Book contents
- Frontmatter
- Contents
- Foreword by D. M. Engelman
- Foreword by Pierre Joliot
- Preface
- Introduction: Molecular biophysics at the beginning of the twenty-first century: from ensemble measurements to single-molecule detection
- Part A Biological macromolecules and physical tools
- Part B Mass spectrometry
- Part C Thermodynamics
- Part D Hydrodynamics
- Chapter D1 Biological macromolecules as hydrodynamic particles
- Chapter D2 Fundamental theory
- Chapter D3 Macromolecular diffusion
- Chapter D4 Analytical ultracentrifugation
- Chapter D5 Electrophoresis
- Chapter D6 Electric birefringence
- Chapter D7 Flow birefringence
- Chapter D8 Fluorescence depolarisation
- Chapter D9 Viscosity
- Chapter D10 Dynamic light scattering
- Chapter D11 Fluorescence correlation spectroscopy
- Part E Optical spectroscopy
- Part F Optical microscopy
- Part G X-ray and neutron diffraction
- Part H Electron diffraction
- Part I Molecular dynamics
- Part J Nuclear magnetic resonance
- References
- Index of eminent scientists
- Subject Index
- References
Chapter D4 - Analytical ultracentrifugation
from Part D - Hydrodynamics
Published online by Cambridge University Press: 05 November 2012
Book contents
- Frontmatter
- Contents
- Foreword by D. M. Engelman
- Foreword by Pierre Joliot
- Preface
- Introduction: Molecular biophysics at the beginning of the twenty-first century: from ensemble measurements to single-molecule detection
- Part A Biological macromolecules and physical tools
- Part B Mass spectrometry
- Part C Thermodynamics
- Part D Hydrodynamics
- Chapter D1 Biological macromolecules as hydrodynamic particles
- Chapter D2 Fundamental theory
- Chapter D3 Macromolecular diffusion
- Chapter D4 Analytical ultracentrifugation
- Chapter D5 Electrophoresis
- Chapter D6 Electric birefringence
- Chapter D7 Flow birefringence
- Chapter D8 Fluorescence depolarisation
- Chapter D9 Viscosity
- Chapter D10 Dynamic light scattering
- Chapter D11 Fluorescence correlation spectroscopy
- Part E Optical spectroscopy
- Part F Optical microscopy
- Part G X-ray and neutron diffraction
- Part H Electron diffraction
- Part I Molecular dynamics
- Part J Nuclear magnetic resonance
- References
- Index of eminent scientists
- Subject Index
- References
Summary
Historical review
1913
A. Dumansky proposed the use of ultracentrifugation to determine the dimensions of colloidal particles.
1923
T. Svedberg and J. B. Nichols constructed the first centrifuge with an optical system to follow particle behaviour in a centrifugal field. One year later, Svedberg noted the decrease in absorbance at the top of the cell during centrifugation of a haemoglobin solution.
1926
Svedberg made the first measurements of protein molecular weights (haemoglobin and ovalbumin) by sedimentation equilibrium and in 1927 he determined the molecular weight of haemoglobin using a combination of sedimentation and diffusion data. These pioneering studies led to the undeniable conclusion that proteins are truly macromolecules, made up of a large number of atoms linked by covalent bonds (Comment D4.1).
(Comment D4.1)
It is interesting to note that Theodor Svedberg was awarded the Nobel prize for his work on colloidal systems and not for inventing the analytical centrifuge.
1929
O. Lamm deduced a general equation describing the behaviour of the moving boundary in the ultracentrifuge field. The exact solution of the equation is an infinite series of integrals, which can be computed only by numerical integration. In later work, the Lamm equation was solved analytically for specific limiting cases (H. Faxen, W. J. Archibald, H. Fujita).
1930s
Schlieren optical systems were designed by J. St. L. Philpot and H. Svenson, and independently by L. G. Longsworth; these allowed a representation of the concentration gradient (or, more precisely, the refractive index increment) as a function of distance in the centrifuge sample cell.
- Type
- Chapter
- Information
- Methods in Molecular BiophysicsStructure, Dynamics, Function, pp. 339 - 387Publisher: Cambridge University PressPrint publication year: 2007
References
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, and (1980). Biophysical Chemistry. Part II. Technique for the Study of Biological Structure and Function. San Francisco, CA: W. H. Freeman and Company.Google Scholar
, , and (1985). Measurement of changes of hydrodynamic properties by sedimentation. Meth. Enzymol., 117, 27–40.CrossRefGoogle ScholarPubMed
(1995). Sedimentation equilibrium as thermodynamic tool. In Methods in Enzymology, eds. and , pp. 427–452. New York: Academic Press.Google Scholar
(1992). Is there a future for the ultracentrifuge? In Analytical Ultracentrifugation in Biochemistry and Polymer Science, eds. , and . Cambridge: Royal Society of Chemistry.Google Scholar
(1993). Introduction to Analytical Ultracentrifugation. Fullerton, CA: Beckman Instruments.Google Scholar
. (1992). The Optima XL-A: A new analytical ultracentrifuge with a novel precision absorption optical system. In Analytical Ultracentrifugation in Biochemistry and Polymer Science, eds. , and . Cambridge: Royal Society of Chemistry,Google Scholar
(1975). Sedimentation analysis of proteins. In The Proteins, third edition., eds. and , Volume VI, pp. 225–291. New York: Academic Press.Google Scholar
(1986). Protein volumes and hydration effects: the calculation of partial specific volumes, neutron scattering matchpoints and 280 nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Eur. J. Biochem., 157, 169–180.CrossRefGoogle Scholar
, , and (eds.) (1992). Analytical Ultracentrifugation in Biochemistry and Polymer Science. Cambridge: The Royal Society of Chemistry.Google Scholar
(1994). Boundary analysis in sedimentation velocity experiments. Methods Enzymol., 240, 478–501.CrossRefGoogle ScholarPubMed
(1994). Determination of macromolecular homogeneity, shape, and interactions using sedimentation velocity analytical centrifugation. In Methods in Molecular Biology, eds. , and , Volume 22. Microscopy, Optical Spectroscopy, and Macroscopic Techniques. Totowa, NJ: Humana Press.Google Scholar
, , and (1994). Analytical utracentrifugation of complex macromolecular systems. Biochemistry, 33, 13155–13163.CrossRefGoogle Scholar
(1996). Defining the structure and stability of macromolecular assemblies in solution: the re-emergence of analytical ultracentrifugation as a practical tool. Structure, 4, 367–373.CrossRefGoogle ScholarPubMed
, and (1999). Modern application of analytical ultracentrifugation. Annu. Rev. Biophys. Biomol. Struct., 28, 75–100.CrossRefGoogle Scholar
, , , and (2000). Sedimentation velocity analysis of macromolecular assemblies. Methods Enzymol., 321, 67Google ScholarPubMed
(2000). Size distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modelling. Biophys. J., 78, 1606–1619.CrossRefGoogle Scholar
, and (1980). Biophysical Chemistry. Part II. Technique for the Study of Biological Structure and Function. San Francisco, CA: W. H. Freeman and Company.Google Scholar
, , and (1985). Measurement of changes of hydrodynamic properties by sedimentation. Meth. Enzymol., 117, 27–40.CrossRefGoogle ScholarPubMed
(1995). Sedimentation equilibrium as thermodynamic tool. In Methods in Enzymology, eds. and , pp. 427–452. New York: Academic Press.Google Scholar