NDLI: Site-specific contributions to the pH dependence of protein stability.

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Site-specific contributions to the pH dependence of protein stability.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Crowhurst, Karin A. Kay, Lewis E. Tollinger, Martin Forman-kay, Julie D.
Description	Author Affiliation: Tollinger M ( Department of Structural Biology and Biochemistry, Hospital for Sick Children, Toronto, ON, Canada M5G 1X8.);
Abstract	Understanding protein stability is a significant challenge requiring characterization of interactions within both folded and unfolded states. Of these, electrostatic interactions influence ionization equilibria of acidic and basic groups and diversify their pK(a) values. The pH dependence of the thermodynamic stability (Delta G(FU)) of a protein arises as a consequence of differential pK(a) values between folded and unfolded states. Previous attempts to calculate pH-dependent contributions to stability have been limited by the lack of experimental unfolded state pK(a) values. Using recently developed NMR spectroscopic methods, we have determined residue-specific pK(a) values for a thermodynamically unstable Src homology 3 domain in both states, enabling the calculation of the pH dependence of stability based on simple analytical expressions. The calculated pH stability profile obtained agrees very well with experiment, unlike profiles derived from two current models of electrostatic interactions within unfolded states. Most importantly, per-residue contributions to the pH dependence of Delta G(FU) derived from the data provide insights into specific electrostatic interactions in both the folded and unfolded states and their roles in protein stability. These interactions include a hydrogen bond between the Asp-8 side-chain and the Lys-21 backbone amide group in the folded state, which represents a highly conserved interaction in Src homology 3 domains.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	8
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Proteins Chemistry Animals Biophysical Phenomena Biophysics Drosophila Proteins Genetics Drug Stability Hydrogen-Ion Concentration Models, Molecular Mutagenesis, Site-Directed Nuclear Magnetic Resonance, Biomolecular Protein Conformation Protein Folding Recombinant Proteins Static Electricity Thermodynamics Src Homology Domains Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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