Protein Science, Vol 5, Issue 7 1229-1239, Copyright © 1996 by Cold Spring Harbor Laboratory Press

ARTICLE

Energetics of hydrogen bonding in proteins: A model compound study

S. M. HABERMANN and K. P. MURPHY
Department of Biochemistry, University of Iowa, Iowa City, Iowa 52242

Differences in the energetics of amide-amide and amide-hydroxyl hydrogen bonds in proteins have been explored from the effect of hydroxyl groups on the structure and dissolution energetics of a series of crystalline cyclic dipeptides. The calorimetrically determined energetics are interpreted in light of the crystal structures of the studied compounds. Our results indicate that the amide-amide and amide-hydroxyl hydrogen bonds both provide considerable enthalpic stability, but that the amide-amide hydrogen bond is about twice that of the amide-hydroxyl. Additionally, the interaction of the hydroxyl group with water is seen most readily in its contributions to entropy and heat capacity changes. Surprisingly, the hydroxyl group shows weakly hydrophobic behavior in terms of these contributions. These results can be used to understand the effects of mutations on the stability of globular proteins.
CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				S. T. Whitten, H.-W. Yang, R. O. Fox, and V. J. Hilser Exploring the impact of polyproline II (PII) conformational bias on the binding of peptides to the SEM-5 SH3 domain Protein Sci., July 1, 2008; 17(7): 1200 - 1211. [Abstract] [Full Text] [PDF]

				B. Nguyen, J. Stanek, and W. D. Wilson Binding-Linked Protonation of a DNA Minor-Groove Agent Biophys. J., February 15, 2006; 90(4): 1319 - 1328. [Abstract] [Full Text] [PDF]

				S. T. Whitten, B. Garcia-Moreno E., and V. J. Hilser Local conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins PNAS, March 22, 2005; 102(12): 4282 - 4287. [Abstract] [Full Text] [PDF]

				S. A. Larson and V. J. Hilser Analysis of the "thermodynamic information content" of a Homo sapiens structural database reveals hierarchical thermodynamic organization Protein Sci., July 1, 2004; 13(7): 1787 - 1801. [Abstract] [Full Text] [PDF]

				K. Ajroud, T. Sugimori, W. H. Goldmann, D. M. Fathallah, J.-P. Xiong, and M. A. Arnaout Binding Affinity of Metal Ions to the CD11b A-domain Is Regulated by Integrin Activation and Ligands J. Biol. Chem., June 11, 2004; 279(24): 25483 - 25488. [Abstract] [Full Text] [PDF]

				A. Baerga-Ortiz, S. Bergqvist, J. G. Mandell, and E. A. Komives Two different proteins that compete for binding to thrombin have opposite kinetic and thermodynamic profiles Protein Sci., January 1, 2004; 13(1): 166 - 176. [Abstract] [Full Text] [PDF]

				K. Takano, J. M. Scholtz, J. C. Sacchettini, and C. N. Pace The Contribution of Polar Group Burial to Protein Stability Is Strongly Context-dependent J. Biol. Chem., August 22, 2003; 278(34): 31790 - 31795. [Abstract] [Full Text] [PDF]

				E. Garcia-Hernandez, R. A. Zubillaga, E. A. Chavelas-Adame, E. Vazquez-Contreras, A. Rojo-Dominguez, and M. Costas Structural energetics of protein-carbohydrate interactions: Insights derived from the study of lysozyme binding to its natural saccharide inhibitors Protein Sci., January 1, 2003; 12(1): 135 - 142. [Abstract] [Full Text] [PDF]

				J. O. Wrabl, S. A. Larson, and V. J. Hilser Thermodynamic environments in proteins: Fundamental determinants of fold specificity Protein Sci., August 1, 2002; 11(8): 1945 - 1957. [Abstract] [Full Text] [PDF]

				R. Ragone Hydrogen-bonding classes in proteins and their contribution to the unfolding reaction Protein Sci., October 19, 2001; 10(10): 2075 - 2082. [Abstract] [Full Text] [PDF]

				J. O. Wrabl, S. A. Larson, and V. J. Hilser Thermodynamic propensities of amino acids in the native state ensemble: Implications for fold recognition Protein Sci., May 1, 2001; 10(5): 1032 - 1045. [Abstract] [Full Text]

				J. G. Pelton, D. A. Torchia, S. J. Remington, K. P. Murphy, N. D. Meadow, and S. Roseman Structures of Active Site Histidine Mutants of IIIGlc, a Major Signal-transducing Protein in Escherichia coli. EFFECTS ON THE MECHANISMS OF REGULATION AND PHOSPHORYL TRANSFER J. Biol. Chem., December 27, 1996; 271(52): 33446 - 33456. [Abstract] [Full Text] [PDF]

				M. G. Rudolph, T. Linnemann, P. Grunewald, A. Wittinghofer, I. R. Vetter, and C. Herrmann Thermodynamics of Ras/Effector and Cdc42/Effector Interactions Probed by Isothermal Titration Calorimetry J. Biol. Chem., June 22, 2001; 276(26): 23914 - 23921. [Abstract] [Full Text] [PDF]

				H. Pan, J. C. Lee, and V. J. Hilser From the Cover: Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensemble PNAS, October 24, 2000; 97(22): 12020 - 12025. [Abstract] [Full Text] [PDF]