Protein folding and misfolding: shining light by infrared spectroscopy
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| Weitere Verfasser: | |
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| Format: | Buch |
| Sprache: | English |
| Veröffentlicht: |
Heidelberg [u.a.]
Springer
2012
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| Schriftenreihe: | Biological and medical physics, biomedical engineering
|
| Schlagworte: | |
| Online-Zugang: | Inhaltstext Inhaltsverzeichnis |
| Beschreibung: | Hergestellt on demand. - Literaturangaben |
| Beschreibung: | XVI, 244 S. Ill., graph. Darst. 24 cm |
| ISBN: | 9783642222290 3642222293 |
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Datensatz im Suchindex
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IMAGE 1
CONTENTS
1 LINKED LANDSCAPES AND CONFORMATIONAL CONVERSIONS: HOW PROTEINS FOLD
AND MISFOLD 1
GARETH J. MORGAN AND SHEENA E. RADFORD 1.1 INTRODUCTION 1
1.2 THE UNFOLDED ENSEMBLE UNDER NATIVE CONDITIONS 4
1.3 FOLDING AND MISFOLDING INTERMEDIATES 6
1.4 PROTOFIBRILS, OLIGOMERS AND TOXICITY 8
1.5 AMYLOID STRUCTURE 9
1.6 FROM THE TEST TUBE TO THE CELL 11
1.7 CONCLUSIONS 13
REFERENCES 13
2 A QUANTITATIVE RECONSTRUCTION OF THE AMIDE I CONTOUR IN THE IR SPECTRA
OF PEPTIDES AND PROTEINS: FROM STRUCTURE TO SPECTRUM 17
JOSEPH W. BRAUNER AND RICHARD MENDELSOHN 2.1 THE APPROACH TO SIMULATION
OF THE AMIDE I CONTOUR 17
2.1.1 INTRODUCTION 17
2.1.2 HISTORICAL BACKGROUND 18
2.1.3 NORMAL COORDINATE CALCULATIONS 19
2.1.4 AB INITIO FORCE FIELD CALCULATIONS 20
2.1.5 THE MODIFIED GF MATRIX METHOD 21
2.1.6 CONSTRUCTING THE G AND F MATRICES IN THE COUPLED OSCILLATORS OF
ONE KIND METHOD 22
2.1.7 SIMULATING THE AMIDE I CONTOUR 31
2.2 APPLICATIONS 32
2.2.1 ISOTOPIC LABELING 33
2.2.2 MODELING THE EARLY STAGES OF THERMAL DENATURATION 39 2.2.3 AMIDE I
STRUCTURE-FREQUENCY CORRELATIONS IN GLOBULAR PROTEINS 41
2.2.4 IRRAS SIMULATIONS 45
BIBLIOGRAFISCHE INFORMATIONEN HTTP://D-NB.INFO/1012462617
DIGITALISIERT DURCH
IMAGE 2
CONTENTS
2.3 CONCLUSIONS AND FUTURE PROSPECTS 50
REFERENCES 51
MILLISECOND-TO-MINUTE PROTEIN FOLDING/MISFOLDING EVENTS MONITORED BY
FTIR SPECTROSCOPY 53
HEINZ FABIAN AND DIETER NAUMANN 3.1 GENERAL CONSIDERATIONS 53
3.2 FTIR SPECTROSCOPY, EXPERIMENTAL ASPECTS 55
3.2.1 PROTEINS IN AQUEOUS SOLUTIONS 55
3.2.2 MEASUREMENTS IN D2 O 56
3.2.3 FTIR SPECTRA OF CHEMICAL DENATURANTS 60
3.3 KINETIC FTIR EXPERIMENTS APPLYING RAPID MIXING AND TEMPERATURE-JUMP
APPROACHES 61
3.3.1 RAPID-SCAN FTIR SPECTROSCOPY: ADVANTAGES AND LIMITATIONS 61
3.3.2 DESIGN AND OPERATION OF A STOPPED-FLOW APPARATUS FOR MEASUREMENTS
IN HEAVY WATER 62
3.3.3 A STOPPED-FLOW APPARATUS FOR MEASUREMENTS OF H2 O-PROTEIN
SOLUTIONS 63
3.3.4 T-JUMP EXPERIMENTS IN HEAVY WATER 64
3.4 EXAMPLES OF APPLYING T-JUMPS ONTO A PROTEIN SOLUTION 66 3.4.1
REFOLDING OF WILD-TYPE RIBONUCLEASE TL AND SOME OF ITS MUTANTS 66
3.4.2 UNFOLDING OF THE A-CRO REPRESSOR 72
3.5 EXAMPLES MAKING USE OF RAPID-MIXING METHODS 74
3.5.1 REFOLDING OF A-LACTALBUMIN STUDIED BY STOPPED-FLOW INFRARED
SPECTROSCOPY AFTER A PH-JUMP 74
3.5.2 MISFOLDING OF SS2-MICROGLOBULIN 78
3.5.3 THE A-TO-/J CONVERSION PROCESS OF THE PRION PROTEIN 85 REFERENCES
87
WATCHING DYNAMICAL EVENTS IN PROTEIN FOLDING IN THE TIME DOMAIN FROM
SUBMILLISECONDS TO SECONDS: CONTINUOUS-FLOW RAPID-MIXING INFRARED
SPECTROSCOPY 91 SATOSHI TAKAHASHI AND TETSUNARI KIMURA 4.1 INTRODUCTION
91
4.2 THE COLLAPSE AND SEARCH MECHANISM OF PROTEIN FOLDING 92 4.2.1 THE
PROTEIN FOLDING MECHANISM DEPENDS ON THE CHAIN LENGTH 92
4.2.2 KINETIC INVESTIGATION OF PROTEIN FOLDING FOR INTERMEDIATE PROTEINS
93
4.3 DEVELOPMENT OF CONTINUOUS-FLOW TIME-RESOLVED INFRARED SPECTROMETER
94
4.3.1 COMPARISON OF DIFFERENT METHODS FOR TRIGGERING PROTEIN FOLDING
EVENTS 94
IMAGE 3
CONTENTS XI
4.3.2 DEVELOPMENT OF A CONTINUOUS-FLOW CELL WITH A T-SHAPED FLOW CHANNEL
95
4.3.3 CONSTRUCTION OF THE TIME-RESOLVED SPECTROMETER BASED ON INFRARED
MICROSCOPY 98
4.4 PRACTICAL ISSUES FOR KINETIC INFRARED INVESTIGATIONS OF PROTEIN
FOLDING 101
4.4.1 SELECTION OF THE INITIAL UNFOLDED STATE 101
4.4.2 SUPPRESSION OF THE AGGREGATE FORMATION 101
4.4.3 METHOD OF SPECTRAL ANALYSIS 102
4.5 APPLICATION TO PROTEIN FOLDING 103
4.5.1 PIONEERING INVESTIGATIONS OF RAPID-MIXING INFRARED SPECTROSCOPY
103
4.5.2 APOMYOGLOBIN 104
4.5.3 SINGLE-CHAIN MONELLIN 107
4.6 SUMMARY AND PERSPECTIVE 110
REFERENCES 113
5 HIGH-PRESSURE VIBRATIONAL SPECTROSCOPY STUDIES OF THE FOLDING,
MISFOLDING AND AMYLOIDOGENESIS OF PROTEINS 117 ROLAND WINTER, MATTHIAS
PIIHSE, AND JONAS MARKGRAF 5.1 INTRODUCTION TO HIGH-PRESSURE BIOSCIENCE
117
5.2 FUNDAMENTAL CONCEPTS: STABILITY DIAGRAM OF PROTEINS 119 5.3
EXPERIMENTAL METHODS 120
5.3.1 HIGH-PRESSURE FTIR SPECTROSCOPY 120
5.3.2 DIAMOND ANVIL CELL TECHNOLOGY 122
5.3.3 PRESSURE CALIBRANTS FOR INFRARED SPECTROSCOPY 123 5.4 EXAMPLES OF
PRESSURE STUDIES ON PROTEINS AND POLYMERS 124 5.4.1 PRESSURE-INDUCED
PROTEIN UN-AND REFOLDING REACTIONS 124
5.4.2 PROTEIN FOLDING KINETICS 127
5.4.3 PRESSURE-ASSISTED COLD DENATURATION OF PROTEINS 130 5.4.4 PRESSURE
EFFECTS ON OLIGOMERIC PROTEINS AND CHAPERONES 132 5.4.5 COSOLVENT
EFFECTS 133
5.4.6 AGGREGATION/FIBRILLATION REACTIONS OF PROTEINS 135 5.4.7 ENZYMATIC
REACTIONS 138
5.4.8 SYNTHETIC POLYMERS AS PROTEIN MIMETICS 139
5.5 CONCLUSIONS AND OUTLOOK 143
REFERENCES 144
6 DYNAMICS OF A-HELIX AND SS-SHEET FORMATION STUDIED BY LASER-INDUCED
TEMPERATURE-JUMP IR SPECTROSCOPY 147 KARIN HAUSER 6.1 PEPTIDE FOLDING
DYNAMICS 147
6.1.1 SECONDARY-STRUCTURE FORMATION 147
6.1.2 THE AMIDE I BAND AS STRUCTURAL PROBE 148
6.1.3 EQUILIBRIUM VS. KINETIC DATA 149
6.1.4 RATE CONSTANTS 150
IMAGE 4
XII CONTENTS
6.2 LASER-INDUCED T-JUMP TECHNIQUE 151
6.2.1 GENERATION OF THE HEATING PULSE 152
6.2.2 PHOTO-ACOUSTIC EFFECTS, CAVITATION AND THERMAL LENSING 156 6.2.3
EXPERIMENTAL SETUP 157
6.3 T-JUMP RELAXATION KINETICS 158
6.3.1 TWO-STATE AND MULTISTATE FOLDERS 158
6.3.2 HELIX DYNAMICS 161
6.3.3 HAIRPIN FORMATION 161
6.4 SITE-SPECIFIC DYNAMICS WITH ISOTOPIC EDITING 162
6.4.1 SITE-SPECIFIC FREQUENCY SHIFTS 162
6.4.2 INSIGHTS INTO FOLDING MECHANISMS ON THE RESIDUE LEVEL 163 6.4.3
SINGLE AND MULTIPLE ISOTOPE LABELS 166
REFERENCES 168
7 LIGHT-TRIGGERED PEPTIDE DYNAMICS 171
WOLFGANG ZINTH AND JOSEF WACHTVEITL 7.1 INTRODUCTION 171
7.2 LIGHT-TRIGGERED PEPTIDES 172
7.2.1 THE PHOTOCHROMIC SWITCHING UNIT 172
7.2.2 THE LINKING GROUP 175
7.2.3 THE PEPTIDE MOIETY 177
7.3 CHARACTERIZATION OF LIGHT-TRIGGERED PEPTIDES BY STATIONARY
SPECTROSCOPY 177
7.4 METHODS FOR THE STUDY OF ULTRAFAST STRUCTURAL DYNAMICS 180 7.5
APPLICATIONS 183
7.5.1 ULTRAFAST SPECTROSCOPY ON CYCLIC AZOBENZENE PEPTIDES 183 7.5.2
UNFOLDING AND FOLDING OF A LIGHT SWITCHABLE HAIRPIN MODEL COMPOUND 184
7.5.3 TOWARD LIGHT SWITCHABLE TERTIARY STRUCTURES: (I) AZO-MAQUETTES 185
7.5.4 TOWARD LIGHT SWITCHABLE TERTIARY STRUCTURES: (II) AZO-COLLAGENS
187
7.6 CONCLUSION 190
REFERENCES 191
8 TIME-RESOLVED FTIR SPECTROSCOPY OF PH-INDUCED AGGREGATION OF PEPTIDES
193
JOHN E.T. CORRIE, ALEX PERALVAREZ-MARIN, AND ANDREAS BARTH 8.1
INTRODUCTION TO INFRARED DIFFERENCE SPECTROSCOPY 193
8.1.1 PRINCIPLES 193
8.1.2 TRIGGERING PROTEIN REACTIONS 194
8.1.3 INTERPRETING DIFFERENCE SPECTRA 196
8.2 CAGED COMPOUNDS 198
8.2.1 INTRODUCTION TO CAGED COMPOUNDS 198
8.2.2 CAGED PROTONS 202
8.2.3 DIFFERENCE SPECTRUM OF CAGED SULFATE PHOTOLYSIS 204
IMAGE 5
CONTENTS XIII
8.3 ACIDIFICATION-INDUCED UNFOLDING OF MYOGLOBIN 206
8.4 ACIDIFICATION-INDUCED AGGREGATION OF THE ALZHEIMER'S PEPTIDE 207
8.4.1 INTRODUCTION TO THE ALZHEIMER'S PEPTIDE 207
8.4.2 TIME-RESOLVED INFRARED DIFFERENCE SPECTROSCOPY OF THE AGGREGATION
OF THE ALZHEIMER'S PEPTIDE 208 8.5 OUTLOOK 212
REFERENCES 213
9 EXAMINING AMYLOID STRUCTURE AND KINETICS WITH ID AND 2D INFRARED
SPECTROSCOPY AND ISOTOPE LABELING 217 LAUREN E. BUCHANAN, EMILY B.
DUNKELBERGER, AND MARTIN T. ZANNI 9.1 INTRODUCTION 217
9.2 VIBRATIONAL MODES OF AMYLOIDS 220
9.3 ISOTOPE LABELING SCHEMES 225
9.4 VIBRATIONAL DYNAMICS OF AMYLOIDS 228
9.5 EXPERIMENTAL METHODS 229
9.6 EXPERIMENTAL DATA 230
9.7 SUMMARY 236
REFERENCES 236
INDEX 239 |
| any_adam_object | 1 |
| author2 | Fabian, Heinz |
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| dewey-ones | 572 - Biochemistry |
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| dewey-tens | 570 - Biology |
| discipline | Biologie |
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| spelling | Protein folding and misfolding shining light by infrared spectroscopy Heinz Fabian ... eds. Heidelberg [u.a.] Springer 2012 XVI, 244 S. Ill., graph. Darst. 24 cm txt rdacontent n rdamedia nc rdacarrier Biological and medical physics, biomedical engineering Hergestellt on demand. - Literaturangaben Zeitauflösung (DE-588)4245662-9 gnd rswk-swf Proteinfaltung (DE-588)4324567-5 gnd rswk-swf Konformationsänderung (DE-588)4164966-7 gnd rswk-swf Infrarotspektroskopie (DE-588)4135411-4 gnd rswk-swf (DE-588)4143413-4 Aufsatzsammlung gnd-content Proteinfaltung (DE-588)4324567-5 s Konformationsänderung (DE-588)4164966-7 s Infrarotspektroskopie (DE-588)4135411-4 s Zeitauflösung (DE-588)4245662-9 s DE-604 Fabian, Heinz edt Erscheint auch als Online-Ausgabe Protein Folding and Misfolding X:MVB text/html http://deposit.dnb.de/cgi-bin/dokserv?id=3835633&prov=M&dok_var=1&dok_ext=htm Inhaltstext DNB Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=025163062&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Protein folding and misfolding shining light by infrared spectroscopy Zeitauflösung (DE-588)4245662-9 gnd Proteinfaltung (DE-588)4324567-5 gnd Konformationsänderung (DE-588)4164966-7 gnd Infrarotspektroskopie (DE-588)4135411-4 gnd |
| subject_GND | (DE-588)4245662-9 (DE-588)4324567-5 (DE-588)4164966-7 (DE-588)4135411-4 (DE-588)4143413-4 |
| title | Protein folding and misfolding shining light by infrared spectroscopy |
| title_auth | Protein folding and misfolding shining light by infrared spectroscopy |
| title_exact_search | Protein folding and misfolding shining light by infrared spectroscopy |
| title_full | Protein folding and misfolding shining light by infrared spectroscopy Heinz Fabian ... eds. |
| title_fullStr | Protein folding and misfolding shining light by infrared spectroscopy Heinz Fabian ... eds. |
| title_full_unstemmed | Protein folding and misfolding shining light by infrared spectroscopy Heinz Fabian ... eds. |
| title_short | Protein folding and misfolding |
| title_sort | protein folding and misfolding shining light by infrared spectroscopy |
| title_sub | shining light by infrared spectroscopy |
| topic | Zeitauflösung (DE-588)4245662-9 gnd Proteinfaltung (DE-588)4324567-5 gnd Konformationsänderung (DE-588)4164966-7 gnd Infrarotspektroskopie (DE-588)4135411-4 gnd |
| topic_facet | Zeitauflösung Proteinfaltung Konformationsänderung Infrarotspektroskopie Aufsatzsammlung |
| url | http://deposit.dnb.de/cgi-bin/dokserv?id=3835633&prov=M&dok_var=1&dok_ext=htm http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=025163062&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
| work_keys_str_mv | AT fabianheinz proteinfoldingandmisfoldingshininglightbyinfraredspectroscopy |