Contributors |
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xv | |
Preface |
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xix | |
Dedication |
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xxiii | |
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SECTION 1 Solution Methods |
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Binding: A Polemic and Rough Guide |
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4 | (1) |
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Binding Constants Provide an Entry into Thermodynamics |
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5 | (2) |
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General Properties of Binding Isotherms |
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7 | (3) |
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Thermodynamics from Thermal Denaturation Methods |
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10 | (3) |
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Completing the Thermodynamic Profile |
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13 | (1) |
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Thermodynamics in the Real World: Some Useful Strategies |
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14 | (2) |
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Ligand-Receptor Binding in the Absence of an Optical Signal |
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16 | (2) |
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Toward High-Throughput Thermodynamics |
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18 | (2) |
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20 | (6) |
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21 | (5) |
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Linked Equilibria in Regulation of Transcription Initiation |
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26 | (1) |
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Multiple Levels of Linkage in Transcription Regulation |
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27 | (3) |
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A Road Map for Quantitative Studies of Assembly of Gene Regulatory Complexes |
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30 | (1) |
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Measurements of Binding Interactions in Transcription Regulation |
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30 | (14) |
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Case Studies of Multiple Linked Equilibria in Transcription Regulatory Systems |
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44 | (10) |
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50 | (4) |
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Biosensor-Surface Plasmon Resonance Methods for Quantitative Analysis of Biomolecular Interactions |
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54 | (1) |
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Rationale: Biomolecular Interactions with SPR Detection |
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55 | (3) |
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58 | (10) |
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Results and Data Analysis |
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68 | (6) |
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74 | (6) |
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75 | (5) |
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Isothermal Titration Calorimetry: Experimental Design, Data Analysis, and Probing Macromolecule/Ligand Binding and Kinetic Interactions |
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80 | (2) |
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Calorimetry Theory and Operation |
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82 | (3) |
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Thermodynamic ITC Experiments |
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85 | (15) |
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100 | (10) |
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110 | (6) |
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111 | (5) |
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Differential Scanning Calorimetry |
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116 | (1) |
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117 | (2) |
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Experimental Protocols and Preliminary Data Treatment |
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119 | (7) |
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126 | (13) |
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139 | (5) |
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140 | (4) |
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Analytical Ultracentrifugation: Sedimentation Velocity and Sedimentation Equilibrium |
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144 | (2) |
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146 | (1) |
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Dilute Solution Measurements |
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147 | (2) |
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Concentrated and Complex Solutions |
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149 | (1) |
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Instrumentation and Optical Systems |
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150 | (8) |
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158 | (2) |
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160 | (1) |
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161 | (7) |
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Sedimentation Equilibrium |
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168 | (6) |
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174 | (8) |
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176 | (6) |
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Determination of Membrane Protein Molecular Weights and Association Equilibrium Constants Using Sedimentation Equilibrium and Sedimentation Velocity |
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182 | (1) |
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183 | (7) |
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190 | (5) |
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195 | (11) |
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206 | (2) |
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208 | (6) |
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209 | (5) |
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Basic Aspects of Absorption and Fluorescence Spectroscopy and Resonance Energy Transfer Methods |
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214 | (1) |
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214 | (9) |
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Fluorescence Spectroscopy |
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223 | (16) |
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239 | (5) |
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239 | (5) |
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Applications of Fluorescence Anisotropy to the Study of Protein---DNA Interactions |
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Introduction and General Background |
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244 | (3) |
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Advantages and Disadvantages of Anisotropy in Monitoring DNA Binding |
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247 | (1) |
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248 | (3) |
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Experimental Design and Performance |
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251 | (9) |
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Other Applications of Fluorescence Anisotropy to the Study of Protein---DNA Interactions |
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260 | (4) |
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260 | (4) |
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Circular Dichroism and Its Application to the Study of Biomolecules |
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264 | (2) |
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Instrumentation and Sample Preparation |
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266 | (3) |
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269 | (2) |
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Data Processing and Spectral Characteristics |
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271 | (5) |
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276 | (14) |
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290 | (6) |
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290 | (6) |
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Protein Folding and Stability Using Denaturants |
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296 | (1) |
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297 | (1) |
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298 | (12) |
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310 | (3) |
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313 | (9) |
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322 | (6) |
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323 | (5) |
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Hydrodynamic Modeling: The Solution Conformation of Macromolecules and Their Complexes |
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328 | (1) |
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329 | (3) |
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332 | (16) |
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348 | (1) |
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349 | (4) |
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Hydrodynamic Calculations |
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353 | (13) |
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Advanced Hydrodynamic Calculations |
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366 | (4) |
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370 | (6) |
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370 | (6) |
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X-Ray and Neutron Scattering Data and Their Constrained Molecular Modeling |
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376 | (4) |
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380 | (2) |
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X-Ray and Neutron Facilities |
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382 | (8) |
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390 | (10) |
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Constrained Scattering Modeling |
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400 | (7) |
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407 | (9) |
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416 | (10) |
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420 | (6) |
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Structural Investigations into Microtubule-MAP Complexes |
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426 | (2) |
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428 | (2) |
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430 | (9) |
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439 | (7) |
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441 | (5) |
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446 | (2) |
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448 | (4) |
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452 | (4) |
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456 | (3) |
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459 | (4) |
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Experimental Design and Data Analysis |
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463 | (7) |
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470 | (4) |
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Data Analysis in Practice |
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474 | (6) |
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476 | (4) |
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Mutagenic Analysis of Membrane Protein Functional Mechanisms: Bacteriorhodopsin as a Model Example |
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480 | (1) |
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481 | (5) |
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486 | (5) |
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491 | (18) |
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509 | (9) |
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511 | (7) |
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Quantifying DNA---Protein Interactions by Single Molecule Stretching |
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518 | (1) |
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Stretching Single DNA Molecules with Optical Tweezers |
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519 | (2) |
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Force-Induced Melting of Single DNA Molecules |
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521 | (1) |
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T4 gp32 Interactions with DNA |
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522 | (9) |
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Model for Salt-Dependent Regulation of T4 Gene 32 Binding to DNA |
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531 | (6) |
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537 | (5) |
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538 | (4) |
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Isotopomer-Based Metabolomic Analysis by NMR and Mass Spectrometry |
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542 | (1) |
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543 | (1) |
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544 | (3) |
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547 | (30) |
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577 | (13) |
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581 | (9) |
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Following Molecular Transitions with Single Residue Spatial and Millisecond Time Resolution |
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590 | (5) |
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Acquisition of •OH Footprinting Time-Progress Curves |
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595 | (7) |
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Data Reduction and Production of Time-Progress Curves |
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602 | (3) |
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Interpretation of Individual Nucleotide Time-Progress Curves |
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605 | (13) |
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611 | (7) |
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Methods and Applications of Site-Directed Spin Labeling EPR Spectroscopy |
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618 | (18) |
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636 | (17) |
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653 | (7) |
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653 | (7) |
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Fluorescence Correlation Spectroscopy and Its Application to the Characterization of Molecular Properties and Interactions |
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660 | (3) |
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Fluorescence Correlation Spectroscopy |
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663 | (3) |
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666 | (2) |
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Sample Preparation and Some Practical Considerations |
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668 | (3) |
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Fluorescence Cross-Correlation Spectroscopy |
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671 | (1) |
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Illustrative Examples of FCS Applications |
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672 | (4) |
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676 | (4) |
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677 | (3) |
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A Practical Guide on How Osmolytes Modulate Macromolecular Properties |
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680 | (3) |
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683 | (15) |
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698 | (16) |
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714 | (10) |
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724 | (16) |
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726 | (14) |
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SECTION 2 Computational Methods |
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740 | (2) |
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Statistics of Data: The 10-Min Review |
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742 | (7) |
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Linear Least Squares---Theory |
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749 | (8) |
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Linear Least Squares---Monte Carlo Illustrations |
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757 | (6) |
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763 | (3) |
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Applications and Illustrations |
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766 | (12) |
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778 | (3) |
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779 | (2) |
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Nonlinear Least-Squares Fitting Methods |
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781 | (4) |
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Formulate a Hypothesis-Based Mathematical Model |
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785 | (2) |
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Determining the Optimal Parameters of the Model |
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787 | (4) |
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Distinguishing Between Multiple Mathematical Models |
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791 | (5) |
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Estimate the Precision of the Model Parameters |
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796 | (4) |
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Cross-Correlation of the Estimated Parameters |
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800 | (3) |
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Uniqueness of the Parameters |
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803 | (1) |
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804 | (4) |
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805 | (3) |
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Methods for Simulating the Dynamics of Complex Biological Processes |
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808 | (1) |
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809 | (1) |
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810 | (13) |
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823 | (12) |
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Modeling and Simulation in Practice |
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835 | (5) |
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840 | (4) |
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840 | (4) |
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Computational Methods for Biomolecular Electrostatics |
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844 | (1) |
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Electrostatics in Cellular Systems |
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844 | (3) |
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Models for Biomolecular Solvation and Electrostatics |
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847 | (9) |
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856 | (5) |
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Conclusion and Future Directions |
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861 | (11) |
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862 | (10) |
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Ligand Effects on the Protein Ensemble: Unifying the Descriptions of Ligand Binding, Local Conformational Fluctuations, and Protein Stability |
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Bertrand E. Garcia-Moreno |
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872 | (3) |
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The Effect of pH on the Conformational Ensemble |
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875 | (6) |
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881 | (5) |
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886 | (8) |
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889 | (5) |
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Molecular Modeling of the Cytoskeleton |
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894 | (1) |
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894 | (4) |
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Applications of Molecular Modeling |
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898 | (6) |
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904 | (3) |
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907 | (5) |
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907 | (5) |
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Mathematical Modeling of Cell Migration |
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912 | (1) |
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912 | (14) |
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Cell Adhesion and Retraction |
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926 | (4) |
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930 | (3) |
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Summary and Future Outlook |
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933 | (6) |
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934 | (5) |
Index |
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939 | (26) |
Volumes in Series |
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965 | |