NDLI: Direct measurement of salt-bridge solvation energies using a peptide model system: implications for protein stability.

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Direct measurement of salt-bridge solvation energies using a peptide model system: implications for protein stability.

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Direct measurement of salt-bridge solvation energies using a peptide model system: implications for protein stability.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wimley, W. C. White, S. H. Gawrisch, K. Creamer, T. P.
Description	Author Affiliation: Wimley WC ( Department of Physiology and Biophysics, University of California, Irvine 92717-4560, USA.);
Abstract	The solvation energies of salt bridges formed between the terminal carboxyl of the host pentapeptide AcWL- X-LL and the side chains of Arg or Lys in the guest (X) position have been measured. The energies were derived from octanol-to-buffer transfer free energies determined between pH 1 and pH 9. 13C NMR measurements show that the salt bridges form in the octanol phase, but not in the buffer phase, when the side chains and the terminal carboxyl group are charged. The free energy of salt-bridge formation in octanol is approximately -4 kcal/mol (1 cal = 4.184 J), which is equal to or slightly larger than the sum of the solvation energies of noninteracting pairs of charged side chains. This is about one-half the free energy that would result from replacing a charge pair in octanol with a pair of hydrophobic residues of moderate size. Therefore, salt bridging in octanol can change the favorable aqueous solvation energy of a pair of oppositely charged residues to neutral or slightly unfavorable but cannot provide the same free energy decrease as hydrophobic residues. This is consistent with recent computational and experimental studies of protein stability.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	7
Volume Number	93
Language	English
Publisher	National Academy of Sciences
Publisher Date	1996-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Oligopeptides Chemistry Protein Conformation Amino Acid Sequence Amino Acids Calorimetry Chromatography, High Pressure Liquid Hydrogen-Ion Concentration Kinetics Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Chemical Synthesis Solubility Spectrometry, Mass, Fast Atom Bombardment Structure-Activity Relationship Thermodynamics Comparative Study Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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