A model-independent, nonlinear extrapolation procedure for the characterization of protein folding energetics from solvent-denaturation data

Biochemistry
B Ibarra-Molero, J M Sanchez-Ruiz

Abstract

We have characterized the guanidine-induced denaturation of hen egg white lysozyme within the 30-75 degrees C temperature range on the basis of equilibrium fluorescence measurements, unfolding assays, kinetic fluorescence measurements, and differential scanning calorimetry. Analysis of the guanidine denaturation profiles according to the linear extrapolation method yields values for the denaturation Gibbs energy which are about 15 kJ/mol lower than those derived from differential scanning calorimetry. Our results strongly suggest that this discrepancy is not due to deviations from the two-state denaturation mechanism. We propose a new method for the determination of denaturation Gibbs energies from solvent-denaturation data (the constant-delta G extrapolation procedure). It employs several solvent-denaturation profiles (obtained at different temperatures) to generate the protein stability curve at zero denaturant concentration within the -8 to 8 kJ/mol delta G range. The method is model-independent and provides a practical, nonlinear alternative to the commonly employed linear extrapolation procedure. The application of the constant-delta G method to our data suggests that the guanidine-concentration dependence of the denaturat...Continue Reading

References

Apr 5, 1992·Journal of Molecular Biology·P L Privalov, G I Makhatadze
Jul 20, 1992·Journal of Molecular Biology·G I Makhatadze, P L Privalov
Dec 5, 1991·Journal of Molecular Biology·K P Murphy, S J Gill
Jan 1, 1987·Annual Review of Biophysics and Biophysical Chemistry·J A Schellman
May 20, 1993·Journal of Molecular Biology·Y HagiharaY Goto
Jul 20, 1993·Journal of Molecular Biology·G I Makhatadze, P L Privalov
Jul 20, 1993·Journal of Molecular Biology·P L Privalov, G I Makhatadze

❮ Previous
Next ❯

Citations

Apr 16, 1998·Protein Science : a Publication of the Protein Society·G I MakhatadzeS T Thomas
Jan 13, 2004·Biochemical and Biophysical Research Communications·Montserrat Andújar-SánchezAna Cámara-Artigas
Feb 16, 1999·Biochimica Et Biophysica Acta·B Ibarra-MoleroJ M Sanchez-Ruiz
Jun 29, 2000·Trends in Biochemical Sciences·A R DinnerM Karplus
Jun 14, 2008·Proceedings of the National Academy of Sciences of the United States of America·Oyvind HalskauJose M Sanchez-Ruiz
Nov 20, 2002·Journal of Biomolecular Structure & Dynamics·Esther Anderson, B Mark Britt
May 4, 2000·Protein Science : a Publication of the Protein Society·B Ibarra-MoleroJ M Sanchez-Ruiz
Sep 25, 2003·Proceedings of the National Academy of Sciences of the United States of America·Srebrenka RobicSusan Marqusee
May 13, 2009·Journal of Biotechnology·Anchanee SangcharoenChartchai Krittanai
Oct 13, 2007·Proteins·Angel L PeyJose M Sanchez-Ruiz
Jul 19, 2006·Chembiochem : a European Journal of Chemical Biology·Irina GitlinGeorge M Whitesides
Mar 26, 2004·Biophysical Journal·Raul Perez-JimenezJose M Sanchez-Ruiz
Jun 21, 2006·Journal of Molecular Biology·David Rodriguez-LarreaJose M Sanchez-Ruiz
Nov 27, 2001·Biophysical Journal·M M Garcia-Mira, J M Sanchez-Ruiz
Sep 24, 1999·Journal of Molecular Biology·A R Dinner, M Karplus
Nov 24, 1999·The Journal of Biological Chemistry·R KleppeJ Haavik
Nov 7, 2019·The Journal of Physical Chemistry. B·Xiaochun Li-Blatter, Joachim Seelig
Aug 29, 2019·ACS Omega·Yehonatan LevartovskyUri Raviv

❮ Previous
Next ❯

Related Concepts

Related Feeds

Bacterial Cell Wall Structure (ASM)

Bacterial cell walls are made of peptidoglycan (also called murein), which is made from polysaccharide chains cross-linked by unusual peptides containing D-amino acids. Here is the latest research on bacterial cell wall structures.

Bacterial Cell Wall Structure

Bacterial cell walls are made of peptidoglycan (also called murein), which is made from polysaccharide chains cross-linked by unusual peptides containing D-amino acids. Here is the latest research on bacterial cell wall structures.