Determination of sedimentation coefficients for small peptides

Biophysical Journal
P SchuckG J Howlett

Abstract

Direct fitting of sedimentation velocity data with numerical solutions of the Lamm equations has been exploited to obtain sedimentation coefficients for single solutes under conditions where solvent and solution plateaus are either not available or are transient. The calculated evolution was initialized with the first experimental scan and nonlinear regression was employed to obtain best-fit values for the sedimentation and diffusion coefficients. General properties of the Lamm equations as data analysis tools were examined. This method was applied to study a set of small peptides containing amphipathic heptad repeats with the general structure Ac-YS-(AKEAAKE)nGAR-NH2, n = 2, 3, or 4. Sedimentation velocity analysis indicated single sedimenting species with sedimentation coefficients (s(20,w) values) of 0.37, 0.45, and 0.52 S, respectively, in good agreement with sedimentation coefficients predicted by hydrodynamic theory. The described approach can be applied to synthetic boundary and conventional loading experiments, and can be extended to analyze sedimentation data for both large and small macromolecules in order to define shape, heterogeneity, and state of association.

References

Jul 1, 1976·Biophysical Chemistry·W K SartoryJ P Breillatt
May 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·R L JacksonA M Gotto
Feb 1, 1967·Biopolymers·V BloomfieldK E Van Holde
Aug 1, 1994·Biophysical Journal·J Garcia de la TorreJ J Lopez Cascales
Jan 1, 1997·European Biophysics Journal : EBJ·J García de la TorreS E Harding

❮ Previous
Next ❯

Citations

Mar 20, 2009·European Biophysics Journal : EBJ·Helmut CölfenBorries Demeler
Aug 1, 2009·European Biophysics Journal : EBJ·Patrick H BrownPeter Schuck
Mar 27, 2004·Biophysical Chemistry·Thomas P Moody, Harvey K Shepard
Jan 12, 2002·Current Opinion in Structural Biology·T Laue
Dec 1, 2004·Drug Discovery Today. Technologies·Tom Laue
May 29, 2015·Biotechnology, Biotechnological Equipment·Nur Royhaila MohamadRoswanira Abdul Wahab
Mar 19, 2013·Analytical Biochemistry·Daniel F LyonsJames L Cole
Jun 26, 2001·Biophysical Journal·D M HattersG J Howlett
Apr 5, 2003·The Journal of Biological Chemistry·Anthony H MerrySimon J Davis
Dec 26, 2001·The Journal of Biological Chemistry·Danny M HattersGeoffrey J Howlett
May 21, 2008·Current Protocols in Immunology·Patrick H BrownPeter Schuck
Jul 14, 2018·European Biophysics Journal : EBJ·Robert T WrightJohn J Correia
Feb 2, 2020·European Biophysics Journal : EBJ·Maximilian J UttingerWolfgang Peukert
Jul 12, 2001·The Journal of Biological Chemistry·D M HattersG J Howlett
Jan 24, 2008·Langmuir : the ACS Journal of Surfaces and Colloids·Nitish NairMichael S Strano
Aug 28, 2009·The Journal of Physical Chemistry. B·Zhenli Luo, Guangzhao Zhang
Oct 21, 1999·Methods : a Companion to Methods in Enzymology·G RivasA P Minton
Jul 13, 2000·Biochemistry·D M HattersG J Howlett

❮ Previous
Next ❯

Related Concepts

Related Feeds

Cajal Bodies & Gems

Cajal bodies or coiled bodies are dense foci of coilin protein. Gemini of Cajal bodies, or gems, are microscopically similar to Cajal bodies. It is believed that Cajal bodies play important roles in RNA processing while gems assist the Cajal bodies. Find the latest research on Cajal bodies and gems here.