help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Originally published as Biophys J. BioFAST on December 30, 2005.
doi:10.1529/biophysj.105.074310
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
biophysj.105.074310v1
90/6/2164    most recent
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 Kameyama, K.
Right arrow Articles by Minton, A. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kameyama, K.
Right arrow Articles by Minton, A. P.
Biophysical Journal 90:2164-2169 (2006)
© 2006 The Biophysical Society

Rapid Quantitative Characterization of Protein Interactions by Composition Gradient Static Light Scattering

Keiichi Kameyama and Allen P. Minton

Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U.S. Department of Health and Human Services, Bethesda, Maryland

Correspondence: Address reprint requests to Dr. Allen P. Minton, Bldg. 8, Rm. 226, National Institutes of Health, Bethesda, MD 20892-0830. Tel.: 301-496-3604; E-mail: minton{at}helix.nih.gov.

Two new applications of the recently developed technique of composition gradient static light scattering (CG-SLS) are presented. 1), The method is demonstrated to be capable of detecting and quantitatively characterizing reversible association of chymotrypsin and bovine pancreatic trypsin inhibitor in a solution mixture and simultaneously occurring reversible self-association of chymotrypsin at low pH in the same mixture. The values of equilibrium constants for both self- and heteroassociation may be determined with reasonable precision from the analysis of data obtained from a single experiment requiring <15 min and <1 mg of each protein. 2), Analysis of the results of a single CG-SLS experiment carried out on Ftsz, a protein that self-associates to form linear oligomers of indefinite size in the presence of guanosine diphosphate, yields the dependence of the equilibrium constant for monomer addition upon oligomer size.




This article has been cited by other articles:


Home page
 Biophys. JHome page
T. E. Williamson, B. A. Craig, E. Kondrashkina, C. Bailey-Kellogg, and A. M. Friedman
Analysis of Self-Associating Proteins by Singular Value Decomposition of Solution Scattering Data
Biophys. J., June 15, 2008; 94(12): 4906 - 4923.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2006 by the Biophysical Society.