help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Schuck, P.
Right arrow Articles by Demeler, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Schuck, P.
Right arrow Articles by Demeler, B.

Biophys J, April 1999, p. 2288-2296, Vol. 76, No. 4

Direct Sedimentation Analysis of Interference Optical Data in Analytical Ultracentrifugation

Peter Schuck* and Borries Demeler#

 *Molecular Interactions Resource, Bioengineering and Physical Science Program, ORS, National Institutes of Health, Bethesda, Maryland 20892, and  #Department of Biochemistry, University of Texas Health Sciences Center at San Antonio, San Antonio, Texas 78284 USA

Sedimentation data acquired with the interference optical scanning system of the Optima XL-I analytical ultracentrifuge can exhibit time-invariant noise components, as well as small radial-invariant baseline offsets, both superimposed onto the radial fringe shift data resulting from the macromolecular solute distribution. A well-established method for the interpretation of such ultracentrifugation data is based on the analysis of time-differences of the measured fringe profiles, such as employed in the g(s*) method. We demonstrate how the technique of separation of linear and nonlinear parameters can be used in the modeling of interference data by unraveling the time-invariant and radial-invariant noise components. This allows the direct application of the recently developed approximate analytical and numerical solutions of the Lamm equation to the analysis of interference optical fringe profiles. The presented method is statistically advantageous since it does not require the differentiation of the data and the model functions. The method is demonstrated on experimental data and compared with the results of a g(s*) analysis. It is also demonstrated that the calculation of time-invariant noise components can be useful in the analysis of absorbance optical data. They can be extracted from data acquired during the approach to equilibrium, and can be used to increase the reliability of the results obtained from a sedimentation equilibrium analysis.

Biophys J, April 1999, p. 2288-2296, Vol. 76, No. 4
© 1999 by the Biophysical Society   0006-3495/99/04/2288/09  $2.00



This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
S. Chinnaswamy, I. Yarbrough, S. Palaninathan, C. T. R. Kumar, V. Vijayaraghavan, B. Demeler, S. M. Lemon, J. C. Sacchettini, and C. C. Kao
A Locking Mechanism Regulates RNA Synthesis and Host Protein Interaction by the Hepatitis C Virus Polymerase
J. Biol. Chem., July 18, 2008; 283(29): 20535 - 20546.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
P. H. Brown and P. Schuck
Macromolecular Size-and-Shape Distributions by Sedimentation Velocity Analytical Ultracentrifugation
Biophys. J., June 15, 2006; 90(12): 4651 - 4661.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. D. Garcia, J. Otero, J. Lebowitz, P. Schuck, and B. Moss
Quaternary Structure and Cleavage Specificity of a Poxvirus Holliday Junction Resolvase
J. Biol. Chem., April 28, 2006; 281(17): 11618 - 11626.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
B. R. Burgess, P. Schuck, and D. N. Garboczi
Dissection of Merozoite Surface Protein 3, a Representative of a Family of Plasmodium falciparum Surface Proteins, Reveals an Oligomeric and Highly Elongated Molecule
J. Biol. Chem., November 4, 2005; 280(44): 37236 - 37245.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
S. Boulant, C. Vanbelle, C. Ebel, F. Penin, and J.-P. Lavergne
Hepatitis C Virus Core Protein Is a Dimeric Alpha-Helical Protein Exhibiting Membrane Protein Features
J. Virol., September 1, 2005; 79(17): 11353 - 11365.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
J. Dam, C. A. Velikovsky, R. A. Mariuzza, C. Urbanke, and P. Schuck
Sedimentation Velocity Analysis of Heterogeneous Protein-Protein Interactions: Lamm Equation Modeling and Sedimentation Coefficient Distributions c(s)
Biophys. J., July 1, 2005; 89(1): 619 - 634.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
S. A. Ali, N. Iwabuchi, T. Matsui, K. Hirota, S.-i. Kidokoro, M. Arai, K. Kuwajima, P. Schuck, and F. Arisaka
Reversible and Fast Association Equilibria of a Molecular Chaperone, gp57A, of Bacteriophage T4
Biophys. J., October 1, 2003; 85(4): 2606 - 2618.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Bernocco, B. M. Steiglitz, D. I. Svergun, M. V. Petoukhov, F. Ruggiero, S. Ricard-Blum, C. Ebel, C. Geourjon, G. Deleage, B. Font, et al.
Low Resolution Structure Determination Shows Procollagen C-Proteinase Enhancer to be an Elongated Multidomain Glycoprotein
J. Biol. Chem., February 21, 2003; 278(9): 7199 - 7205.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
C. J. Ackerman, M. M. Harnett, W. Harnett, S. M. Kelly, D. I. Svergun, and O. Byron
19 A Solution Structure of the Filarial Nematode Immunomodulatory Protein, ES-62
Biophys. J., January 1, 2003; 84(1): 489 - 500.
[Abstract] [Full Text] [PDF]


Home page
Protein Sci.Home page
J. Lebowitz, M. S. Lewis, and P. Schuck
Modern analytical ultracentrifugation in protein science: A tutorial review
Protein Sci., September 1, 2002; 11(9): 2067 - 2079.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. Josse, C. Ebel, D. Stroebel, A. Fontaine, F. Borges, A. Echalier, D. Baud, F. Renault, M. le Maire, E. Chabrieres, et al.
Oligomeric States of the Detergent-solubilized Human Serum Paraoxonase (PON1)
J. Biol. Chem., August 30, 2002; 277(36): 33386 - 33397.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
Z. F. Taraporewala, P. Schuck, R. F. Ramig, L. Silvestri, and J. T. Patton
Analysis of a Temperature-Sensitive Mutant Rotavirus Indicates that NSP2 Octamers Are the Functional Form of the Protein
J. Virol., June 14, 2002; 76(14): 7082 - 7093.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. Arthos, C. Cicala, T. D. Steenbeke, T.-W. Chun, C. D. Cruz, D. B. Hanback, P. Khazanie, D. Nam, P. Schuck, S. M. Selig, et al.
Biochemical and Biological Characterization of a Dodecameric CD4-Ig Fusion Protein. IMPLICATIONS FOR THERAPEUTIC AND VACCINE STRATEGIES
J. Biol. Chem., March 22, 2002; 277(13): 11456 - 11464.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
P. Schuck, Z. Taraporewala, P. McPhie, and J. T. Patton
Rotavirus Nonstructural Protein NSP2 Self-assembles into Octamers That Undergo Ligand-induced Conformational Changes
J. Biol. Chem., March 23, 2001; 276(13): 9679 - 9687.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
B. Franzetti, G. Schoehn, C. Ebel, J. Gagnon, R. W. H. Ruigrok, and G. Zaccai
Characterization of a Novel Complex from Halophilic Archaebacteria, Which Displays Chaperone-like Activities in Vitro
J. Biol. Chem., August 3, 2001; 276(32): 29906 - 29914.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Bernocco, S. Finet, C. Ebel, D. Eichenberger, M. Mazzorana, J. Farjanel, and D. J. S. Hulmes
Biophysical Characterization of the C-propeptide Trimer from Human Procollagen III Reveals a Tri-lobed Structure
J. Biol. Chem., December 21, 2001; 276(52): 48930 - 48936.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1999 by the Biophysical Society.