Molecular dynamics analyses of prion protein structures: the resistance to prion diseases Down Under
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| Sprache: | English |
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Singapore, Singapore
Springer
[2018]
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| Schriftenreihe: | Focus on structural biology
10 |
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| Beschreibung: | Bestellnummer: 86935473 |
| Beschreibung: | xxix, 375 Seiten Illustrationen, Diagramme 23.5 cm x 15.5 cm |
| ISBN: | 9789811088148 9811088144 |
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MARC
| LEADER | 00000nam a2200000 cb4500 | ||
|---|---|---|---|
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| 005 | 20180912 | ||
| 007 | t | ||
| 008 | 180619s2018 si a||| |||| 00||| eng d | ||
| 016 | 7 | |a 1152088920 |2 DE-101 | |
| 020 | |a 9789811088148 |c Book : circa EUR 149.79 (DE) (freier Preis), circa EUR 153.99 (AT) (freier Preis), circa CHF 154.00 (freier Preis) |9 978-981-10-8814-8 | ||
| 020 | |a 9811088144 |9 981-10-8814-4 | ||
| 024 | 3 | |a 9789811088148 | |
| 035 | |a (OCoLC)1050934954 | ||
| 035 | |a (DE-599)DNB1152088920 | ||
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| 084 | |a WD 5275 |0 (DE-625)148197: |2 rvk | ||
| 100 | 1 | |a Zhang, Jiapu |d 1971- |e Verfasser |0 (DE-588)1136047387 |4 aut | |
| 245 | 1 | 0 | |a Molecular dynamics analyses of prion protein structures |b the resistance to prion diseases Down Under |c Jiapu Zhang |
| 264 | 1 | |a Singapore, Singapore |b Springer |c [2018] | |
| 300 | |a xxix, 375 Seiten |b Illustrationen, Diagramme |c 23.5 cm x 15.5 cm | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b n |2 rdamedia | ||
| 338 | |b nc |2 rdacarrier | ||
| 490 | 1 | |a Focus on structural biology |v 10 | |
| 500 | |a Bestellnummer: 86935473 | ||
| 650 | 0 | 7 | |a Prionprotein |0 (DE-588)4619314-5 |2 gnd |9 rswk-swf |
| 650 | 0 | 7 | |a Molekülstruktur |0 (DE-588)4170383-2 |2 gnd |9 rswk-swf |
| 653 | |a Prion Protein Structure | ||
| 653 | |a Molecular Dynamics Simulation | ||
| 653 | |a Structural Dynamics | ||
| 653 | |a Molecular Structure | ||
| 653 | |a Prion Infection | ||
| 689 | 0 | 0 | |a Prionprotein |0 (DE-588)4619314-5 |D s |
| 689 | 0 | 1 | |a Molekülstruktur |0 (DE-588)4170383-2 |D s |
| 689 | 0 | |5 DE-604 | |
| 710 | 2 | |a Springer Malaysia Representative Office |0 (DE-588)1065365012 |4 pbl | |
| 776 | 0 | 8 | |i Erscheint auch als |n Online-Ausgabe |z 978-981-10-8815-5 |
| 830 | 0 | |a Focus on structural biology |v 10 |w (DE-604)BV014030722 |9 10 | |
| 856 | 4 | 2 | |m X:MVB |q text/html |u http://deposit.dnb.de/cgi-bin/dokserv?id=e232012d58a949a6bc7abf87be8427d3&prov=M&dok_var=1&dok_ext=htm |3 Inhaltstext |
| 856 | 4 | 2 | |m X:MVB |u http://www.springer.com/ |
| 856 | 4 | 2 | |m Digitalisierung UB Regensburg - ADAM Catalogue Enrichment |q application/pdf |u http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=030419565&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |3 Inhaltsverzeichnis |
| 999 | |a oai:aleph.bib-bvb.de:BVB01-030419565 | ||
Datensatz im Suchindex
| _version_ | 1804178631272955904 |
|---|---|
| adam_text | Contents
1 Basic Knowledge..................................................... 1
1.1 Molecular Dynamics (MD)..................................... 1
1.2 MD Simulation Methods .......................................... 5
1.2.1 Initialization......................................... 5
1.2.2 Heating the System..................................... 6
1.2.3 Equilibration.......................................... 7
1.2.4 Production Phase....................................... 7
1.3 MD Analysis Methods............................................ 8
1.4 Quantum Mechanics/Molecular Mechanics (QM/MM) ................. 10
1.5 Optimization Methods Used in MD, QM............................ 11
1.6 Protein, Prion Protein and Prion .............................. 12
Part I Prion Resistance Species
2 Rabbits: Wild-Type and Mutants...................................... 17
2.1 The Wild-Type NMR Structure (PDB Entry 2FJ3) .................. 17
2.1.1 MD at 300 K........................................... 17
2.1.2 MD at 350 K........................................... 21
2.1.3 MD at 450 K........................................... 27
2.2 The Wild-Type X-ray Structure (PDB Entry 3079)................. 30
2.2.1 MD at 300 K .......................................... 30
2.2.2 MD at 350 K .......................................... 31
2.2.3 MD at 450 K........................................... 34
2.2.4 A Concluding Remark................................... 36
2.3 The 1214V Mutant (NMR Structure PDB Entry 2JOM)................ 36
2.3.1 MD at 300 K........................................... 37
2.3.2 MD at 350 K .......................................... 38
2.3.3 MD at 450 K .......................................... 40
2.4 The S173N Mutant (NMR Structure PDB Entry 2JOH,
X-ray Structure PDB Entry 4HMM)............................. 43
2.4.1 MD at 300 K .......................................... 43
xvii
jçyiii Contents
2.4.2 MD at 350 K............................................. 46
2.4.3 MD at 450 K............................................. 50
2.5 The S170N Mutant (X-ray Structure PDB Entry 4HLS)................. 53
2.5.1 MD at 300K........................................... 54
2.5.2 MD at 350K........................................... 55
2.5.3 MD at 450 K............................................. 57
2.6 The S170N and S174N Mutants (X-ray Structure PDB
Entry 4HMR)................................................... 59
2.6.1 MD at 300 K.......................................... 59
2.6.2 MD at 350 K............................................. 61
2.6.3 MD at 450 K ............................................ 63
2.7 The Structure Without the Disulfide Bond (SS) (Homology
Structure).................................................... 64
3 Dogs: Wild-Type and D159N Mutant....................................... 67
3.1 The Wild-Type NMR Structure (PDB Entry 1XYK) ..................... 67
3.1.1 MD at 300 K ............................................ 67
3.1.2 MD at 350 K ............................................ 67
3.1.3 MD at 450 K.......................................... 71
3.2 The D159N Mutant (Homology Structure)............................. 73
3.2.1 MD at 300K............................................. 73
3.2.2 MD at 350 K............................................. 73
3.2.3 MD at 450K.............................................. 77
4 Horses, Buffaloes, and Pigs............................................... 81
4.1 Horse’s Wild-Type NMR Structure (PDB Entry 2KU4)............... 81
4.1.1 MD at 300 K ............................................ 81
4.1.2 MD at 350 K............................................. 83
4.1.3 MD at 450 K............................................. 85
4.2 Buffalo’s Homology Structure...................................... 87
4.2.1 MD at 300 K............................................. 87
4.2.2 MD at 350 K............................................. 87
4.2.3 MD at 450 K............................................. 91
4.3 Pig’s Wild-Type NMR Structure (PDB Entry 1XYQ).................... 93
4.3.1 MD at 300 K............................................. 93
4.3.2 MD at 350 K............................................ 93
4.3.3 MD at 450K............................................ 95
5 Chicken, Turtles, and Frogs............................................... 99
5.1 Chicken’s Wild-Type NMR Structure (PDB Entry 1U3M)................ 99
5.1.1 MD at 300 K........................................... 99
5.1.2 MD at 350K............................................. 101
5.1.3 MD at 450 K............................................ 103
5.2 Turtle’s Wild-Type NMR Structure (PDB Entry 1U5L)................ 105
5.2.1 MD at 300 K........................................... 105
5.2.2 MD at 350 K............................................ 107
Contents
xix
5.2.3 MD at 450 K.................................... 108
5.3 Frog’s Wild-Type NMR Structure (PDB Entry 1XU0)........... 111
5.3.1 MD at 300 K ..................................... 111
5.3.2 MD at 350 K ..................................... 113
5.3.3 MD at 450 K ..................................... 115
6 Other Species..................................................... 117
6.1 Syrian Hamster’s Wild-Type NMR Structure (PDB Entry IB 10) 117
6.2 Bovine.................................................... 117
6.2.1 The Wild-Type NMR Structure (PDB Entry 1DWY).. 117
6.2.2 The N-Terminal PrP(l-30) (PDB Entry 1SKH)...... 121
6.3 Sheep, Ovine, Ovis Aries.................................. 123
6.3.1 The Wild-Type X-ray Structure (PDB Entry 1UW3) .. 123
6.3.2 The Sheep Q168H Mutant (PDB Entry 1XYU)
at 300K in Low or Neutral pH Environments)..... 125
6.3.3 The Sheep PrPc(135-155) (PDB Entry 1S4T)......... 127
6.3.4 The Sheep PrPc(142—166) with Mutation
Y155A/R156A (PDB Entries 2RMV/W)................. 128
6.3.5 The Ovine Q168R Mutant (PDB Entry 1Y2S) at
300K in Low or Neutral pH Environments)........ 132
6.3.6 The Ovine H2H3 Domain (PDB Entry 2KTM)
at 300K in Low or Neutral pH Environments) .... 134
6.3.7 Ovis Aries....................................... 136
6.4 Cat’s Wild-Type NMR Structure (PDB Entry 1XYJ)............ 144
6.5 Doppel.................................................... 146
6.5.1 The Human Doppel Protein (PDB Entry 1LG4)........ 146
6.5.2 Mouse Doppel Proteins........................... 148
6.5.3 The Ovine Doppel Single Peptide 1—30 (PDB
Entry 2M1J)...................................... 150
Part II ß2-a2 Loop
7 Wild-Type Mouse 37 °C and 19.85 °C Structures .................. 155
7.1 The 37 °C (310.2 K) Structure (PDB Entry 2L39)............ 155
7.2 The 19.85 °C (293 K) Structure (PDB Entry 1AG2)........... 155
7.2.1 MD at 300 K...................................... 157
7.2.2 MD at 350 K ..................................... 158
7.2.3 MD at 450 K ..................................... 161
7.3 The 19.85 °C (293 K) Structure............................ 163
8 Mouse Mutants .................................................... 167
8.1 The V166A Mutant (PDB Entry 2KFO)......................... 167
8.2 The D167S Mutant at 20 °C (PDB Entry 2KU5)................ 169
8.3 The D167S-N173K Mutant (PDB Entry 2KU6)................ 171
8.4 The Y169G Mutant (PDB Entry 2L1D)......................... 173
8.5 The Y169A Mutant (PDB Entry 2L40)......................... 174
XX
Contents
8.6 The S170N Mutant (PDB Entry 2K50) ....................... 177
8.7 The S170N-N174T Mutant (PDB Entry 1Y16).................. 179
8.8 The N174T Mutant (PDB Entry 1Y15)........................ 180
8.9 The F175A Mutant (PDB Entry 2L1E)........................ 182
8.10 The Y225A-Y226A Mutant (PDB Entry 2KFM).................. 186
8.11 The Y169 A-Y225A-Y226A-20 °C Mutant (PDB Entry 2L1K) .. 188
9 Other Species with an Ordered /?2-a2 Loop ...................... 191
9.1 Bank Vale (Clethrionomys Glareolus) (PDB Entry 2K56)..... 191
9.2 Tammar Wallaby (Macropus Eugenii) (PDB Entry 2KFL)....... 191
9.3 Elk (PDB Entry 1XYW) at 300, 350, 450 K in Low or
Neutral pH Environment................................... 193
9.3.1 MD at 300 K .................................... 196
9.3.2 MD at 350 K..................................... 196
9.3.3 MD at 450 K .................................... 199
9.4 Rabbits ............................................... 202
9.4.1 NMR Structure (PDB Entry 2FJ3) at 300, 350,
450 K in Low pH or Neutral pH Environment
(Sect. 2.1)..................................... 202
9.4.2 X-ray Structure (PDB Entry 3079) at 300, 350,
450 K in Low or Neutral pH Environment (Sect. 2.2).. 202
9.5 Horse (PDB Entry 2KU4) at 300, 350, 450K in Low or
Neutral pH Environment (Sect. 4.1)....................... 202
9.6 Pig (PDB Entry 1XYQ) at 300, 350, 450K in Low or
Neutral pH Environment (Sect. 4.3)....................... 202
9.7 Syrian Hamsters (Sects. 6.1 and 10.10)................... 203
Part III Human Mutants
10 Human Mutants .................................................. 207
10.1 The PrP 226* (PDB Entry 5L6R).......................... 207
10.2 The R220K Mutant (PDB Entries 1E1U/W).................... 207
10.2.1 PDB Entry 1E1U................................. 209
10.2.2 PDB Entry 1E1W.................................. 211
10.3 The E219K Mutant (PDB Entry 2LFT)........................ 212
10.4 The Q212P Mutant (PDB Entry 2KUN)........................ 214
10.5 The V210I Mutant (PDB Entries 2LEJ/V1)................... 216
10.5.1 The pH 5.5 Structure (PDB Entry 2LEJ)........... 216
10.5.2 The pH 7.2 Structure (PDB Entry 2LV1)........... 218
10.6 The V209M Mutant (PDB Entry 2M8T)........................ 220
10.7 The E200K Mutant (PDB Entries 1FKC/07)................... 220
10.7.1 The PDB Entry 1FKC.............................. 222
10.7.2 The PDB Entry 1F07.............................. 223
10.8 The F198S Mutants...................................... 225
10.8.1 With M129 (PDB Entry 3HES)...................... 225
10.8.2 With V129 (PDB Entry 3HER)........................ 227
Contents
xxi
10.9 The Dl78N Mutants...................................... 228
10.9.1 The D178N Mutant (PDB Entry 3HEQ)............... 228
10.9.2 The D178N-M129V Mutant (PDB Entry 3HJX)
pH 7.0 Structure............................... 230
10.9.3 The D178N-M129V Mutant (PDB Entry 2K1D)
pH 4.6 Structure............................... 231
10.10 The S170N Mutant (PDB Entries 1E1P/S).................. 233
10.10.1 The PDB Entry 1E1P.............................. 233
10.10.2 The PDB Entry IE IS............................. 235
10.11 The M166C and E221C Mutant (PDB Entry 1 HOL)............ 236
10.12 The Ml66V Mutant (PDB Entries 1E1G/J)................... 238
10.12.1 PDB Entry 1E1G ................................. 238
10.12.2 PDB Entry 1E1J.................................. 240
10.13 The M129V Mutant (PDB Entry 3HAK)....................... 241
10.14 The G127V Mutant (PDB Entry 5 YJ4)...................... 243
11 Human PrPc Monomer, Dimer and Its M129V Mutant................ 245
11.1 Monomer................................................. 245
11.1.1 The Wild-Type pH 4.5 Structure (PDB Entry
1QLX/5YJ5) at 300, 350, 450K.................. 245
11.1.2 The Wild-Type pH 7.0 Structure (PDB Entry
1HJM/N) at 300 K............................... 252
11.2 Dimer................................................... 256
11.2.1 The Wild-Type Dimer (PDB Entry 114M) at 300 K.... 256
11.2.2 The Dimer M129V Mutant (PDB Entry 3HJ5) at
300 K in Neutral pH Environment............... 259
11.2.3 The Dimer M129V Mutant (PDB Entry 3HAF)
at 300 K in Neutral pH Environment............ 260
12 Human Peptides................................................. 263
12.1 The Peptide PrP( 180-195) (PDB Entry 21V4).............. 263
12.2 The Peptide PrP(173-195) (PDB Entry 2IV5)............... 263
12.3 The Peptide PrP(173-195) with D178N Mutation (PDB
Entry 2IV6)............................................. 266
12.4 The Peptide PrP(61-84) (PDB Entry lOEI)................. 267
12.4.1 The Peptide 61-68 (PDB Entry lOEH) ............. 269
12.5 The Peptide PrP(l 10-136) (PDB Entry 2LBG).............. 270
Part IV PrP Binding/Docking
13 PrP Bounded to Antibodies, Nanobody, RNA Aptamer, etc......... 273
13.1 PrPs Complexed with POM1 FAB [1-218(H), 1-213(L)]
(PDB Entries 4YX2, 4YXH, 4YXK, 4YXL, 4H88,4DGI)........ 273
13.1.1 Bovine PrP(136-236)............................. 273
13.1.2 Deer PrP(l 17-217).............................. 274
13.1.3 Elk PrP( 122-222)............................... 275
xxii Contents
13.1.4 Syrian Hamster PrP(l23-225)........................ 276
13.1.5 Mouse PrP( 124-225)................................ 277
13.1.6 Human PrP(126-222)................................. 278
13.2 Human PrP Bound to a Nanobody............................ 279
13.2.1 PrP(l 17-225) (P) with Nanobody [1—123(B)]
(PDB Entry 4KML)................................... 279
13.2.2 PrP(l 18-224) (P) with Nanobody [1-124(B)]
(PDB Entry 4N90) .................................. 280
13.3 Human PrP(125-223) Bound to ICSM 18 FAB [1—215(H),
1-212(L)] (PDB Entry 2W9E) ............................... 281
13.4 Mouse PrP Bound to Phenothiazine Compounds............... 283
13.4.1 Mouse PrP( 119-228) Bound to Promazine
[1-218(H), 1-213(L)] (PDB Entry 4MA7).............. 283
13.4.2 Mouse PrP(l 19—226) Bound to Chlorpromazine
[1-218(H), 1—213(L)] (PDB Entry 4MA8)............ 284
13.5 Syrian Hamster PrP(125—228) Bound to Thiamine
(PDB Entry 2LH8)............................................ 285
13.6 Ovine PrP(127—228) Variants Complexed with VRQ14
FAB [1—223(B), 1-214(C)] (PDB Entries 1TPX, 1TQB, 1TQC) 286
13.6.1 ARQ................................................ 286
13.6.2 VRQ.............................................. 287
13.6.3 ARR................................................ 288
13.7 Bindings in PrP Unstructured Regions....................... 289
13.7.1 Syrian Hamster PrP104-l 13(P) Complexed with
FAB 3F4 [3-213(H), 1—214(E)] (PDB Entry 1CU4) .. 289
13.7.2 Octapeptide Repeat 1-9(1) 1-8(J) Complexed
with POM2 FAB (PDB Entry 4J8R)..................... 290
13.7.3 Bovine PrP Bound to RNA Aptamer R12 (PDB
Entries 2RU7, 2RSK, 2RQJ).......................... 291
13.7.4 PrP(57—91) Octarepeats Bound with PPS
(Pentosan Polysulfate) (PDB Entry 2KKG)............ 295
13.8 Mouse PrP(125-224) Complexed with POM6 FAB [1-214
(H), 1—216(L)] (PDB Entry 6AQ7)........................... 295
14 Potential Antiprion Drugs......................................... 297
14.1 A List of Drugs Tested for Prion Diseases................ 297
14.2 Optimize Some Drugs by QM Density Functional Theory...... 297
14.2.1 Chlorpromazine (Drug Bank ID DB00477).............. 297
14.2.2 Doxycycline (Drug Bank ID DB00254)................. 298
14.2.3 GN8................................................ 299
Part V Prion Peptides with Cross-/! Structures
15 Mathematical Formulas for All PrP Peptides’ Cross-/? Structures ... 307
15.1 A Table of All PrP Peptides with Cross-/! Structures....... 307
15.2 Human PrP(126-131) (PDB Entries 4TUT, 4TBY/Z).............. 307
Contents xxiii
15.3 Human PrP(126-132) (PDB Entries 4W5L/M/P)................. 311
15.4 Human PrP(127-133) (PDB Entries 4W5Y, 4W67, 4W71)......... 314
15.5 Human PrP(127-132) (PDB Entries 4WBU/V, 3MD4/5,
3NHC/D).................................................. 316
15.6 Mouse PrP(137-142) (PDB Entry 3NVG)....................... 321
15.7 Mouse PrP(137-143) (PDB Entry 3NVH)....................... 322
15.8 PrP(138—143) ........................................... 323
15.8.1 Syrian Hamster (PDB Entry 3NVE)................. 323
15.8.2 Human (PDB Entry 3NVF) ......................... 324
15.9 Sheep PrP( 142-166) (1G04)................................ 325
15.10 PrP(168-176): Bank Vole.................................. 326
15.10.1 PDB Entry 6AXZ................................. 326
15.10.2 PDB Entry 6BTK................................. 327
15.11 PrP(170-175) ............................................. 329
15.11.1 Human (PDB Entry 20L9)........................... 329
15.11.2 Elk (PDB Entry 3FVA)............................. 330
15.11.3 Human PrP(169-175) GSNQNNF (PDB Entries
6CLC/D/E/F/G/H/I/J/K/L/M/N/0/P/Q/R/S/T).......... 331
15.12 Human PrP(177-182, 211-216) (PDB Entries 4E1I/H).......... 331
15.13 A Concluding Remark....................................... 331
15.14 QM Informatics for the PrP(l 13-120) AGAAAAGA Peptide ... 333
15.14.1 Single Point (sp) (Energy) Calculation Results .. 333
15.14.2 Optimization (opt) Calculation Results........... 334
15.14.3 Frequency (freq) IR/Raman Calculation Results... 335
15.14.4 PES Scan Calculation Results.................... 338
15.14.5 Stability (stable) Calculation Results........... 340
15.14.6 NMR Calculation Results.......................... 340
15.14.7 HOMO Cube(orbital, 30) Calculation Results....... 341
15.14.8 Molecular Property
Pop = Full/Hirshfeld/MK/NBO/Req
Calculations Results ............................ 341
15.14.9 The AGAAAAGA.pdb that Passed the Opt Calculation 342
16 Hydrogen Bonds Between Two Optimized Fundamental
Chains of Each Model............................................. 347
16.1 Optimize Each Model with the Two Fundamental Chains...... 347
16.2 The Hydrogen Bonds Between the Two Chains................. 347
16.3 A List of Residues in the /J-Sheet of All PiPc Species.... 348
References........................................................... 355
Index
369
|
| any_adam_object | 1 |
| author | Zhang, Jiapu 1971- |
| author_GND | (DE-588)1136047387 |
| author_facet | Zhang, Jiapu 1971- |
| author_role | aut |
| author_sort | Zhang, Jiapu 1971- |
| author_variant | j z jz |
| building | Verbundindex |
| bvnumber | BV045027712 |
| classification_rvk | WD 5100 WD 5275 |
| ctrlnum | (OCoLC)1050934954 (DE-599)DNB1152088920 |
| discipline | Biologie |
| format | Book |
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| id | DE-604.BV045027712 |
| illustrated | Illustrated |
| indexdate | 2024-07-10T08:07:02Z |
| institution | BVB |
| institution_GND | (DE-588)1065365012 |
| isbn | 9789811088148 9811088144 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-030419565 |
| oclc_num | 1050934954 |
| open_access_boolean | |
| owner | DE-355 DE-BY-UBR DE-11 |
| owner_facet | DE-355 DE-BY-UBR DE-11 |
| physical | xxix, 375 Seiten Illustrationen, Diagramme 23.5 cm x 15.5 cm |
| publishDate | 2018 |
| publishDateSearch | 2018 |
| publishDateSort | 2018 |
| publisher | Springer |
| record_format | marc |
| series | Focus on structural biology |
| series2 | Focus on structural biology |
| spelling | Zhang, Jiapu 1971- Verfasser (DE-588)1136047387 aut Molecular dynamics analyses of prion protein structures the resistance to prion diseases Down Under Jiapu Zhang Singapore, Singapore Springer [2018] xxix, 375 Seiten Illustrationen, Diagramme 23.5 cm x 15.5 cm txt rdacontent n rdamedia nc rdacarrier Focus on structural biology 10 Bestellnummer: 86935473 Prionprotein (DE-588)4619314-5 gnd rswk-swf Molekülstruktur (DE-588)4170383-2 gnd rswk-swf Prion Protein Structure Molecular Dynamics Simulation Structural Dynamics Molecular Structure Prion Infection Prionprotein (DE-588)4619314-5 s Molekülstruktur (DE-588)4170383-2 s DE-604 Springer Malaysia Representative Office (DE-588)1065365012 pbl Erscheint auch als Online-Ausgabe 978-981-10-8815-5 Focus on structural biology 10 (DE-604)BV014030722 10 X:MVB text/html http://deposit.dnb.de/cgi-bin/dokserv?id=e232012d58a949a6bc7abf87be8427d3&prov=M&dok_var=1&dok_ext=htm Inhaltstext X:MVB http://www.springer.com/ Digitalisierung UB Regensburg - ADAM Catalogue Enrichment application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=030419565&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Zhang, Jiapu 1971- Molecular dynamics analyses of prion protein structures the resistance to prion diseases Down Under Focus on structural biology Prionprotein (DE-588)4619314-5 gnd Molekülstruktur (DE-588)4170383-2 gnd |
| subject_GND | (DE-588)4619314-5 (DE-588)4170383-2 |
| title | Molecular dynamics analyses of prion protein structures the resistance to prion diseases Down Under |
| title_auth | Molecular dynamics analyses of prion protein structures the resistance to prion diseases Down Under |
| title_exact_search | Molecular dynamics analyses of prion protein structures the resistance to prion diseases Down Under |
| title_full | Molecular dynamics analyses of prion protein structures the resistance to prion diseases Down Under Jiapu Zhang |
| title_fullStr | Molecular dynamics analyses of prion protein structures the resistance to prion diseases Down Under Jiapu Zhang |
| title_full_unstemmed | Molecular dynamics analyses of prion protein structures the resistance to prion diseases Down Under Jiapu Zhang |
| title_short | Molecular dynamics analyses of prion protein structures |
| title_sort | molecular dynamics analyses of prion protein structures the resistance to prion diseases down under |
| title_sub | the resistance to prion diseases Down Under |
| topic | Prionprotein (DE-588)4619314-5 gnd Molekülstruktur (DE-588)4170383-2 gnd |
| topic_facet | Prionprotein Molekülstruktur |
| url | http://deposit.dnb.de/cgi-bin/dokserv?id=e232012d58a949a6bc7abf87be8427d3&prov=M&dok_var=1&dok_ext=htm http://www.springer.com/ http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=030419565&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
| volume_link | (DE-604)BV014030722 |
| work_keys_str_mv | AT zhangjiapu moleculardynamicsanalysesofprionproteinstructurestheresistancetopriondiseasesdownunder AT springermalaysiarepresentativeoffice moleculardynamicsanalysesofprionproteinstructurestheresistancetopriondiseasesdownunder |