Summary
The amino acid side chains of Ser, Thr and Tyr contain the hydroxyl functional group that is characteristic of alcohols, and a variety of different alcohols are used either as structure-inducing or denaturing co-solvents in physical-chemical studies of proteins. This article surveys selected aspects of the influence of protein-intrinsic and — extrinsic hydroxyl groups on studies of the solvation of peptides and proteins by nuclear magnetic resonance (NMR) spectroscopy.
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References
Bothner-By, A.A., Stephens, R.L., Lee, J., Warren, C.D. and Jeanloz, R.W. (1984) Structure determination of a tetrasaccharide: transient nuclear Overhauser effects in the rotating frame. J. Am. Chem. Soc.106: 811–813.
Brunne, R.M., Liepinsh, E., Otting, G., Wüthrich, K. and van Gunsteren, W.F. (1993) Hydration of proteins. A comparison of experimental residence times of water molecules solvating the bovine pancreatic trypsin inhibitor with theoretical model calculations. J. Mol. Biol.231: 1040–1048.
Buck, M., Radford, S.E. and Dobson, C.M. (1993) A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding. Biochemistry32: 669–678.
Clore, G.M., Bax, A., Wingfield, P.T. and Gronenborn, A.M. (1990) Identification and localization of bound internal water in the solution structure of Interleukin lb by heteronuclear three-dimensional H rotating-frame Overhauser t5N-H multiple quantum coherence NMR spectroscopy. Biochemistry29: 5671–5676.
Forman-Kay, J.D., Gronenbom, A.M., Wingfield, P.T. and Clore, G.M. (1991) Determination of the positions of bound water molecules in the solution structure of reduced human thioredoxin by heteronuclear three-dimensional nuclear magnetic resonance spectroscopy. J. Mol. Biol.220: 209–216.
Kubinec, M.G. and Wemmer, D.E. (1992) NMR evidence for DNA-bound water in solution. J. Amer. Chem. Soc.114: 8739–8740.
Liepinsh, E., Otting, G. and Wüthrich, K. (1992a) NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins. J. Biomol. NMR2: 447–465.
Liepinsh, E., Otting, G. and Wüthrich, K. (1992b) NMR observation of individual molecules of hydration water bound to DNA duplexes: direct evidence for a spine of hydration water present in aqueous solution. Nucl. Acids Res.20: 6549–6553.
Liepinsh, E., Rink, H., Otting, G. and Wüthrich, K. (1993) Contribution from hydration of carboxylate groups to the spectrum of water-polypeptide proton-proton Overhauser effects in aqueous solution. J. Biomol. NMR3: 253–257.
Otting, G. and Wüthrich, K. (1989) Studies of protein hydration in aqueous solution by direct NMR observation of individual protein-bound water molecules. J. Amer. Chem. Soc.111: 1871–1875.
Otting, G., Liepinsh, E. and Wüthrich, K. (1991a) Protein hydration in aqueous solution. Science254: 974–980.
Otting, G., Liepinsh, E. and Wüthrich, K. (1991b) Proton exchange with internal water molecules in the protein BPTI in aqueous solution. J. Amer. Chem. Soc.113: 4363–4364.
Otting, G., Liepinsh, E., Farmer II, B.T. and Wüthrich, K. (1991c) Protein hydration studied with homonuclear 3D H NMR experiments. J. Biomol. NMR1: 209–215.
Otting, G., Liepinsh, E. and Wüthrich, K. (1992) Polypeptide hydration in mixed solvents at low temperatures. J. Amer. Chem. Soc.114: 7093–7095.
Pan, Y. and Briggs, M.S. (1992) Hydrogen exchange in native and alcohol forms of ubiquitin. Biochemistry31: 11405–11412.
Qian, Y.Q., Otting, G. and Wüthrich, K. (1993) NMR detection of hydration water in the intermolecular interface of a protein-DNA complex. J. Amer. Chem. Soc.115: 1189–1190.
Storrs, R.W., Truckses, D. and Wemmer, D.E. (1992) Helix propagation in trifluoroethanol solutions. Biopolymers32: 1695–1702.
Timasheff, S.N. (1992) Water as ligand: preferential binding and exclusion of denaturants in protein unfolding. Biochemistry31: 9857–9864.
Wüthrich, K. (1986) NMR of proteins and nucleic acids. Wiley, New York.
Wüthrich, K. (1993) Hydration of biological macromolecules in solution, surface structure and molecular recognition. In: DNA and chromosomes. 58th Cold Spring Harbor Laboratory Symposium on Quantitative Biology, in press.
Wüthrich, K. and Otting, G. (1992) Studies of protein hydration in aqueous solution by highresolution nuclear magnetic resonance spectroscopy. Int. J. Quant. Chem.42: 1553–1561.
Wüthrich, K., Otting, G. and Liepinsh, E. (1992) Protein hydration in aqueous solution. Faraday Discuss. 93: 35–45.
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© 1994 Birkhäuser Verlag Basel/Switzerland
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Wüthrich, K. (1994). NMR, alcohols, protein solvation and protein denaturation. In: Jansson, B., Jörnvall, H., Rydberg, U., Terenius, L., Vallee, B.L. (eds) Toward a Molecular Basis of Alcohol Use and Abuse. Experientia, vol 71. Birkhäuser Basel. https://doi.org/10.1007/978-3-0348-7330-7_26
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DOI: https://doi.org/10.1007/978-3-0348-7330-7_26
Publisher Name: Birkhäuser Basel
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