE-588)4006851-1 |D s |
| 689 | 1 | |8 2\p |5 DE-604 | |
| 700 | 1 | |a Jakubke, Hans-Dieter |d 1933- |e Verfasser |0 (DE-588)1056797495 |4 aut | |
| 780 | 0 | 0 | |i 1. Auflage |a Sewald, Norbert |t Peptides |w (DE-604)BV014331025 |
| 856 | 4 | 2 | |q text/html |u http://deposit.dnb.de/cgi-bin/dokserv?id=3192083&prov=M&dok_var=1&dok_ext=htm |3 Inhaltstext |
| 856 | 4 | 2 | |m Digitalisierung UB Regensburg |q application/pdf |u http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=017307758&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |3 Inhaltsverzeichnis |
| 883 | 1 | |8 1\p |a cgwrk |d 20201028 |q DE-101 |u https://d-nb.info/provenance/plan#cgwrk | |
| 883 | 1 | |8 2\p |a cgwrk |d 20201028 |q DE-101 |u https://d-nb.info/provenance/plan#cgwrk | |
| 943 | 1 | |a oai:aleph.bib-bvb.de:BVB01-017307758 | |
Datensatz im Suchindex
| _version_ | 1805092094898864128 |
|---|---|
| adam_text |
Contents
Prefece
to the second edition
XIII
Prefece
to the first edition XV
Ί
Introduction and Background
1
References
4
2
Fundamental Chemical and Structural Principles
5
2.1
Definitions and Main Conformational Features of the
Peptide
Bond
5
2.2
Building Blocks, Classification, and Nomenclature
7
2.3
Analysis of the Covalent Structure of Peptides and Proteins
11
2.3.1
Separation and Purification
13
2.3.1.1
Separation Principles
13
2.3.1.2
Purification Techniques
17
2.3.1.3
Stability Problems
19
2.3.1.4
Evaluation of Homogeneity
20
2.3.2
Primary Structure Determination
20
2.3.2.1
End Group Analysis
21
2.3.2.2
Cleavage of Disulfide Bonds
24
2.3.2.3
Analysis of
Amino
Acid Composition
24
2.3.2.4
Selective Methods of Cleaving
Peptide
Bonds
26
2.3.2.5
N-Terminal Sequence Analysis
(Edman
Degradation)
28
2.3.2.6
C-Terminal
Sequence Analysis
30
2.3.2.7
Mass Spectrometry
31
2.3.2.8
Peptide
Ladder Sequencing
32
2.3.2.9
Assignment of Disulfide Bonds and
Peptide
Fragment Ordering
Зі
2.3.2.10
Location of Post-Translational Modifications and Bound Cofactors
34
2.4
Three-Dimensional Structure
36
2.4.1
Secondary Structure
36
2.4.1.1
Helices
37
2.4.1.2 ß-Sheets 39
2.4.1.3
Turns
40
2.4.1.4
Amphiphilic Structures
42
VI
Contents
2.4.2
Tertiary Structure
44
2.4.2.1
Structure Prediction
48
2.5
Methods of Structural Analysis
49
2.5.1
Circular Dichroism
49
2.5.2
Infrared Spectroscopy
51
2.5.3
NMR Spectroscopy
52
2.5.4
Х
-Ray Crystallography
54
2.5.5
UV Fluorescence Spectroscopy
55
2.6
Review Questions
56
References
57
3
Biology of Peptides
63
3.1
Historical Aspects and Biological Functions
3.2
Biosynthesis
75
3.2.1
Ribosomal
Peptide
Synthesis
75
3.2.2
Post-Translational Modification
79
3.2.2.1
Enzymatic Cleavage of
Peptide
Bonds
79
3.2.2.2
Hydroxylation
80
3.2.2.3
Carboxylation
81
3.2.2.4
Glycosylation
81
3.2.2.5
Amidation
86
3.2.2.6
Phosphorylation
87
3.2.2.7
Lipidation
88
3.2.2.8
Pyroglutamyl Formation
90
3.2.2.9
Sulfation 91
3.2.2.10
Further Post-Translational Modifications
92
3.2.3
Nonribosomal
Peptide
Synthesis
94
3.3
Selected Biologically Active Peptides
96
3.3.1
Gastroenteropancreatic
Peptide
Families
96
3.3.1.1
The Gastrin Family
97
3.3.1.2
Secretin Family
98
3.3.1.3
The Insulin Superfamily
101
3.3.1.4
The Somatostatin Family
104
3.3.1.5
The Tachykinin Family
105
3.3.1.6
The
Neuropeptide
Y
family
106
3.3.1.7
The Ghrelin Family
108
3.3.1.8
The EGF Family
109
3.3.2
Hypothalamic Liberins and Statins
110
3.3.2.1
Thyroliberin
112
3.3.2.2
Gonadoliberin
113
3.3.2.3
Corticoliberin
113
3.3.2.4
Growth Hormone-Releasing Hormone
114
3.3.3
Pituitary Hormones
115
3.3.3.1
Growth Hormone
115
3.3.3.2
Corticotropin
115
63
Contents
VII
3.3.3.3 Melanotropin 117
3.3.4 Neurohypophyseal
Hormones
118
3.3.4.1
Oxytocin
118
3.3.4.2 Vasopressin
í
19
3.3.5
Parathyroid Hormone and Calcitonin/Calcitonin Gene-Related
Peptide
Family
120
3.3.5.1
Parathyroid Hormone
120
3.3.5.2
Parathyroid Hormone-Related Peptides
121
3.3.5.3
The Calcitonin/Calcitonin Gene-Related
Peptide
Family
121
3.3.6
The Blood Pressure Regulating
Peptide
Families
123
3.3.6.1
Angiotensin-Kinin System
123
3.3.6.2
Endothelins and Endothelin-Like Peptides
125
3.3.6.3
Cardiac
Peptide
Hormones
127
3.3.7
Neuropeptides
128
3.3.7.1
Endorphins
131
3.3.7.2
Dynorphins
136
3.3.7.3
Hypocretins (Orexins)
136
3.3.7.4
Dermorphins
137
3.3.7.5
Deltorphins
138
3.3.7.6
Nociceptin/Orphanin and Nodstatin
138
3.3.7.7
Exorphins
139
3.3.7.8
The Adipokinetic Hormone/Red Pigment-Concentrating Hormone
Family
140
3.3.7.9
Endomorphins
141
3.3.7.10
The Allatostatin Families
141
3.3.7.11
Neuromedins
142
3.3.7.12
Additional Neuroactive Peptides
143
3.3.8
Peptide
Antibiotics
146
3.3.8.1
Nonribosomally Synthesized
Peptide
Antibiotics
147
3.3.8.2
Ribosomally Synthesized
Peptide
Antibiotics
152
3.3.9
Peptide
Toxins
156
3.4
Review Questions
262
References
163
4
Peptide
Synthesis
175
4.1
Principles and Objectives
175
4.1.1
Main Targets of
Peptide
Synthesis
175
4.1.2
Basic Principles of
Peptide
Bond Formation
178
4.2
Protection of Functional Groups
181
4.2.1
N'-Amino Protection
182
4.2.1.1
Alkoxycarbonyl-Type (Urethane-Type) Protecting Groups
183
4.2.1.2
Carboxamide-Type Protecting Groups
192
4.2.1.3
Sulfonamide and Sulfenamide-Type Protecting Groups
192
4.2.1.4
Alkyl
-Туре
Protecting Groups
192
4.2.2
Ca-Carboxy
Protection
193
VIII Contents
4.2.2.1 Esters 194
4.2.2.2
Amides and Hydrazides
299
4.2.3
C-Terminal
and Backbone N^carboxamide Protection
199
4.2.4
Side-Chain Protection
201
4.2.4.1
Guanidino Protection
202
4.2.4.2
ω
-Amino
Protection
204
4.2.4.3
ω
-СагЪоху
Protection
205
4.2.4.4
Thiol Protection
208
4.2.4.5
Imidazole Protection
211
4.2.4.6
Hydroxy Protection
214
4.2.4.7
Thioether Protection
226
4.2.4.8
Indole
Protection
227
4.2.4.9
ω
-Amide
Protection 22S
4.2.5
Enzyme-Labile Protecting Groups
220
4.2.5.1
Enzyme-labile Na-amino Protection
221
4.2.5.2
Enzyme-labile C-carboxy Protection and Enzyme-labile Linker
Moieties
223
4.2.6
Protecting Group Compatibility
223
4.3
Peptide
Bond Formation
224
4.3.1
Acyl Azides
225
4.3.2
Anhydrides
226
4.3.2.1
Mixed Anhydrides
227
4.3.2.2
Symmetrical Anhydrides
229
4.3.2.3
N-Carboxy Anhydrides
229
4.3.3
Carbodiimides
232
4.3.4
Active Esters
235
4.3.5
Acyl Halides
237
4.3.6
Phosphonium Reagents
239
4.3.7
Guanidinium/Uronium Reagents
240
4.3.8
Immonium Type Coupling Reagents
242
4.3.9
Further Special Methods for
Peptide
Synthesis
243
4.4
Racemization During Synthesis
246
4.4.1
Direct Enolization
246
4.4.2
5(4H)-Oxazolone Mechanism
247
4.4.3
Racemization Tests: Stereochemical Product Analysis
249
4.5
Solid-Phase
Peptide
Synthesis (SPPS)
251
4.5.1
Solid Supports and Linker Systems
253
4.5.2
Safety-Catch linkers
262
4.5.3
Protection Schemes
265
4.5.3.1
Boc/Bzl-protecting Groups Scheme (Merrifield Tactics)
265
4.5.3.2
Fmoc/tBu-Protecting Groups Scheme (Sheppard Tactics)
267
4.5.3.3
Three- and More-Dimensional Orthogonality
268
4.5.4
Chain Elongation
269
4.5.4.1
Coupling Methods
269
4.5.4.2
Undesired Problems During Elongation
269
Contents
IX
4.5.4.3
Difficult Sequences
271
4.5.4.4
Chemical Strategies for SPPS Methodological Improvements
273
4.5.4.5
On-Resin Monitoring
273
4.5.5
Automation of the Process
274
4.5.6
Peptide
Cleavage from the Resin
275
4.5.6.1
Acidolytic Methods
275
4.5.6.2
Side Reactions
276
4.5.6.3
Advantages and Disadvantages of the Boc/Bzl and
Fmoc/tBu Schemes
277
4.5.7
Examples of Syntheses by Linear SPPS
277
4.5.8
Special Methods of Polymer-supported Synthesis
278
4.5.9
Microwave-Enhanced
Peptide
Synthesis
280
4.6
Biochemical Synthesis
281
4.6.1
Recombinant
DNA
Techniques
281
4.6.1.1
Principles of
DNA
Technology
282
4.6.1.2
Examples of Synthesis by Genetic Engineering
285
4.6.1.3
Cell-free Translation Systems
288
4.6.1.4
Proteins Containing Non-Proteinogenic
Amino
Acids
-
The Expansion
of the Genetic Code
290
4.6.2
Enzymatic
Peptide
Synthesis
291
4.6.2.1
Approaches to Enzymatic Synthesis
291
4.6.2.2
Manipulations to Suppress Competitive Reactions
294
4.6.2.3
Substrate Mimetic Approach
295
4.6.3
Further Selected Biochemical Methods
297
4.6.3.1
Non-ribosomal
Peptide
Synthesis
297
4.6.3.2
Peptide
Bond Formation by LF-Transferase
297
4.6.3.3
Antibody-catalyzed
Peptide
Bond Formation
297
4.7
Review Questions
300
References
301
5
Synthesis Concepts for Peptides and Proteins
317
5.1
Strategy and Tactics
317
5.1.1
Linear or Stepwise Synthesis
317
5.1.2
Convergent Synthesis
320
5.1.3
Tactical Considerations
321
5.1.3.1
Selected Protecting Group Schemes
321
5.1.3.2
Preferred Coupling Procedures
324
5.2
Solution Phase Synthesis (SPS)
325
5.2.1
Convergent Synthesis Using Maximally Protected Segments
325
5.2.2
Convergent Synthesis Using Minimally Protected Segments
327
5.2.2.1
Chemical Approaches
327
5.2.2.2
Enzymatic Approaches
329
5.3
Solution Phase/Solid Phase-Hybrid Approaches
332
5.3.1
Solid Phase Synthesis of Protected Segments
332
5.3.2
SPS/SPPS-Hybrid Condensrion of Lipophilic Segments
333
X
Contents
5.3.3
Phase Change
Synthesis
335
5.3.4
SPS/SPPS-Hybrid Approach to Protein and Large Scale
Peptide
Synthesis
335
5.4
Optimized Strategies on a Polymeric Support
337
5.4.1
Standard SPPS
337
5.4.2
Convergent Solid-Phase
Peptide
Synthesis
339
5.4.3
Handle Approaches
341
5.4.3.1
Positively Charged Handles
341
5.4.3.2
Liquid Phase Method
342
5.4.3.3
Excluded Protecting Group Method
343
5.5
Chemical Iigation Strategies
343
5.5.1
Native Chemical Ligation
344
5.5.1.1
Facile
Peptide Thioester
Synthesis
346
5.5.1.2
Extended Native Chemical Ligation
346
5.5.1.3
Kinetically Controlled Ligation
348
5.5.1.4
Solid Phase Chemical Ligation
350
5.5.1.5
Alternative Approaches to Native Chemical Ligation
350
5.5.2
Expressed Protein Ligation (Intein-mediated Protein Ligation)
351
5.5.3
Prior Capture-mediated Ligation
353
5.5.3.1
Template-mediated Ligation
353
5.5.4
Non-native Chemoselective Ligation
355
5.5.4.1
Thioester- and Thioether-forming Ligations
355
5.5.4.2 Hydrazone-
and Oxime-forming Ligations
356
5.5.5
Alternative Ligation Approaches
356
5.5.5.1
Staudinger Ligation
357
5.5.5.2
Ketoacid-hydroxylamine Amide Ligations
357
5.5.5.3
Expressed enzymatic ligation
358
5.5.5.4
Sortase-mediated Ligation
359
5.6
Review Questions
359
References
360
6
Synthesis of Special Peptides and
Peptide
Conjugates
365
6.1
Cyclopeptides
365
6.1.1
Backbone Cyclization (Head-to-Tail Cyclization)
371
6.1.2
Side Chain-to-Head and Tail-to-Side Chain
Cyclizaüons
380
6.1.3
Side Chain-to-Side Chain Cyclizations
380
6.2
Cystine Peptides
381
6.3
Glycopeptides
386
6.4
Phosphopeptides
395
6.5
Lipopeptides
398
6.6
Sulfated Peptides
402
6.7
Review Questions
403
References
403
7
Peptide
and Protein Design, Pseudopeptides, and Peptidomimetics
411
7.1
Peptide
Design
413
Contents
XI
7.2
Modified Peptides
418
7.2.1
Side-Chain Modification
418
7.2.2
Backbone Modification
421
7.2.3
Combined Modification (Global Restriction) Approaches
423
7.2.4
Modification by Secondary Structure Mimetics
425
7.2.5
Transition State Inhibitors
427
7.3
Peptidomimetics
428
7.4
Pseudobiopolymers
431
7.4.1
Peptoids
432
7.4.2
Peptide
Nucleic Acids
(PNA)
434
7.4.3 ß-Peptides, Hydrazino
Peptides, Aminoxy Peptides, and
Oligosulfonamides
435
7.4.4
Oligocarbamates
437
7.4.5
Oligopyrrolinones
438
7.5
Macropeptides and
de novo
Design of Peptides and Proteins
439
7.5.1
Protein Design
439
7.5.2
Peptide Dendrimers
444
7.5.3
Peptide
Polymers
447
7.6
Review Questions
447
References
448
8
Combinatorial
Peptide
Synthesis
457
8.1
Parallel Synthesis
460
8.1.1
Synthesis in Teabags
461
8.1.2
Synthesis on Polyethylene Pins (Multipin Synthesis)
462
8.1.3
Parallel Synthesis of Single Compounds on Cellulose or Polymer
Strips
464
8.1.4
light-Directed, Spatially Addressable Parallel Synthesis
465
8.1.5
liquid-Phase Synthesis using Soluble Polymeric Support
466
8.2
Synthesis of Mixtures
467
8.2.1
Reagent Mixture Method
468
8.2.2
Split and Combine Method
468
8.2.3
Encoding Methods
470
8.2.4
Peptide
Library Deconvolution
474
8.2.5
Dynamic Combinatorial Libraries
476
8.2.6
Biological Methods for the Synthesis of
Peptide
Libraries
477
8.3
Review Questions
478
References
479
9
Application of Peptides and Proteins
483
9.1
General Production Strategies
483
9.2
Improvement of the Therapeutic Potential
486
9.2.1
Peptide
and Protein Drug Modifications
486
9.2.2
Peptide
Drag Delivery Systems
488
9.3
Protein Pharmaceuticals
492
9.3.1
Importance and Sources
492
XII Contents
9.3.2
Endogenous Pharmaceutical Proteins
493
9.3.3
Engineered Protein Pharmaceuticals
493
9.3.3.1
Selected
Recombinant
Proteins
493
9.3.3.2
Peptide-Based Vaccines
497
9.3.3.3
Monoclonal Antibodies
498
9.3.3.4
Future Perspectives
500
9.4
Peptide
Pharmaceuticals
502
9.4.1
Large-Scale
Peptide
Synthesis
502
9.4.2
Peptide
Drugs and Drug Candidates
507
9.4.3
Peptides as Tools in Drug Discovery
515
9.4.4
Peptides Targeted to Functional Sites of Proteins
517
9.4.5
Peptides Used in Target Validation
517
9.4.6
High-throughput Screening
(HTS)
Using Peptides as Surrogate
Iigands
518
9.4.7
Artificial
Peptide
Analogs in Drug Discovery
521
9.5
Review Questions
522
References
523
10
Peptides in Proteomics
529
10.1
Genome and Proteome
529
10.2
Separation Methods
530
10.2.1
Depletion Strategies
530
10.2.2
Two-Dimensional Polyacrylamide Gel-Electrophoresis
530
10.2.3
Gel-Free Methods
-
Two-Dimensional Liquid Chromatography
(2D-LC, MudPIT)
531
10.3
Peptide
and Protein Analysis in Proteomics
532
10.3.1
Mass Spectrometry
532
10.3.2
Quantitative Proteomics
533
10.3.2.1
Metabolic Stable-Isotope Labelling
533
10.3.2.2
Tagging Methods
533
10.3.2.3
Enzymatic Stable-Isotope Labeling
535
10.4
Activity-Based Proteomics
535
10.4.1
Irreversibly Binding Affinity-Based Probes
536
10.4.2
Reversibly Binding Affinity-Based Probes
539
10.4.2.1
Inhibitor Affinity Chromatography
(IAC)
540
10.4.2.2
Labelling Strategies with Reversibly Binding Protein Iigands
541
10.5
Review Questions
543
References
543
Glossary
547
Index
559 |
| any_adam_object | 1 |
| author | Sewald, Norbert 1961- Jakubke, Hans-Dieter 1933- |
| author_GND | (DE-588)120773473 (DE-588)1056797495 |
| author_facet | Sewald, Norbert 1961- Jakubke, Hans-Dieter 1933- |
| author_role | aut aut |
| author_sort | Sewald, Norbert 1961- |
| author_variant | n s ns h d j hdj |
| building | Verbundindex |
| bvnumber | BV035386905 |
| callnumber-first | Q - Science |
| callnumber-label | QD431 |
| callnumber-raw | QD431 |
| callnumber-search | QD431 |
| callnumber-sort | QD 3431 |
| callnumber-subject | QD - Chemistry |
| classification_rvk | VK 8560 WD 5250 |
| classification_tum | CHE 820f |
| ctrlnum | (OCoLC)271775096 (DE-599)DNB99167653X |
| dewey-full | 547.7 |
| dewey-hundreds | 500 - Natural sciences and mathematics |
| dewey-ones | 547 - Organic chemistry |
| dewey-raw | 547.7 |
| dewey-search | 547.7 |
| dewey-sort | 3547.7 |
| dewey-tens | 540 - Chemistry and allied sciences |
| discipline | Chemie / Pharmazie Biologie Chemie |
| edition | 2., rev. and updated ed. |
| format | Book |
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| id | DE-604.BV035386905 |
| illustrated | Illustrated |
| indexdate | 2024-07-20T10:06:08Z |
| institution | BVB |
| isbn | 9783527318674 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-017307758 |
| oclc_num | 271775096 |
| open_access_boolean | |
| owner | DE-91G DE-BY-TUM DE-20 DE-19 DE-BY-UBM DE-M49 DE-BY-TUM DE-29T DE-355 DE-BY-UBR DE-703 DE-92 DE-83 DE-11 DE-188 DE-634 DE-1102 |
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| physical | XVI, 578 S. Ill., graph. Darst. |
| publishDate | 2009 |
| publishDateSearch | 2009 |
| publishDateSort | 2009 |
| publisher | WILEY-VCH |
| record_format | marc |
| spelling | Sewald, Norbert 1961- Verfasser (DE-588)120773473 aut Peptides: chemistry and biology Norbert Sewald and Hans-Dieter Jakubke 2., rev. and updated ed. Weinheim WILEY-VCH 2009 XVI, 578 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Früher mit der Nummer 9783527304059. - Literaturangaben Peptide Peptides Chemie (DE-588)4009816-3 gnd rswk-swf Biologie (DE-588)4006851-1 gnd rswk-swf Peptide (DE-588)4045125-2 gnd rswk-swf Peptide (DE-588)4045125-2 s Chemie (DE-588)4009816-3 s 1\p DE-604 Biologie (DE-588)4006851-1 s 2\p DE-604 Jakubke, Hans-Dieter 1933- Verfasser (DE-588)1056797495 aut 1. Auflage Sewald, Norbert Peptides (DE-604)BV014331025 text/html http://deposit.dnb.de/cgi-bin/dokserv?id=3192083&prov=M&dok_var=1&dok_ext=htm Inhaltstext Digitalisierung UB Regensburg application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=017307758&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis 1\p cgwrk 20201028 DE-101 https://d-nb.info/provenance/plan#cgwrk 2\p cgwrk 20201028 DE-101 https://d-nb.info/provenance/plan#cgwrk |
| spellingShingle | Sewald, Norbert 1961- Jakubke, Hans-Dieter 1933- Peptides: chemistry and biology Peptide Peptides Chemie (DE-588)4009816-3 gnd Biologie (DE-588)4006851-1 gnd Peptide (DE-588)4045125-2 gnd |
| subject_GND | (DE-588)4009816-3 (DE-588)4006851-1 (DE-588)4045125-2 |
| title | Peptides: chemistry and biology |
| title_auth | Peptides: chemistry and biology |
| title_exact_search | Peptides: chemistry and biology |
| title_full | Peptides: chemistry and biology Norbert Sewald and Hans-Dieter Jakubke |
| title_fullStr | Peptides: chemistry and biology Norbert Sewald and Hans-Dieter Jakubke |
| title_full_unstemmed | Peptides: chemistry and biology Norbert Sewald and Hans-Dieter Jakubke |
| title_old | Sewald, Norbert Peptides |
| title_short | Peptides: chemistry and biology |
| title_sort | peptides chemistry and biology |
| topic | Peptide Peptides Chemie (DE-588)4009816-3 gnd Biologie (DE-588)4006851-1 gnd Peptide (DE-588)4045125-2 gnd |
| topic_facet | Peptide Peptides Chemie Biologie |
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| work_keys_str_mv | AT sewaldnorbert peptideschemistryandbiology AT jakubkehansdieter peptideschemistryandbiology |