Relation between peptide backbone solvation and the energetics of peptide hydrogen bonds

Biophysical Chemistry

Volumn 101-102, Issue , 2002, Pages 203-210

  Baldwin, Robert L ^a  

^a STANFORD UNIVERSITY   (United States)

Author keywords

Alanine helix; Electrostatic solvation; Enthalpy change; H bond inventory

Indexed keywords

ALANINE; HYDROGEN; PEPTIDE; WATER;

ALPHA HELIX; ARTICLE; ELECTRICITY; ENERGY; ENERGY TRANSFER; ENTHALPY; HYDROGEN BOND; PRIORITY JOURNAL; SOLVATION; STANDARD; CHEMISTRY;

HYDROGEN BONDING; PEPTIDES;

EID: 0037059044     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(02)00195-3     Document Type: Article

References (39)

1. Schellman J.A. The stability of hydrogen-bonded peptide structures in aqueous solution. C.R. Trav. Lab. Carslberg Ser. Chim. 29:1955;230-259.
2. Baldwin R.L. α-Helix formation by peptides of defined sequence. Biophys. Chem. 55:1995;127-135.
3. Aurora R., Rose G.D. Helix capping. Protein Sci. 7:1998;21-38.
4. Zimm B.H., Bragg J.K. Theory of the phase transition between helix and random coil in polypeptide chains. J. Chem. Phys. 31:1959;526-535.
5. Lifson S., Roig A. On the theory of helix-coil transition in polypeptides. J. Chem. Phys. 34:1961;1963-1974.
6. Klotz I.M., Franzen J.S. Hydrogen bonds between model peptide groups in solution. J. Am. Chem. Soc. 84:1962;3461-3466.
7. Klotz I.M. Non-covalent bonds in protein structure, Brookhaven. Symp. Biol. 13:1960;25-48.
8. Shirley B.A., Stanssens P., Hahn U., Pace C.N. Contribution of hydrogen bonding to conformational stability of ribonuclease T1. Biochemistry. 31:1992;725-732.
9. Honig B., Yang A.-S. Free energy balance in protein folding. Adv. Protein Chem. 46:1995;27-58.
10. Marqusee S., Robbins V.H., Baldwin R.L. Unusually stable helix formation in short alanine-based peptides. Proc. Natl. Acad. Sci. USA. 86:1989;5286-5290.
11. Rohl C.A., Chakrabartty A., Baldwin R.L. Helix propagation and N-cap propensities of amino acids measured in alanine-based peptides in 40% trifluoroethanol. Protein Sci. 5:1996;2623-2637.
12. Spek E.J., Olson C.A., Shi Z., Kallenbach N.R. Alanine is an intrinsic α-helix stabilizing amino acid. J. Am. Chem. Soc. 121:1999;5571-5572.
13. Lopez M., Chin D.-H., Baldwin R.L., Makhatadze G.I. The enthalpy of the alanine peptide helix measured by isothermal titration calorimetry using metal-binding to induce helix formation. Proc. Natl. Acad. Sci. USA. 99:2002;1298-1302.
14. Scholtz J.M., Marqusee S., Baldwin R.L., et al. Calorimetric determination of the enthalpy change for the α-helix to coil transition of an alanine peptide in water. Proc. Natl. Acad. Sci. USA. 88:1991;2854-2858.
15. Richardson J.M., McMahon K.W., MacDonald C.C., Makhatadze G.I. MEARA sequence repeat of human CstF-64 polyadenylation factor is helical in solution. A spectroscopic and calorimetric study. Biochemistry. 38:1999;12869-12875.
16. Ben-Tal N., Sitkoff D., Topol I.A., Yang A.-S., Burt S.K., Honig B. Free energy of amide hydrogen bond formation in vacuum, in water and in liquid alkane solution. J. Phys. Chem. B. 101:1997;450-457.
17. Mitchell J.B.O., Price S.L. On the relative strengths of amide.amide and amide.water hydrogen bonds. Chem. Phys. Lett. 180:1991;517-523.
18. Fersht A.R. The hydrogen bond in molecular recognition. Trends Biochem. Sci. 12:1987;301-304.
19. Atkins P.W. Physical Chemistry. Fifth Ed. 1996;Freeman and Co, New York.
20. Ben-Naim A., Marcus Y. Solvation thermodynamics of non-ionic solutes. J. Chem. Phys. 81:1984;2016-2027.
21. Lee B. Analyzing solvent reorganization and hydrophobicity. Methods Enzymol. 259:1995;555-577.
22. Sitkoff D., Sharp K.A., Honig B. Accurate calculation of hydration free energies using macroscopic solvent models. J. Phys. Chem. 98:1994;1978-1988.
23. Makhatadze G.I., Privalov P.L. Contribution of hydration to protein folding thermodynamics. I. The enthalpy of hydration. J. Mol. Biol. 232:1993;639-659.
24. Avbelj F., Luo P., Baldwin R.L. Energetics of the interaction between water and the helical peptide group and its role in determining helix propensities. Proc Natl. Acad. Sci. USA. 97:2000;10786-10791.
25. Wolfenden R. Interaction of the peptide bond with solvent water: a vapor phase analysis. Biochemistry. 17:1978;201-204.
26. Della Gatta G., Barone G., Elia V. Enthalpies of solvation for N-alkylamides in water and in carbon tetrachloride at 25 °C. J. Solution Chem. 15:1986;157-167.
27. Dunitz J.D. The entropic cost of bound water in crystals and biomolecules. Science. 264:1994;670.
28. Rashin A.A., Honig B. Reevaluation of the Born model of ion hydration. J. Phys. Chem. 89:1985;5588-5593.
29. Henn A.R., Kauzmann W. Equation of state of a random network, continuum model of liquid water. J. Phys. Chem. 93:1989;3770-3783.
30. Avbelj F. Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins. J. Mol. Biol. 300:2000;1335-1359.
31. Florian J., Warshel A. Langevin dipoles model for ab initio calculations of chemical processes in solution: parameterization and application to hydration free energies of neutral and ionic solutes and conformational analysis in aqueous solution. J. Phys. Chem. B. 101:1997;5583-5595.
32. Cramer C.J., Truhlar D.G. An SCF solvation model for the hydrophobic effect and absolute free energies of aqueous solvation. Science. 256:1992;213-217.
33. Pauling L. The Nature of the Chemical Bond, Second Edition. 1940;284-327 Cornell Univ. Press, Ithaca, NY.
34. Lifson S., Hagler A.T., Dauber P. Consistent force field studies of intermolecular forces in hydrogen-bonded crystals. 1. Carboxylic acids, amides and the C=O ⋯⋯⋯ H hydrogen bonds. J. Am. Chem. Soc. 101:1979;5111-5121.
35. Weinhold F. Nature of H-bonding in clusters, liquids, and enzymes: An ab initio, natural bond orbital perspective. J. Mol. Struct. (Theochem). 398-399:1997;181-197.
36. Dannenberg J.J., Haskamp L., Masunov A. Are hydrogen bonds covalent or electrostatic? A molecular orbital comparison of molecules in electric fields and H-bonding environments. J. Phys. Chem. A. 103:1999;7083-7086.
37. Kobko N., Paraskevas L., Del Rio E., Dannenberg J.J. Cooperativity in amide hydrogen-bonding chains: implications for protein folding models. J. Am. Chem. Soc. 123:2001;4348-4349.
38. Avbelj F., Baldwin R.L. Role of backbone solvation in determining thermodynamic (-propensities of the amino acids. Proc. Natl. Acad. Sci. USA. 99:2002;1309-1313.
39. Avbelj F., Fele L. Role of main-chain electrostatics, hydrophobic effect and side-chain conformational entropy in determining the secondary structure of proteins. J. Mol. Biol. 279:1998;665-684.