Physical methods to characterize pharmaceutical proteins
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| Format: | Buch |
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| Sprache: | English |
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New York [u.a.]
Plenum Press
1995
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| Schriftenreihe: | Pharmaceutical biotechnology
7 |
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| 245 | 1 | 0 | |a Physical methods to characterize pharmaceutical proteins |c ed. by James N. Herron ... |
| 264 | 1 | |a New York [u.a.] |b Plenum Press |c 1995 | |
| 300 | |a XVII, 362 S. |b graph. Darst. | ||
| 336 | |b txt |2 rdacontent | ||
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| 490 | 1 | |a Pharmaceutical biotechnology |v 7 | |
| 650 | 4 | |a Drugs - Chemical analysis | |
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| 650 | 7 | |a Geneesmiddelen |2 gtt | |
| 650 | 7 | |a Wetenschappelijke technieken |2 gtt | |
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| 650 | 4 | |a Biopharmaceutics |x methods | |
| 650 | 4 | |a Chemistry, Pharmaceutical |x methods | |
| 650 | 4 | |a Molecular Structure | |
| 650 | 4 | |a Protein drugs |x Analysis | |
| 650 | 4 | |a Proteins |x chemistry | |
| 700 | 1 | |a Herron, James N. |e Sonstige |4 oth | |
| 830 | 0 | |a Pharmaceutical biotechnology |v 7 |w (DE-604)BV007730074 |9 7 | |
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Datensatz im Suchindex
| _version_ | 1819771962891698176 |
|---|---|
| adam_text | PHYSICAL METHODS TO CHARACTERIZE PHARMACEUTICAL PROTEINS EDITED BY JAMES
N. HERRON UNIVERSITY OF UTAH SALT LAKE CITY; UTAH WIM JISKOOT NATIONAL
INSTITUTE OF PUBLIC HEALTH AND ENVIRONMENTAL PROTECTION BILTHOVEN. THE
NETHERLANDS AND DAAN J. A. CROMMELIN UTRECHT UNIVERSITY, AND UTRECHT
INSTITUTE FOR PHARMACEUTICAL SCIENCES GRONINGEN-UTRECHT INSTITUTE FOR
DRUG EXPLORATION UTRECHT, THE NETHERLANDS PLENUM PRESS * NEW YORK AND
LONDON CONTENTS CHAPTER 1 APPLICATION OF FLUORESCENCE SPECTROSCOPY FOR
DETERMINING THE STRUCTURE AND FUNCTION OF PROTEINS WIM JISKOOT, VLADIMIR
HLADY, JOHN J. NALEWAY, AND JAMES N. HERRON 1. INTRODUCTION 1 2.
TECHNIQUES 5 2.1. SPECTRAL MEASUREMENTS 5 2.2. QUANTUM YIELD OF
FLUORESCENCE 11 2.3. FLUORESCENCE LIFETIMES 11 2.4. QUENCHING OF
FLUORESCENCE 15 2.5. ANISOTROPY 17 2.6. ENERGY TRANSFER 21 2.7.
INTERFACIAL FLUORESCENCE SPECTROSCOPY 24 3. PROTEIN FLUORESCENCE 27 3.1.
INTRINSIC FLUORESCENCE 28 3.2. EXTRINSIC FLUOROPHORES 32 4. APPLICATIONS
35 4.1. PROTEIN FOLDING 35 4.2. PROTEIN DYNAMICS 36 4.3. LIGAND BINDING
38 4.4. ENZYME KINETICS 42 4.5. INTERFACIAL PROTEIN STUDIES 48 5.
CONCLUSIONS 51 REFERENCES 53 XII CONTENTS CHAPTER 2 STRUCTURAL
INFORMATION ON PROTEINS FROM CIRCULAR DICHROISM SPECTROSCOPY:
POSSIBILITIES AND LIMITATIONS MICHAEL BLOEMENDAL AND W. CURTIS JOHNSON,
JR. 1. INTRODUCTION 65 2. WHAT IS CIRCULAR DICHROISM? 66 2.1. GENERAL
CONSIDERATIONS AND HISTORY 66 2.2. CD-CHROMOPHORES AND THEIR INFORMATION
66 2.3. PARAMETERS AND UNITS 68 2.4. INSTRUMENTATION 69 2.5. CD VERSUS
ORD 70 3. FAR-UV CIRCULAR DICHROISM 70 3.1. INTRODUCTION 70 3.2. WHAT
DOES IT MEASURE? 71 3.3. EXPERIMENTAL DETAILS 71 3.4. ESTIMATION OF THE
SECONDARY STRUCTURE 73 3.5. ADVANTAGES, LIMITATIONS, AND CONCLUSIONS 77
3.6. RECENT APPLICATIONS: ACID-INDUCED STRUCTURAL CHANGES 79 4. NEAR-UV
AND VISIBLE CIRCULAR DICHROISM 81 4.1. INTRODUCTION 81 4.2. WHAT DOES IT
MEASURE? 81 4.3. EXPERIMENTAL DETAILS 82 4.4. ADVANTAGES, LIMITATIONS,
AND CONCLUSIONS 83 4.5. RECENT APPLICATIONS 83 5. VIBRATIONAL CIRCULAR
DICHROISM 87 5.1. INTRODUCTION 87 5.2. WHAT DOES IT MEASURE? 87 5.3.
EXPERIMENTAL DETAILS 88 5.4. ADVANTAGES, LIMITATIONS, AND CONCLUSIONS 89
5.5. RECENT APPLICATIONS 91 6. TIME-RESOLVED CIRCULAR DICHROISM 92 7.
CONCLUDING REMARKS 93 REFERENCES 93 CONTENTS XIII CHAPTER 3 FOURIER
TRANSFORM INFRARED SPECTROSCOPY INVESTIGATIONS OF PROTEIN STRUCTURE E.
A. COOPER AND K. KNUTSON 1. INTRODUCTION 101 2. INFRARED SPECTROSCOPY
102 3. BAND ASSIGNMENTS 104 3.1. AMIDE A AND B 109 3.2. AMIDE I 110 3.3.
AMIDE II 115 3.4. AMIDE III 116 3.5. OTHER AMIDE BANDS 117 3.6. OTHER
PROTEIN BANDS 118 4. SAMPLING METHODS 118 4.1. SOLID STATE 118 4.2.
SOLUTION 120 4.3. ATTENUATED TOTAL REFLECTION 122 4.4. DICHROIC
MEASUREMENTS 124 5. DATA ANALYSIS 125 5.1. SUBTRACTION 126 5.2.
RESOLUTION ENHANCEMENT 127 5.3. QUANTITATION 129 6. LITERATURE EXAMPLES
131 6.1. SOLUTION STUDIES 132 6.2. MEMBRANE STUDIES 134 6.3. OTHER
STUDIES 135 7. SUMMARY 136 REFERENCES 137 CHAPTER 4 MASS SPECTROMETRY IN
PROTEIN STRUCTURAL ANALYSIS PETER ROEPSTORFF 1. INTRODUCTION TO MASS
SPECTROMETRY OF PROTEINS 145 2. THE CONTEMPORARY MASS SPECTROMETRIC
TECHNIQUES 147 2.1. PLASMA DESORPTION MASS SPECTROMETRY 147 XIV CONTENTS
2.2. FAST ATOM BOMBARDMENT MASS SPECTROMETRY 148 2.3. MATRIX-ASSISTED
LASER DESORPTION IONIZATION MASS SPECTROMETRY 149 2.4. ELECTROSPRAY
IONIZATION MASS SPECTROMETRY 151 3. TYPE OF INFORMATION AVAILABLE FROM
MASS SPECTRA OF PROTEINS 152 3.1. MOLECULAR WEIGHT INFORMATION 152 3.2.
STRUCTURAL INFORMATION BASED ON FRAGMENT IONS 154 3.3. INFORMATION ON
NONCOVALENT STRUCTURE AND INTERACTION 157 4. EXAMPLES OF APPLICATIONS OF
MASS SPECTROMETRY TO PROTEIN STUDIES 158 4.1. MOLECULAR WEIGHT
DETERMINATION OF INTACT PROTEINS 158 4.2. THE USE OF MASS SPECTROMETRY
IN COMBINATION WITH AUTOMATIC EDMAN DEGRADATION IN PROTEIN SEQUENCING
160 4.3. DIRECT SEQUENCING BY MASS SPECTROMETRY 163 4.4.
POSTTRANSLATIONALLY MODIFIED PROTEINS 165 4.5. MAPPING OF MUTANTS AND
ISOFORMS AND INTERSPECIES VARIATION 166 4.6. MASS SPECTROMETRY COMBINED
WITH PROTEIN OR DNA SEQUENCE INFORMATION 168 5. MASS SPECTROMETRY OF
PHARMACEUTICAL PROTEINS 169 6. CONCLUSIVE REMARKS AND FUTURE ASPECTS 171
REFERENCES 172 CHAPTER 5 TWO-, THREE-, AND FOUR-DIMENSIONAL NUCLEAR
MAGNETIC RESONANCE SPECTROSCOPY OF PROTEIN PHARMACEUTICALS DAVID G.
WANDER VELDE, JAMES MATSUURA, AND MARK C. MANNING 1. INTRODUCTION 179 2.
NMR METHODS 180 2.1. DESCRIPTION OF MULTIDIMENSIONAL NMR 181 2.2. SURVEY
OF KEY MULTIDIMENSIONAL METHODS 183 2.3. THREE- AND FOUR-DIMENSIONAL
EXPERIMENTS 188 2.4. EXPERIMENTAL CONSIDERATIONS 191 3. COMPUTATIONAL
TECHNIQUES 195 3.1. DISTANCE GEOMETRY 195 3.2. RESTRAINED MOLECULAR
DYNAMICS 197 3.3. SIMULATED ANNEALING 197 4. CASE HISTORIES 198 4.1.
INTERLEUKIN-IB 198 4.2. INTERLEUKIN-LA 200 CONTENTS XV 4.3.
INTERLEUKIN-1 RECEPTOR ANTAGONIST 200 4.4. INTERLEUKIN-4 201 4.5.
INTERLEUKIN-6 202 4.6. INTERLEUKIN-8 202 4.7. INSULINLIKE GROWTH FACTOR
203 4.8. INSULIN 203 4.9. INTERFERON-7 204 4.10. EPIDERMAL GROWTH FACTOR
204 5. SUMMARY 207 REFERENCES 207 CHAPTER 6 THERMODYNAMIC STRATEGIES FOR
RATIONAL PROTEIN AND DRUG DESIGN KENNETH P. MURPHY AND ERNESTO FREIRE 1.
INTRODUCTION 219 2. THERMODYNAMIC DESCRIPTION OF PROTEIN STABILITY AND
LIGAND BINDING 220 2.1. INTERACTIONS IMPORTANT TO FOLDING AND BINDING
220 2.2. FORMAL DESCRIPTION OF STABILITY AND BINDING 221 2.3. GROUP
ADDITIVITY AND ACCESSIBLE SURFACE AREA 221 2.4. DETERMINATION OF
EMPIRICAL PARAMETERS 223 2.5. LIMITATIONS OF THE MODEL 226 3.
APPLICATION TO PROTEIN STABILITY 227 4. APPLICATION TO PROTEIN-LIGAND
INTERACTIONS 231 4.1. ENTROPIC EFFECTS IN BINDING INTERACTIONS 231 4.2.
BINDING OF ANGIOTENSIN II TO AN ANTIBODY 232 4.3. ANTIBODY BINDING TO
CYTOCHROME C 235 5. CONCLUSIONS 237 REFERENCES 238 CHAPTER 7
CHROMATOGRAPHIC TECHNIQUES FOR THE CHARACTERIZATION OF PROTEINS JOOST J.
M. HOLTHUIS AND REINOUD J. DRIEBERGEN 1. INTRODUCTION 243 2.
REVERSED-PHASE CHROMATOGRAPHY 245 XVI CONTENTS 2.1. GENERAL 245 2.2.
STATIONARY PHASE 247 2.3. MOBILE PHASE 248 2.4. EXAMPLES 249 2.5.
DETECTION 259 3. HYDROPHOBIC INTERACTION CHROMATOGRAPHY 259 3.1. GENERAL
259 3.2. STATIONARY PHASE 260 3.3. MOBILE PHASE 261 3.4. EXAMPLES 262 4.
ION-EXCHANGE CHROMATOGRAPHY 264 4.1. GENERAL 264 4.2. STATIONARY PHASE
265 4.3. MOBILE PHASE 267 4.4. EXAMPLES 268 5. SIZE-EXCLUSION
CHROMATOGRAPHY 272 5.1. GENERAL 272 5.2. STATIONARY PHASE 273 5.3.
MOBILE PHASE 274 5.4. EXAMPLES 274 6. AFFINITY AND IMMUNOAFFINITY
CHROMATOGRAPHY 277 6.1. GENERAL 277 6.2. STATIONARY PHASE 279 6.3.
MOBILE PHASE 281 6.4. EXAMPLES 282 7. RECENT DEVELOPMENTS 285 7.1.
PERFUSION CHROMATOGRAPHY 285 7.2. HYDROPHYLIC INTERACTION CHROMATOGRAPHY
287 7.3. HIGH-PERFORMANCE AFFINITY CHROMATOGRAPHY 287 7.4. LIQUID
CHROMATOGRAPHY IN COMBINATION WITH MASS SPECTROMETRY 289 REFERENCES 290
CHAPTER 8 CAPILLARY ELECTROPHORESIS OF PROTEINS TOM A. A. M. VAN DE GOOR
1. GENERAL INTRODUCTION 301 2. PRINCIPLES OF CAPILLARY ELECTROPHORESIS
302 CONTENTS XVII 2.1. ELECTROPHORESIS AND ELECTROPHORETIC MOBILITY 302
2.2. ELECTROOSMOSIS AND ELECTROOSMOTIC MOBILITY 302 2.3. ELECTROPHORESIS
AND ELECTROOSMOSIS 303 2.4. EFFICIENCY AND RESOLUTION 303 2.5. MODES IN
CAPILLARY ELECTROPHORESIS 304 2.6. SETUP OF CAPILLARY ELECTROPHORESIS
305 2.7. ADVANTAGES OF CAPILLARY ELECTROPHORESIS 306 3. STRATEGIES FOR
PROTEIN SEPARATIONS 307 3.1. ANALYSIS AT EXTREME ELECTROLYTE PH 308 3.2.
MODIFICATION OF THE CAPILLARY TUBE 309 3.3. CAPILLARY ISOELECTRIC
FOCUSING 313 3.4. CAPILLARY SODIUM DODECYL SULFATE GEL ELECTROPHORESIS
315 4. INFORMATION FROM CAPILLARY ELECTROPHORESIS 315 4.1. ANALYSIS OF
NATIVE PROTEINS 316 4.2. ANALYSIS OF DENATURED PROTEINS 317 4.3.
MICROPREPARATIVE ANALYSIS AND COMBINED METHODS 317 4.4. PEPTIDE MAPPING
318 4.5. MASS SPECTROMETRY INTERFACING 318 4.6. APPLICATIONS OF CE FOR
THE ANALYSIS OF PROTEINS 320 5. CONCLUSIONS 321 REFERENCES 321 CHAPTER 9
APPLYING GENETIC ENGINEERING TO THE STRUCTURAL ANALYSIS OF PROTEINS PAUL
T. HAMILTON 1. INTRODUCTION 329 2. MOLECULAR CLONING AND EXPRESSION 330
2.1. DNA CLONING 330 2.2. EXPRESSION 332 2.3. GENE FUSIONS FOR PROTEIN
PURIFICATION 335 2.4. MUTAGENESIS OF DNA SEQUENCES 337 3. APPLYING
GENETIC ENGINEERING: PHAGE DISPLAY TECHNOLOGY 341 4. SUMMARY 344
REFERENCES 345 INDEX 351
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| indexdate | 2024-12-23T15:09:45Z |
| institution | BVB |
| isbn | 0306450267 |
| language | English |
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| publishDate | 1995 |
| publishDateSearch | 1995 |
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| publisher | Plenum Press |
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| series | Pharmaceutical biotechnology |
| series2 | Pharmaceutical biotechnology |
| spellingShingle | Physical methods to characterize pharmaceutical proteins Pharmaceutical biotechnology Drugs - Chemical analysis Eiwitten gtt Geneesmiddelen gtt Wetenschappelijke technieken gtt Wissenschaftliches Arbeiten Biopharmaceutics methods Chemistry, Pharmaceutical methods Molecular Structure Protein drugs Analysis Proteins chemistry |
| title | Physical methods to characterize pharmaceutical proteins |
| title_auth | Physical methods to characterize pharmaceutical proteins |
| title_exact_search | Physical methods to characterize pharmaceutical proteins |
| title_full | Physical methods to characterize pharmaceutical proteins ed. by James N. Herron ... |
| title_fullStr | Physical methods to characterize pharmaceutical proteins ed. by James N. Herron ... |
| title_full_unstemmed | Physical methods to characterize pharmaceutical proteins ed. by James N. Herron ... |
| title_short | Physical methods to characterize pharmaceutical proteins |
| title_sort | physical methods to characterize pharmaceutical proteins |
| topic | Drugs - Chemical analysis Eiwitten gtt Geneesmiddelen gtt Wetenschappelijke technieken gtt Wissenschaftliches Arbeiten Biopharmaceutics methods Chemistry, Pharmaceutical methods Molecular Structure Protein drugs Analysis Proteins chemistry |
| topic_facet | Drugs - Chemical analysis Eiwitten Geneesmiddelen Wetenschappelijke technieken Wissenschaftliches Arbeiten Biopharmaceutics methods Chemistry, Pharmaceutical methods Molecular Structure Protein drugs Analysis Proteins chemistry |
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