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INTRODUCTION TO
ANALYTICAL
ULTRACENTRIFUGATION
iiINTRODUCTION TO ANALYTICAL ULTRACENTRIFUGATION
GREG RALSTON
DEPARTMENT OF BIOCHEMISTRY
THE UNIVERSITY OF SYDNEY
SYDNEY, AUSTRALIA
iii ivCONTENTS
About the Author
About this Handbook
Glossary
Recommended Reading
Analytical Ultracentrifugation and Molecular Characterization The Unique Features of Analytical UltracentrifugationExamination of Sample Purity
Molecular Weight Determination
Analysis of Associating Systems
Conformation Changes
Ligand Binding
Sedimentation of Particles in a Gravitational FieldInstrumentation
Rotors
CellsBoundary forming cells
Band forming cells
Methods of Detection and Data Collection
Refractometric Methods
Schlieren
Rayleigh interference optics
Absorbance
Sample Preparation
Multiple Boundaries
Determination of s
Solvent Effects
Concentration Dependence
Radial Dilution
Analysis of Boundaries
Self-Sharpening of Boundaries
Tests for Homogeneity vi
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Speed Dependence
Primary Charge Effect
Association Behavior
Band Sedimentation
Active Enzyme Sedimentation
Diffusion
Sedimentation Equilibrium
Subunit Structure
Heterogeneity
Nonideality
Association Reactions
Determination of Thermodynamic Parameters
Detergent-Solubilized Proteins
Behavior in "Crowded" Solutions
Archibald Approach-to-Equilibrium Method
Density Gradient Sedimentation Equilibrium (IsopycnicSedimentation Equilibrium)
The Future
References
IndexFIGURES
Figure 2
Double-sector centerpiece
Figure 3
Comparison of the data obtained from the schlieren, interference, photographic absorbance, and photoelectric absorbance optical systemsFigure 4
Schematic diagram of the optical system of the BeckmanFigure 5
Movement of the boundary in a sedimentation
velocity experiment with a recombinant malaria antigen proteinFigure 6
Plot of the logarithm of the radial position, r
bnd , of a sedimenting boundary as a function of time for recombinant dihydroorotase domain protein 3333
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Figure 7
Concentration dependence of the sedimentation
Figure 8
thymus DNA fragmentsFigure 9
The primary charge effect
Figure 10 Concentration-dependent increase in weight average Figure 11 Schematic appearance of a bimodal boundary for a hypothetical monomer-tetramer association reaction Figure 12 Spreading of the boundary with time in a diffusion experiment with dextranFigure 13
Figure 14 Schematic representation of sedimentation equilibrium Figure 15 Schematic representation of the meniscus in a centrifuge cell Figure 16 Sedimentation equilibrium distribution of two different solutes Figure 17 Decrease in apparent molecular weight with Figure 18 Sedimentation equilibrium analysis of the selfassociation of a DNA-binding protein from B. subtilis Figure 19 Diagnostic plots for assessing the self-association ofΆ-lactoglobulin C
Figure 20 Sedimentation equilibrium analysis of human spectrin TABLETable 1
for Common Biological Macromolecules 2730
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