Structural insights into multidomain toxins - Mcf1 (P. Iuminescens) and TcdA&TcdB (C. difficile):
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|---|---|
| Format: | Thesis Book |
| Language: | English |
| Published: |
Dortmund
[2018?]
|
| Subjects: | |
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| Physical Description: | 148 Seiten Illustrationen 21 cm |
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| 100 | 1 | |a Hagel, Philine |d 1989- |e Verfasser |0 (DE-588)1175005274 |4 aut | |
| 245 | 1 | 0 | |a Structural insights into multidomain toxins - Mcf1 (P. Iuminescens) and TcdA&TcdB (C. difficile) |c submitted 2018 by Philine Nagel |
| 264 | 1 | |a Dortmund |c [2018?] | |
| 300 | |a 148 Seiten |b Illustrationen |c 21 cm | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b n |2 rdamedia | ||
| 338 | |b nc |2 rdacarrier | ||
| 502 | |b Dissertation |c Technical University of Dortmund |d 2018 | ||
| 655 | 7 | |0 (DE-588)4113937-9 |a Hochschulschrift |2 gnd-content | |
| 856 | 4 | 2 | |m B:DE-101 |q application/pdf |u http://d-nb.info/1176153064/04 |3 Inhaltsverzeichnis |
| 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=032365656&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |3 Inhaltsverzeichnis |
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| adam_text | CONTENT
CONTENT.............................................................................................................................................................................
1
I. LIST OF
ABBREVIATIONS.................................................................................................................................................
1
1 ABSTRACT /
SUMMARY...........................................................................................................................................
4
1.1
ABSTRACT...............................................................................................................................................................
4
1.2
ZUSAMMENFASSUNG.............................................................................................................................................
5
2
INTRODUCTION........................................................................................................................................................6
2.1 PHOTORHABDUS
LUMINESCENS.............................................................................................................................6
2.1.1 LIFE C
YCLE...........................................................................................................................................6
2.1.2 PATHOGENESIS
MECHANISMS..............................................................................................................
7
2.1.3 TOXINS OF PHOTORHABDUS
LUMINESCENS..............................................................................................
8
2.1.3.1 TOXIN COMPLEX
(TC)-TOXINS........................................................................................................
9
2.1.3.2 PHOTORHABDUS VIRULENCE CASSETTES
(PVCS)...........................................................................10
2.1.3.3 BINARY PHOTORHABDUS
TOXINS...................................................................................................
11
2.1.3.4 MAKES CATERPILLARS FLOPPY
(MCF)-TOXINS................................................................................11
2.2 CLOSTRIDIUM
DIFFICILE.........................................................................................................................................
14
2.2.1 LARGE CLOSTRIDIAL GLYCOSYLATING
TOXINS.............................................................................................14
2.2.1.1 MECHANISM OF ACTION OF TCDA AND
TCDB..............................................................................14
2.2.1.2 ARCHITECTURE AND STRUCTURE OF TCDA AND
TCDB.....................................................................16
2.3 STRUCTURAL
ANALYSIS............................................................................................................................................19
2.3.1 ELECTRON MICROSCOPY ON BIOLOGICAL
SAMPLES.................................................................................
20
2.3.1.1 RECENT DEVELOPMENTS AND THE RESOLUTION
REVOLUTION.......................................................23
2.3.1.1.1 VOLTA PHASE P LA TE
.............................................................................................................
25
2.3.1.2 SINGLE PARTICLE
ANALYSIS...........................................................................................................
26
3
MATERIALS..............................................................................................................................................................
29
3.1 DEVICES,
ACCESSORIES.....................................................................................................................................
29
3.1.1 CHROMATOGRAPHY
COLUMNS...........................................................................................................
30
3.2 CHEMICALS, SOLUTIONS,
CONSUMABLES............................................................................................................31
3.3 MEDIA,
BUFFERS..................................................................................................................................................
32
3.4
KITSYSTEMS/SCREENS.........................................................................................................................................
33
3.4.1 CRYSTALLIZATION
KITS/SCREENS..............................................................................................................
33
3.5 ENZYMES,
ANTIBODIES.......................................................................................................................................34
3.6
SOFTWARE............................................................................................................................................................
34
4
METHODS.................................................................................................................................................................35
4.1 MOLECULAR-BIOLOGICAL & PROTEINBIOCHEMICAL
METHODS.............................................................................
35
4.1.1 TRANSFORMATION OF CHEMICAL COM PETENT CELLS VIA
HEATSHOCK......................................................35
4.1.2 EXPRESSION IN E. CO
LI..........................................................................................................................35
4.1.3 PROTEIN
PURIFICATION..........................................................................................................................
35
4.1.3.1 AFFINITY
CHROMATOGRAPHY.......................................................................................................
36
4.1.3.2 SIZE EXCLUSION
CHROMATOGRAPHY............................................................................................
36
4.1.3.3 LONEXCHANGE
CHROMATOGRAPHY............................................................................................
37
4.1.4 VISUALIZATION VIA
SDS-PAGE.............................................................................................................
37
4.1.5 WESTERN
BLOT.....................................................................................................................................37
4.1.6 TRYPTIC IN-GEL DIGESTION & HPLC-MS-ANALYSIS OF DIGESTED PROTEINS
...............................................
38
4.1.7 CONCENTRATION DETERMINATION OF PROTEINS VIA UV-ABSORPTION
.......................................................
38
4.1.8 PROTEIN STABILITY SCREEN
(NANODSF).................................................................................................
39
4.1.9 INSPOE-INDUCED AUTOCATALYTIC C
LEAVAGE.........................................................................................39
4.1.10 RECONSTITUTION OF PROTEINS INTO MEMBRANE SYSTEMS
...............................................................
42
4.1.10.1 NANODISCS AND
LIPOSOMES....................................................................................................
43
4.1.10.2 CELL
GHOSTS...............................................................................................................................
44
4.2 CELL BIOLOGICAL M
ETHODS.................................................................................................................................45
4.2.1 CELL
PROPAGATION.............................................................................................................................
45
4.2.1.1 INSECT
CELLS...............................................................................................................................45
4.2.1.2 MAMMALIAN
CELLS....................................................................................................................
45
4.2.2 CELLTITER BLUE
ASSAY..........................................................................................................................
45
4.3 STRUCTURAL BIOLOGY
METHODS............................................................................................................................
47
4.3.1 NEGATIVE STAIN ELECTRON M
ICROSCOPY.............................................................................................
47
4.3.1.1 SAMPLE
PREPARATION................................................................................................................47
4.3.1.2 DATA C
OLLECTION......................................................................................................................
48
4.3.1.3 SINGLE PARTICLE ANALYSIS &
PROCESSING.....................................................................................
48
4.3.1.4 GOLD
LABELING.........................................................................................................................
49
4.3.2 ELECTRON
CRYO-MICROSCOPY...............................................................................................................49
4.3.2.1 SAMPLE
PREPARATION..............................................................................................................
49
4.3.2.1.1 PURE IC E
.............................................................................................................................
50
4.3.2.1.2 GRAPHENE
OXIDE................................................................................................................51
4.3.2.2 DATA C
OLLECTION......................................................................................................................
51
4.3.2.2.1 M CFL ON FEI TITAN KRIOS WITH FALCON
II.................................................................................51
4.3.2.2.2 M C FL, TCDA/TCDB ON FEI TITAN KRIOS WITH K2 SUMMIT, ENERGY
FILTER AND VOLTA PHASE
PLATE 52
4.3.2.3 SINGLE PARTICLE
ANALYSIS...........................................................................................................
53
4.3.2.3.1
PRE-PROCESSING....................................................................................................................54
4.3.2.3.2
PROCESSING...........................................................................................................................
55
4.3.2.4 STRUCTURE
ANALYSIS....................................................................................................................57
4.3.3 PROTEIN
CRYSTALLOGRAPHY...................................................................................................................57
4.3.3.1 PROTEIN
CONCENTRATION............................................................................................................
57
4.3.3.2 CRYSTALLIZATION ACCORDING TO
VAPOR-DIFFUSION........................................................................58
4.3.3.3 OPTIMIZATION OF CRYSTALLIZATION
CONDITIONS...........................................................................
59
4.3.3.3.1 LIMITED
PROTEOLYSIS...............................................................................................................
59
4.3.3.3.2 LYSINE
METHYLATION.............................................................................................................
60
4.3.3.4 PROTEIN CRYSTAL CRYO
CONSERVATION.........................................................................................
61
5 RESULTS AND
DISCUSSION...............................................................................................................................
62
5.1 PHOTORHABDUS LUMINESCENS M CFL
TOXIN.......................................................................................................
62
5.1.1 PROTEIN ISOLATION AFTER EXPRESSION IN E.
COLI......................................................................................
62
5.1.1.1 ANALYSIS OF PROTEIN STABILITY IN VARIOUS BUFFER
CONDITIONS...................................................... 64
5.1.2 M CFL IS TOXIC TO INSECT AND MAMMALIAN
CELLS...............................................................................66
5.1.2.1 EFFECT ON THE INSECT CELL LINES SF9, HIGH FIVE*, TNAO38 AND
DS2.......................................66
5.1.2.2 EFFECT ON THE MAMMALIAN CELL LINE
HEK293.........................................................................69
5.1.3 STRUCTURE DETERMINATION BY X-RAY
CRYSTALLOGRAPHY........................................................................70
5.1.3.1 LIMITED PROTEOLYSIS FOR RECEIVING STABLE PROTEIN FRAGMENTS
..............................................
72
5.1.4 STRUCTURE DETERMINATION BY ELECTRON MICROSCOPY
......................................................................
75
5.1.4.1 EVALUATION WITH NEGATIVE STAIN
EM......................................................................................76
5.1.4.1.1 M CFL DOES NOT SHOW A PH-DEPENDENT STRUCTURAL REARRANGEMENT
.............................
77
5.1.4.1.2 THE M CFL HYDROPHOBICITY PATTERN AND SECONDARY STRUCTURE
PREDICTIONS SUGGEST A
HELICAL
PORE.........................................................................................................................................
78
5.1.4.1.3 M CFL BINDS TO MEMBRANES - RECONSTITUTION INTO DIFFERENT
MEMBRANE SYSTEMS
(NANODISCS, LIPOSOMES,
CELL-GHOSTS)....................................................................................................80
5.1.4.2 EVALUATION WITH
CRYO-EM.........................................................................................................
84
5.1.4.2.1 VITRIFICATION OF M C
FL..........................................................................................................
84
5.1.4.2.2 PROCESSING AND STRUCTURE OF M C
FL....................................................................................86
5.1.5 DOES M CFL HAVE AN LNSP6 INDUCIBLE INTRINSIC CYSTEINE PROTEASE
DOMAIN
...................................
91
5.2 CLOSTRIDIUM DIFFICILE ENTEROTOXIN A (TCDA) & CYTOTOXIN B (TCDB)
............................................................
94
5.2.1 EVALUATION WITH NEGATIVE STAIN
EM................................................................................................
94
5.2.1.1 ACIDIC PH CAUSES A STRUCTURAL REARRANGEMENT FOR BOTH TOXINS,
TCDA AND TCDB
..............
95
5.2.1.2 RECONSTITUTION OF TCDA AND TCDB INTO LIPID
BILAYERS.............................................................97
5.2.1.2.1 CHOLESTEROL IS NOT NECESSARY FOR THE RECONSTITUTION OF TCDB
INTO LIPOSOMES AND
NANODISCS 98
5.2.1.2.2 TCDA REQUIRES CHOLESTEROL FOR THE INSERTION INTO LIPOSOMES
......................................
101
5.2.2 EVALUATION OF TCDA WITH
CRYO-EM.................................................................................................
102
5.2.2.1 VITRIFICATION, PROCESSING AND STRUCTURE OF
TCDA...................................................................102
5.2.2.1.1 AA BEING INVOLVED IN THE INTERACTION BETWEEN THE TCDA CORE-
AND CROPS-DOMAIN
107
5.3 STRUCTURAL COMPARISON OF M CFL AND
TCDA................................................................................................I
L L
5.4 COMPREHENSIVE
DISCUSSION........................................................................................................................
114
6
REFERENCES..........................................................................................................................................................
117
7
APPENDIX..............................................................................................................................................................130
7.1
CONSTRUCTS.......................................................................................................................................................130
7.1.1 M C
FL................................................................................................................................................130
7.1.1.1 568 PETL 9_6HIS_3C_MCFL Q439K PHOTO, LUM.
AKHURSTII.......................................................131
7.1.1.2 573 PET19 MCFL_3C_6HIS PHOTO, LUM.
AKHURSTII..................................................................132
7.1.1.3 1195 PETL 9_NHIS_MCF
1_837-1585_CYSPROT............................................................................132
7.1.1.4 1196 PETL 9_CHIS_MCF 1
_837-1585_CYSPROT............................................................................133
7.1.1.5 1221 PETL 9_NHIS_3C_MCF 1
_AA_1277-1585_CYSPROT.............................................................133
7.1.1.6 1222 PETL 9_CHIS_3C_MCF 1
_AA_1277-1585_CYSPROT.............................................................134
7.1.1.7 1223 PETL9_NHIS_3C_MCF 1
_AA_2275-2890...........................................................................134
7.1.1.8 1224 PETL9_CHIS_3C_MCF 1
_AA_2275-2890...........................................................................135
7.1.1.9 1446 PET19 MCFL_3C_STREPLL PHOTO, LUM.
AKHURSTII.............................................................135
7.1.1.10 1452 PETL 9_STREP_3C_MCFL Q439K PHOTO, LUM.
AKHURSTII.................................................136
7.1.1.11 1504 PETL9_6HIS_3C_MCFL Q439K PHOTO, LUM. AKHURSTII_C1397A
....................................
136
7.2 SECONDARY STRUCTURE PREDICTION OF M C
FL...................................................................................................137
7.3 HPLC-MS RAW DATA OF LIMITED PROTEOLYSIS
FRAGMENTS...........................................................................142
7.4 PROCESSING
COMMANDS................................................................................................................................
145
ACKNOWLEDGEMENT..................................................................................................................................................
147
PUBLICATIONS/CONFERENCE
CONTRIBUTIONS......................................................................................................
148
|
| adam_txt |
CONTENT
CONTENT.
1
I. LIST OF
ABBREVIATIONS.
1
1 ABSTRACT /
SUMMARY.
4
1.1
ABSTRACT.
4
1.2
ZUSAMMENFASSUNG.
5
2
INTRODUCTION.6
2.1 PHOTORHABDUS
LUMINESCENS.6
2.1.1 LIFE C
YCLE.6
2.1.2 PATHOGENESIS
MECHANISMS.
7
2.1.3 TOXINS OF PHOTORHABDUS
LUMINESCENS.
8
2.1.3.1 TOXIN COMPLEX
(TC)-TOXINS.
9
2.1.3.2 PHOTORHABDUS VIRULENCE CASSETTES
(PVCS).10
2.1.3.3 BINARY PHOTORHABDUS
TOXINS.
11
2.1.3.4 MAKES CATERPILLARS FLOPPY
(MCF)-TOXINS.11
2.2 CLOSTRIDIUM
DIFFICILE.
14
2.2.1 LARGE CLOSTRIDIAL GLYCOSYLATING
TOXINS.14
2.2.1.1 MECHANISM OF ACTION OF TCDA AND
TCDB.14
2.2.1.2 ARCHITECTURE AND STRUCTURE OF TCDA AND
TCDB.16
2.3 STRUCTURAL
ANALYSIS.19
2.3.1 ELECTRON MICROSCOPY ON BIOLOGICAL
SAMPLES.
20
2.3.1.1 RECENT DEVELOPMENTS AND THE RESOLUTION
REVOLUTION.23
2.3.1.1.1 VOLTA PHASE P LA TE
.
25
2.3.1.2 SINGLE PARTICLE
ANALYSIS.
26
3
MATERIALS.
29
3.1 DEVICES,
ACCESSORIES.
29
3.1.1 CHROMATOGRAPHY
COLUMNS.
30
3.2 CHEMICALS, SOLUTIONS,
CONSUMABLES.31
3.3 MEDIA,
BUFFERS.
32
3.4
KITSYSTEMS/SCREENS.
33
3.4.1 CRYSTALLIZATION
KITS/SCREENS.
33
3.5 ENZYMES,
ANTIBODIES.34
3.6
SOFTWARE.
34
4
METHODS.35
4.1 MOLECULAR-BIOLOGICAL & PROTEINBIOCHEMICAL
METHODS.
35
4.1.1 TRANSFORMATION OF CHEMICAL COM PETENT CELLS VIA
HEATSHOCK.35
4.1.2 EXPRESSION IN E. CO
LI.35
4.1.3 PROTEIN
PURIFICATION.
35
4.1.3.1 AFFINITY
CHROMATOGRAPHY.
36
4.1.3.2 SIZE EXCLUSION
CHROMATOGRAPHY.
36
4.1.3.3 LONEXCHANGE
CHROMATOGRAPHY.
37
4.1.4 VISUALIZATION VIA
SDS-PAGE.
37
4.1.5 WESTERN
BLOT.37
4.1.6 TRYPTIC IN-GEL DIGESTION & HPLC-MS-ANALYSIS OF DIGESTED PROTEINS
.
38
4.1.7 CONCENTRATION DETERMINATION OF PROTEINS VIA UV-ABSORPTION
.
38
4.1.8 PROTEIN STABILITY SCREEN
(NANODSF).
39
4.1.9 INSPOE-INDUCED AUTOCATALYTIC C
LEAVAGE.39
4.1.10 RECONSTITUTION OF PROTEINS INTO MEMBRANE SYSTEMS
.
42
4.1.10.1 NANODISCS AND
LIPOSOMES.
43
4.1.10.2 CELL
GHOSTS.
44
4.2 CELL BIOLOGICAL M
ETHODS.45
4.2.1 CELL
PROPAGATION.
45
4.2.1.1 INSECT
CELLS.45
4.2.1.2 MAMMALIAN
CELLS.
45
4.2.2 CELLTITER BLUE
ASSAY.
45
4.3 STRUCTURAL BIOLOGY
METHODS.
47
4.3.1 NEGATIVE STAIN ELECTRON M
ICROSCOPY.
47
4.3.1.1 SAMPLE
PREPARATION.47
4.3.1.2 DATA C
OLLECTION.
48
4.3.1.3 SINGLE PARTICLE ANALYSIS &
PROCESSING.
48
4.3.1.4 GOLD
LABELING.
49
4.3.2 ELECTRON
CRYO-MICROSCOPY.49
4.3.2.1 SAMPLE
PREPARATION.
49
4.3.2.1.1 PURE IC E
.
50
4.3.2.1.2 GRAPHENE
OXIDE.51
4.3.2.2 DATA C
OLLECTION.
51
4.3.2.2.1 M CFL ON FEI TITAN KRIOS WITH FALCON
II.51
4.3.2.2.2 M C FL, TCDA/TCDB ON FEI TITAN KRIOS WITH K2 SUMMIT, ENERGY
FILTER AND VOLTA PHASE
PLATE 52
4.3.2.3 SINGLE PARTICLE
ANALYSIS.
53
4.3.2.3.1
PRE-PROCESSING.54
4.3.2.3.2
PROCESSING.
55
4.3.2.4 STRUCTURE
ANALYSIS.57
4.3.3 PROTEIN
CRYSTALLOGRAPHY.57
4.3.3.1 PROTEIN
CONCENTRATION.
57
4.3.3.2 CRYSTALLIZATION ACCORDING TO
VAPOR-DIFFUSION.58
4.3.3.3 OPTIMIZATION OF CRYSTALLIZATION
CONDITIONS.
59
4.3.3.3.1 LIMITED
PROTEOLYSIS.
59
4.3.3.3.2 LYSINE
METHYLATION.
60
4.3.3.4 PROTEIN CRYSTAL CRYO
CONSERVATION.
61
5 RESULTS AND
DISCUSSION.
62
5.1 PHOTORHABDUS LUMINESCENS M CFL
TOXIN.
62
5.1.1 PROTEIN ISOLATION AFTER EXPRESSION IN E.
COLI.
62
5.1.1.1 ANALYSIS OF PROTEIN STABILITY IN VARIOUS BUFFER
CONDITIONS. 64
5.1.2 M CFL IS TOXIC TO INSECT AND MAMMALIAN
CELLS.66
5.1.2.1 EFFECT ON THE INSECT CELL LINES SF9, HIGH FIVE*, TNAO38 AND
DS2.66
5.1.2.2 EFFECT ON THE MAMMALIAN CELL LINE
HEK293.69
5.1.3 STRUCTURE DETERMINATION BY X-RAY
CRYSTALLOGRAPHY.70
5.1.3.1 LIMITED PROTEOLYSIS FOR RECEIVING STABLE PROTEIN FRAGMENTS
.
72
5.1.4 STRUCTURE DETERMINATION BY ELECTRON MICROSCOPY
.
75
5.1.4.1 EVALUATION WITH NEGATIVE STAIN
EM.76
5.1.4.1.1 M CFL DOES NOT SHOW A PH-DEPENDENT STRUCTURAL REARRANGEMENT
.
77
5.1.4.1.2 THE M CFL HYDROPHOBICITY PATTERN AND SECONDARY STRUCTURE
PREDICTIONS SUGGEST A
HELICAL
PORE.
78
5.1.4.1.3 M CFL BINDS TO MEMBRANES - RECONSTITUTION INTO DIFFERENT
MEMBRANE SYSTEMS
(NANODISCS, LIPOSOMES,
CELL-GHOSTS).80
5.1.4.2 EVALUATION WITH
CRYO-EM.
84
5.1.4.2.1 VITRIFICATION OF M C
FL.
84
5.1.4.2.2 PROCESSING AND STRUCTURE OF M C
FL.86
5.1.5 DOES M CFL HAVE AN LNSP6 INDUCIBLE INTRINSIC CYSTEINE PROTEASE
DOMAIN
.
91
5.2 CLOSTRIDIUM DIFFICILE ENTEROTOXIN A (TCDA) & CYTOTOXIN B (TCDB)
.
94
5.2.1 EVALUATION WITH NEGATIVE STAIN
EM.
94
5.2.1.1 ACIDIC PH CAUSES A STRUCTURAL REARRANGEMENT FOR BOTH TOXINS,
TCDA AND TCDB
.
95
5.2.1.2 RECONSTITUTION OF TCDA AND TCDB INTO LIPID
BILAYERS.97
5.2.1.2.1 CHOLESTEROL IS NOT NECESSARY FOR THE RECONSTITUTION OF TCDB
INTO LIPOSOMES AND
NANODISCS 98
5.2.1.2.2 TCDA REQUIRES CHOLESTEROL FOR THE INSERTION INTO LIPOSOMES
.
101
5.2.2 EVALUATION OF TCDA WITH
CRYO-EM.
102
5.2.2.1 VITRIFICATION, PROCESSING AND STRUCTURE OF
TCDA.102
5.2.2.1.1 AA BEING INVOLVED IN THE INTERACTION BETWEEN THE TCDA CORE-
AND CROPS-DOMAIN
107
5.3 STRUCTURAL COMPARISON OF M CFL AND
TCDA.I
L L
5.4 COMPREHENSIVE
DISCUSSION.
114
6
REFERENCES.
117
7
APPENDIX.130
7.1
CONSTRUCTS.130
7.1.1 M C
FL.130
7.1.1.1 568 PETL 9_6HIS_3C_MCFL Q439K PHOTO, LUM.
AKHURSTII.131
7.1.1.2 573 PET19 MCFL_3C_6HIS PHOTO, LUM.
AKHURSTII.132
7.1.1.3 1195 PETL 9_NHIS_MCF
1_837-1585_CYSPROT.132
7.1.1.4 1196 PETL 9_CHIS_MCF 1
_837-1585_CYSPROT.133
7.1.1.5 1221 PETL 9_NHIS_3C_MCF 1
_AA_1277-1585_CYSPROT.133
7.1.1.6 1222 PETL 9_CHIS_3C_MCF 1
_AA_1277-1585_CYSPROT.134
7.1.1.7 1223 PETL9_NHIS_3C_MCF 1
_AA_2275-2890.134
7.1.1.8 1224 PETL9_CHIS_3C_MCF 1
_AA_2275-2890.135
7.1.1.9 1446 PET19 MCFL_3C_STREPLL PHOTO, LUM.
AKHURSTII.135
7.1.1.10 1452 PETL 9_STREP_3C_MCFL Q439K PHOTO, LUM.
AKHURSTII.136
7.1.1.11 1504 PETL9_6HIS_3C_MCFL Q439K PHOTO, LUM. AKHURSTII_C1397A
.
136
7.2 SECONDARY STRUCTURE PREDICTION OF M C
FL.137
7.3 HPLC-MS RAW DATA OF LIMITED PROTEOLYSIS
FRAGMENTS.142
7.4 PROCESSING
COMMANDS.
145
ACKNOWLEDGEMENT.
147
PUBLICATIONS/CONFERENCE
CONTRIBUTIONS.
148 |
| any_adam_object | 1 |
| any_adam_object_boolean | 1 |
| author | Hagel, Philine 1989- |
| author_GND | (DE-588)1175005274 |
| author_facet | Hagel, Philine 1989- |
| author_role | aut |
| author_sort | Hagel, Philine 1989- |
| author_variant | p h ph |
| building | Verbundindex |
| bvnumber | BV046957237 |
| ctrlnum | (OCoLC)1220914438 (DE-599)DNB1176153064 |
| discipline | Biologie Medizin |
| discipline_str_mv | Biologie Medizin |
| format | Thesis Book |
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| genre | (DE-588)4113937-9 Hochschulschrift gnd-content |
| genre_facet | Hochschulschrift |
| id | DE-604.BV046957237 |
| illustrated | Illustrated |
| index_date | 2024-07-03T15:42:55Z |
| indexdate | 2024-07-10T08:58:34Z |
| institution | BVB |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-032365656 |
| oclc_num | 1220914438 |
| open_access_boolean | |
| owner | DE-355 DE-BY-UBR |
| owner_facet | DE-355 DE-BY-UBR |
| physical | 148 Seiten Illustrationen 21 cm |
| publishDate | 2018 |
| publishDateSearch | 2018 |
| publishDateSort | 2018 |
| record_format | marc |
| spelling | Hagel, Philine 1989- Verfasser (DE-588)1175005274 aut Structural insights into multidomain toxins - Mcf1 (P. Iuminescens) and TcdA&TcdB (C. difficile) submitted 2018 by Philine Nagel Dortmund [2018?] 148 Seiten Illustrationen 21 cm txt rdacontent n rdamedia nc rdacarrier Dissertation Technical University of Dortmund 2018 (DE-588)4113937-9 Hochschulschrift gnd-content B:DE-101 application/pdf http://d-nb.info/1176153064/04 Inhaltsverzeichnis DNB Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=032365656&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Hagel, Philine 1989- Structural insights into multidomain toxins - Mcf1 (P. Iuminescens) and TcdA&TcdB (C. difficile) |
| subject_GND | (DE-588)4113937-9 |
| title | Structural insights into multidomain toxins - Mcf1 (P. Iuminescens) and TcdA&TcdB (C. difficile) |
| title_auth | Structural insights into multidomain toxins - Mcf1 (P. Iuminescens) and TcdA&TcdB (C. difficile) |
| title_exact_search | Structural insights into multidomain toxins - Mcf1 (P. Iuminescens) and TcdA&TcdB (C. difficile) |
| title_exact_search_txtP | Structural insights into multidomain toxins - Mcf1 (P. Iuminescens) and TcdA&TcdB (C. difficile) |
| title_full | Structural insights into multidomain toxins - Mcf1 (P. Iuminescens) and TcdA&TcdB (C. difficile) submitted 2018 by Philine Nagel |
| title_fullStr | Structural insights into multidomain toxins - Mcf1 (P. Iuminescens) and TcdA&TcdB (C. difficile) submitted 2018 by Philine Nagel |
| title_full_unstemmed | Structural insights into multidomain toxins - Mcf1 (P. Iuminescens) and TcdA&TcdB (C. difficile) submitted 2018 by Philine Nagel |
| title_short | Structural insights into multidomain toxins - Mcf1 (P. Iuminescens) and TcdA&TcdB (C. difficile) |
| title_sort | structural insights into multidomain toxins mcf1 p iuminescens and tcda tcdb c difficile |
| topic_facet | Hochschulschrift |
| url | http://d-nb.info/1176153064/04 http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=032365656&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
| work_keys_str_mv | AT hagelphiline structuralinsightsintomultidomaintoxinsmcf1piuminescensandtcdatcdbcdifficile |
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