New revolutions in the evolution of analytical ultracentrifugation

Current Opinion in Structural Biology

Volumn 6, Issue 5, 1996, Pages 650-658

  Schuster, Todd M ^a   Toedtt, John M ^a  

^a UNIVERSITY OF CONNECTICUT   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOPHYSICS; COMPUTER; COMPUTER PROGRAM; GENETIC ANALYSIS; MACROMOLECULE; MOLECULAR BIOLOGY; PRIORITY JOURNAL; REVIEW; ULTRACENTRIFUGATION; ULTRACENTRIFUGE;

EID: 0030272150     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(96)80032-7     Document Type: Article

References (42)

1. Laue TM: On-line data acquisition and analysis from the rayleigh interferometer. In Analytical Ultracentrifugation in Biochemistry and Polymer Science. Edited by Handing SE, Rowe AJ. Cambridge, UK: Royal Society of Chemistry; 1992.
2. Yphantis DA, Stafford WF, Liu S, Olsen PH, Lary JW, Hayes DB, Moody TP, Ridgeway TM, Lyons DA, Laue TM: Online data acquisition for the Rayleigh interference optical system of the analytical ultracentrifuge. In Modem Analytical Ultracentrifugation. Edited by Schuster TM, Laue TM. Boston: Birkhauser; 1994:209-226.
3. Hansen JC, Lebowitz J, Démêler B: Analytical Ultracentrifugation of complex macromolecular systems. Biochemistry 1994, 33:13155-13163.
4. Harding SE: The sedimentation equilibrium analysis polysaccharides and mucins: a guided tour of the problem solving for difficult heterogeneous systems. In Modern Analytical U/tracentrifugation. Edited by Schuster TM, Laue TM. Boston: Birkhauser; 1994:315-342.
5. Minton AP: Conservation of signal: a new algorithm for the elimination of the reference concentration as an independently variable parameter in the analysis of sedimentation equilibrium. In Modem Analytical Ultracentrifugation. Edited by Schuster TM, Laue TM. Boston: Birkhauser; 1994:81-93.
6. Fujita H: Notes on the derivation of sedimentation equilibrium equations. In Modern Analytical U/tracentrifugation. Edited by Schuster TM, Laue TM. Boston: Birkhauser; 1994:3-15.
7. Schuster TM, Laue TM (Eds): Modern Analytical U/tracentrifugation. Boston: Birkhauser; 1994.
8. Harding SE: The analytical ultracentrifuge spins again. Trends Ana/Chem 1994, 13:439-446.
9. Hensley P: Defining the structure and stability of macromolecular assemblies in solution: the re-emergence of analytical Ultracentrifugation as a practical tool. Structure 1996, 4:367-373. Presents the use of AU in conjunction with other biophysical methods in the characterization of macromolecules and macromolecular interactions. Mass spectrometry, surface plasmon resonance, isothermal titration calorimetry, differential scanning calorimetry, and spectral approaches are examined to distinguish their uses both alone and in combination with each other and AU. In addition, sedimentation velocity analysis, (in particular the DCDT method) and equilibrium sedimentation analysis are reviewed.
10. Harding SE: Analytical ultracentrifugation and the genetic engineering of macromolecules. Biotechnol Genet Eng Rev 1993, 11:317-356.
11. RASMB Home Page on World Wide Web URL: http://bbriwww.eri.harvard.edu/RASMB/rasmb.html For contents of the home page, see text. The available software includes that from Stafford, Johnson and Yphantis/National Analytical Ultracentrifuge Facility, Minton, Holladay, Philo, Démêler, and Ralston. Information about the mail server is also given. You can join the server by e-mailing RASMB-man-ager@bbri.eri.harvard.edu.
12. Bo Demeler's XL-A and RASMB/Analytical Ultracentrifugation page at the UTHSCSA Biochemistry Department on World Wide Web \JRL:http://bioc02.uthscsa.eduJ.biochem/xla.html This site has the same downloadable software available on the RASMB site [11] but in addition it has Jeff Hansen's AU review article, the RASMB mailing list with past communications, collaboration and fee-for-service information, a tutorial on the van Holde-Weischet method, and data analysis examples.
13. Beckman Home Page on World Wide Web URL: http://www.beckman.com This is the main Beckman home page. From here you can easily access the Optima XL-A application and reference list, the XL-A/XL-I description at and the exploration site. The reference site here is exceptional because the XL-A applications are separated into several categories which include binding studies and complexes, general studies, glycoproteins and proteoglycans, lipoproteins, miscellaneous samples (including peptides), new, nucleic acids, proteins (enzymes), proteins (receptors), other proteins, synthetic polymers, and viruses.
14. Cantor CR, Schimmel PR: Biophysical Chemistry, Part II. San Francisco: W.H. Freeman and Company; 1980.
15. 5. Stafford WF III: Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile. Anal Biochem 1992, 203:295-301.
16. 6. Stafford WF III: Sedimentation boundary analysis of interacting systems: use of the apparent sedimentation coefficient distribution function. In Modern Analytical Ultracentrifugation. Edited by Schuster TM, Laue TM. Boston: Birkhauser; 1994:119-137.
17. 7. Stafford WF III: Boundary analysis in sedimentation velocity experiments. Methods Enzymol 1994, 240:478-501.
18. Stafford WF III: Rapid molecular weight determination by sedimentation velocity analysis [abstract]. Biophys J 1996, 70:A231.
19. 9. Van Holde KE, Weischet W: Boundary analysis of sedimentation-velocity experiments with monodisperse and paucidisperse solutes. Biopolymers 1978, 17:1387-1403.
20. Holladay LA: An approximate solution to the Lamm equation. Biophys Chem 1979, 10:187-190.
21. Holladay LA: Simultaneous rapid estimation of sedimentation coefficient and molecular weight Biophys Chem 1980, 11:303-308.
22. Philo JS: Measuring sedimentation, diffusion, and molecular weights of small molecules by direct fitting of sedimentation velocity concentration profiles. In Modern Analytical Ultracentrifugation. Edited by Schuster TM, Laue TM. Boston: Birkhauser; 1994:156-170.
23. Stafford WF, Schuster TM: Hydrodynamic methods. In introduction to Biophysical Methods for Protein and Nucleic Acid Research. Edited by Glasel JA, Deutscher MP. New York: Academic Press; 1995:111-143.
24. Johnson ML, Frasier SG: Nonlinear least-squares analysis. Methods Enzymol 1985, 117:301-341.
25. Johnson ML, Correia JJ, Yphantis DA, Halvorson HR: Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques. Biophys J 1981, 36:575-585.
26. Wmzor DJ, Wills PR: Omega analysis and the characterization of solute self-Association by sedimentation equilibrium. In Modern Analytical U/tracentrifugation. Edited by Schuster TM, Laue TM. Boston: Birkhauser; 1994:66-80.
27. Johnson ML, Straume M: Comments on the analysis of sedimentation equilibrium experiments. In Modern Analytical Ultracentrifugation. Edited by Schuster TM, Laue TM. Boston: Birkhauser; 1994:37-65.
28. Advant SJ, Braswell EH, Kumar CV, Kalonia DS: The effect of pH and temperature on the self-association of recombinant human interleukin-2 as studied by equilibrium sedimentation. Pharm Res 1995, 12:637-641. The self-association of recombinant human interleukin-2 in solution was investigated as a function of pH and temperature using equilibrium sedimentation at 10°C and 20°C. The data at both both temperatures are best described by a weak monomer-dimer association equilibrium.
29. Henniker A, Ralston GB: Reinvestigation of the thermodynamics of spectrin self-association. Biophys Chem 1994, 52:251-258.
30. Behal RH, DeBuysere MS, Démêler B, Hansen JC, Olson MS: Pyruvate dehydrogenase multienzyme complex: characterization of assemble intermediates by sedimentation velocity analysis. J Blol Chem 1994, 296:31372-31377
31. Darawshe S, Minton AP: Quantitative characterization of macromolecular associations in solution via real-time and postcentrifugation measurements of sedimentation equilibrium (SE): a comparison. Anal Biochem 1994, 220:1-4.
32. Zarina S, Slingsby C, Jaenicke R, Zaldi ZH, Driessen H, Srinivasan N: Three-dimensional model and quaternary structure of the human eye lens protein yS-crystallin based on β- and y-crystallin X-ray coordinates and Ultracentrifugation. Protein Sc/1994, 3:184-186.
33. Wu Z, Johnson KW, Goldstein B, Choi Y, Eaton SF. Laue TM, Ciardelli TL: Solution assembly of a soluble, heteromeric, high affinity interleukin-2 receptor complex. 1 Bio/ Chem 1995, 270:16039-16044. In this biophysical study, the authors report the use of coiled-coil (leucine zipper) molecular recognition for the solution assembly of stable, high affinity, heteromeric interleukin-2 receptor complexes. Interleukin-2 receptor and extracellular domains, each fused to seven coiled-coil heptad repeats, resulted in the formation of heteromeric complexes that bound interleukin-2 in a cooperative fashion and with much higher affinity than similar homomeric complexes.
34. Correia JJ, Gilbert SP, Moyer ML, Johnson KA: Sedimentation studies on the kinesin motor domain constructs K401, K366 and K341. Biochemistry 1995, 34:4898-4907. AU studies of bacterially expressed kinesin motor domains revealed that domain K401 is predominantly a dimer in solution but is able to associate into higher oligomers by a 1 -2-4 mechanism. Values of the dissociation constant in the presence and absence of ATP were obtained. A good discussion of experimental procedure is presented.
35. Hensley R McDevitt PJ, Brooks I, Trill JJ, Field JA, McNulty DE, Connor JR, Griswold DE, Kumar NV, Kopple KD et al.: THe soluble form of E-selectin is an asymmetric monomer: expression, purification, and characterizion of the recombinant protein. J Biol Chem 1994, 269:23949-23958.
36. Venugopal MG, Ramshaw JAM, Braswell E, Zhu D, Brodsky B: Electrostatic interactions in collagen-like triple-helical peptides. Biochemistry 1994, 33:7948-7956.
37. Kirn S, Tsukiyama T, Lewis MS, Wu C: Interaction of the DMAbinding domain of Drosophila heat shock factor with its cognate DMA site: a thermodynamic analysis using analytical Ultracentrifugation. Protein Sei 1994, 3:1040-1050.
38. Stafford WF, Mabuchi K, Takahashi K, Toa T: Physical characterization of calponin. J Biol Chem 1995, 270:10576-10579. This reference is discussed in detail in the text. It is a classic example of how AU can be used to determine size and shape of a macromolecule.
39. Stafford WF III, Liu S: A real-time video-based Rayleigh optical system for an analytical ultracentrifuge allowing imaging of the entire centrifuge cell [abstract]. Biophys J 1992, 61:A476
40. Philo JS, Wen J, Wypych J, Schwartz MG, Mendiaz E, Langley K: Human stem cell factor dimer forms a complex with two molecules of the extracellular domain of its receptor, Kit j Biol Chem 1996, 271:6895-6902.
41. The National Analytical Ultracentrifugation Facility at the University of Connecticut on World Wide Web URL: http://gopher.uconn.edu :80/~wwwbtotc/uaf.html
42. The UK National Centre for Macromolecular Hydrodynamics (NCMH) on World Wide Web URL: http://www.ccc.nottingham.ac.uk/-~sczles/ncmhpage.html