Calorimetry:
Gespeichert in:
| Weitere Verfasser: | |
|---|---|
| Format: | Buch |
| Sprache: | English |
| Veröffentlicht: |
Amsterdam
Elsevier
2016
|
| Ausgabe: | First edition |
| Schriftenreihe: | Methods in enzymology
volume 567 |
| Schlagworte: | |
| Online-Zugang: | Calorimetry Inhaltsverzeichnis |
| Beschreibung: | xix, 493 Seiten Illustrationen, Diagramme 23 cm |
| ISBN: | 9780128029060 |
Internformat
MARC
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| 245 | 1 | 0 | |a Calorimetry |c edited by Andrew L. Feig |
| 250 | |a First edition | ||
| 264 | 1 | |a Amsterdam |b Elsevier |c 2016 | |
| 300 | |a xix, 493 Seiten |b Illustrationen, Diagramme |c 23 cm | ||
| 336 | |b txt |2 rdacontent | ||
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| 490 | 1 | |a Methods in enzymology |v volume 567 | |
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Datensatz im Suchindex
| _version_ | 1804176693447884800 |
|---|---|
| adam_text | Titel: Calorimetry
Autor: Feig, Andrew
Jahr: 2016
CONTENTS
Contributors xi
Preface xvii
Section I
ITC
1. Isothermal Titration Calorimetry Measurements of Metal Ions
Binding to Proteins 3
Colette F. Quinn, Margaret C. Carpenter, Molly L. Croteau,
and Dean E. Wilcox
1. Introduction 4
2. Metal Ion Properties Relevant to ITC Measurements 5
3. ITC Measurements Involving Metal Ions 9
4. Fitting ITC Data Involving Metal Ions 12
5. Post Hoc Analysis of ITC Data Involving Metal Ions 13
6. Additional Considerations with Metal Ions 18
7. Conclusion 19
Acknowledgments 20
References 20
2. Assessing Coupled Protein Folding and Binding Through
Temperature-Dependent Isothermal Titration Calorimetry 23
Debashish Sahu, Monique Bastidas, Chad W. Lawrence, William G. Noid,
and Scott A. Showalter
1. Introduction 24
2. Sample Preparation 27
3. Special Considerations for ITC of Intrinsically Disordered Proteins 29
4. Data Fitting and Analysis 31
5. Summary 41
Acknowledgments 43
References 43
3. Fragment-Based Screening for Enzyme Inhibitors
Using Calorimetry 47
Michael I. Recht, Vicki Nienaber, and Francisco E, Torres
1. Introduction 48
vi
Contents
2. Required Materials 52
3. Instrumentation 53
4. Fragment Library Selection 56
5. Calorimetric Enzyme Assay: Nanocalorimeter 59
6. Calorimetric Enzyme Assay: Commercial Microcalorimeters 64
7. Summary 66
Acknowledgments 67
References 67
4. Measuring Multivalent Binding Interactions by Isothermal
Titration Calorimetry 71
Tarun K. Dam, Melanie L. Talaga, Ni Fan, and Curtis F. Brewer
1. Introduction 72
2. Determining the Thermodynamics of Lectin Binding to Multivalent
Synthetic Analogs 73
3. Determination that the Epitopes of Multivalent Analogs Possess
a Gradient of Decreasing Microscopic-Binding Affinities (Ka) 81
4. Direct Calorimetric Measurements of Microscopic Thermodynamic
Binding Parameters by Reverse ITC 86
5. ITC Studies of Lectin Binding to Multivalent Glycoproteins 88
6. ITC Studies of Lectin Binding to Polyvalent Mucins 91
Acknowledgments 93
References 94
5. Calorimetric and Spectroscopic Analysis of the Thermal Stability
of Short Duplex DNA-Containing Sugar and Base-Modified
Nucleotides 97
Kareem Fakhfakh, Curtis B. Hughesman, A. Louise Creagh, Vincent Kao,
and Charles Haynes
1. Introduction 98
2. Melting Thermodynamics from DSC 100
3. Melting Thermodynamics from UV Spectroscopy 112
4. Errors Analysis 121
5. Understanding the Contribution to Duplex Stability of Specific Nucleotide
Modifications 122
References 125
6. Calorimetric Quantification of Cydodextrin-Mediated Detergent
Extraction for Membrane-Protein Reconstitution 129
Martin Textor and Sandro Keller
1. Introduction
130
Contents vii
2. Membrane-Protein Reconstitution
3. Practical Approach to CD-Driven Reconstitution
4. Concluding Remarks
Acknowledgments
References
7. Extending ITC to Kinetics with kinlTC
Philippe Dumas, Eric Ennifar, Cyrielle Da Veiga, Guillaume Bee,
William Palau, Carmelo Di Primo, Angel Pineiro, Juan Sabin, Eva Munoz,
and Javier Rial
1. Introduction
2. The Theoretical Basis of kinlTC-ETC
3. Practical Aspects of the Method
4. Results
5. Instrument Response Time: Measurement and Important Facts
6. Conclusions
Acknowledgments
Appendix Geometrical Features of an ETC
References
8. Measuring the Kinetics of Molecular Association by Isothermal
Titration Calorimetry 181
Kirk A. Vander Meulen, Scott Horowitz, Raymond C. Trievel,
and Samuel E. Butcher
1. Introduction 182
2. Background 183
3. Procedure and Results 187
4. Method Details 207
Acknowledgments 212
References 212
9. Isothermal Titration Calorimetry to Characterize Enzymatic
Reactions 215
Luca Mazzei, Stefano Ciurli, and Barbara Zambelli
1. Introduction 216
2. Instrumental Setup 218
3. Methods and Theory 219
4. Experimental Conditions 221
5. Data Analysis 224
130
136
151
153
153
157
158
160
163
165
174
176
177
177
179
viii
Contents
6. Representative Results 225
7. Conclusions 234
References 234
10. Avoiding Buffer Interference in ITC Experiments: A Case
Study from the Analysis of Entropy-Driven Reactions
of Glucose-6-Phosphate Dehydrogenase 237
M. Lucia Bianconi
1. Introduction 238
2. Correcting for Protonation Effects 241
3. Materials and Methods 245
4. Results and Discussion 246
5. Taking Advantage of the Heat Effect of Buffer Protonation/Deprotonation 252
6. Final Remarks 253
Acknowledgments 254
References 254
11. ITC Methods for Assessing Buffer/Protein Interactions from
the Perturbation of Steady-State Kinetics: A Reactivity Study
of Homoprotocatechuate 2,3-Dioxygenase 257
Kate L. Henderson, Delta K. Boyles, Vu H. Le, Edwin A. Lewis,
and Joseph P. Emerson
1. Introduction 258
2. Required Materials 261
3. Instrumentation and Sample Considerations 261
4. Steady-State ITC Method Applied to HPCD 262
5. Discussion 272
6. Conclusions 276
References 277
Section II
DSC
12. Modern Analysis of Protein Folding by Differential
Scanning Calorimetry 281
Beatriz Ibarra-Molero, Athi N. Naganathan, Jose M. Sanchez-Ruiz,
and Victor Munoz
1. Introduction 282
2. Thermodynamics and the DSC Experiment 285
Contents____jx
3. Absolute Heat Capacity and DSC Baselines 293
4. Equilibrium Thermodynamics Analysis: Microstates Versus Macrostates 296
5. Statistical Mechanics Analysis of DSC Experiments 299
6. Concluding Remarks 313
Acknowledgments 314
References 314
13. A Guide to Differential Scanning Calorimetry of Membrane
and Soluble Proteins in Detergents 319
Zhengrong Yang and Christie G. Brouillette
1. Introduction 320
2. Detergent Properties 328
3. Detergent Effects on Proteins and Detection by DSC 332
4. Complementary Noncalorimetry Approaches to Study
Thermal Unfolding 339
5. Choice of Detergents 340
6. Case Studies 343
7. Experimental Procedures 347
8. Concluding Remarks 352
Acknowledgment 352
References 352
14. Orthogonal Methods for Characterizing the Unfolding of
Therapeutic Monoclonal Antibodies: Differential Scanning
Calorimetry, Isothermal Chemical Denaturation, and Intrinsic
Fluorescence with Concomitant Static Light Scattering 359
Deniz B. Temel, Pavel Landsman, and Mark L. Brader
1. Introduction 360
2. Therapeutic Monoclonal Antibodies 361
3. Performing and Detecting Protein Unfolding 363
4. Experimental 373
5. Data Interpretation 380
Acknowledgments 387
References 387
15.IATC, DSC, and PPC Analysis of Reversible and Multistate
Structural Transition of Cytochrome c 391
Shun-ichi Kidokoro and Shigeyoshi Nakamura
1. Introduction
2. Isothermal Acid-Titration Calorimetry
392
396
X
Contents
3. Differential Scanning Calorimetry 403
4. Pressure Perturbation Calorimetry with DSC Analysis 408
5. Summary 410
Acknowledgment 411
References 411
16. The Complementarity of the Loop to the Stem in DNA
Pseudoknots Gives Rise to Local TAT Base-Triplets 413
Calliste Reiling-Steffensmeier and Luis A. Marky
1. Introduction 414
2. Materials and Methods 416
3. Results and Discussion 419
4. Conclusions 427
Acknowledgments 429
References 429
Section III
Calorimetry Facilities
17. A High-Throughput Biological Calorimetry Core: Steps
to Startup, Run, and Maintain a Multiuser Facility 435
Neela H. Yennawar, Julia A. Fecko, Scott A. Showalter,
and Philip C. Bevilacqua
1. Introduction 436
2. Instruments at the Facility 437
3. Running of the Facility 441
4. Science Facilitated 453
5. Conclusions 458
Acknowledgments 459
References 459
Author Index 46 j
Subject Index 481
|
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| language | English |
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| series | Methods in enzymology |
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| spelling | Calorimetry edited by Andrew L. Feig First edition Amsterdam Elsevier 2016 xix, 493 Seiten Illustrationen, Diagramme 23 cm txt rdacontent n rdamedia nc rdacarrier Methods in enzymology volume 567 Calorimetry Kalorimetrie (DE-588)4029367-1 gnd rswk-swf (DE-588)4143413-4 Aufsatzsammlung gnd-content Kalorimetrie (DE-588)4029367-1 s DE-604 Feig, Andrew L. edt Methods in enzymology volume 567 (DE-604)BV000000938 567 http://digitool.hbz-nrw.de:1801/webclient/DeliveryManager?pid=6648325&custom_att_2=simple_viewer Calorimetry Inhaltsverzeichnis HBZ Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=029241790&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
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| title | Calorimetry |
| title_auth | Calorimetry |
| title_exact_search | Calorimetry |
| title_full | Calorimetry edited by Andrew L. Feig |
| title_fullStr | Calorimetry edited by Andrew L. Feig |
| title_full_unstemmed | Calorimetry edited by Andrew L. Feig |
| title_short | Calorimetry |
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