- About this Journal ·
- Abstracting and Indexing ·
- Aims and Scope ·
- Article Processing Charges ·
- Articles in Press ·
- Author Guidelines ·
- Bibliographic Information ·
- Citations to this Journal ·
- Contact Information ·
- Editorial Board ·
- Editorial Workflow ·
- Free eTOC Alerts ·
- Publication Ethics ·
- Reviewers Acknowledgment ·
- Submit a Manuscript ·
- Subscription Information ·
- Table of Contents
Journal of Amino Acids
Volume 2012 (2012), Article ID 565404, 11 pages
On the Hydration State of Amino Acids and Their Derivatives at Different Ionization States: A Comparative Multinuclear NMR and Crystallographic Investigation
Section of Organic Chemistry and Biochemistry, Department of Chemistry, University of Ioannina, 45110 Ioannina, Greece
Received 15 December 2011; Accepted 8 March 2012
Academic Editor: Heather M. Wallace
Copyright © 2012 Charalampos G. Pappas et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- G. A. Jeffrey and W. Saenger, Hydrogen Bonding in Biological Structures, Springer, New York, NY, USA, 1991.
- I. P. Gerothanassis, “Multinuclear and multidimensional NMR methodology for studying individual water molecules bound to peptides and proteins in solution: principles and applications,” Progress in Nuclear Magnetic Resonance Spectroscopy, vol. 26, no. 3, pp. 171–237, 1994.
- G. D. Rose and R. Wolfenden, “Hydrogen bonding, hydrophobicity, packing, and protein folding,” Annual Review of Biophysics and Biomolecular Structure, vol. 22, pp. 381–415, 1993.
- Y. Levy and J. N. Onuchic, “Water mediation in protein folding and molecular recognition,” Annual Review of Biophysics and Biomolecular Structure, vol. 35, pp. 389–415, 2006.
- Y. Levy, J. Jortner, and O. M. Becker, “Solvent effects on the energy landscapes and folding kinetics of polyalanine,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 5, pp. 2188–2193, 2001.
- J. C. Covalt, M. Roy, and P. A. Jennings, “Core and surface mutations affect folding kinetics, stability and cooperativity in IL-1β: does alteration in buried water play a role?” Journal of Molecular Biology, vol. 307, no. 2, pp. 657–669, 2001.
- M. S. Cheung, A. E. García, and J. N. Onuchic, “Protein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after the structural collapse,” Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 2, pp. 685–690, 2002.
- Y. Van Haverbeke, R. N. Muller, and L. Vander Elst, “pH-induced motional and conformational changes of amino acids. A reexamination by deuterium longitudinal nuclear relaxation,” Journal of Physical Chemistry, vol. 88, no. 21, pp. 4978–4980, 1984.
- A. Spisni, E. D. Gotsis, and D. Fiat, “17O NMR investigation of the hydration of L-Alanine and L-Proline in water/Me2SO mixtures,” Biochemical and Biophysical Research Communications, vol. 135, no. 2, pp. 363–366, 1986.
- J. Lauterwein, I. P. Gerothanassis, R. N. Hunston, and M. Schumacher, “17O NMR relaxation times of the protein amino acids in aqueous solution. Estimation of the relative hydration numbers in the cationic, anionic, and zwitterionic forms,” Journal of Physical Chemistry, vol. 95, no. 9, pp. 3804–3811, 1991.
- A. N. Troganis, C. Tsanaktsidis, and I. P. Gerothanassis, “14N NMR relaxation times of several protein amino acids in aqueous solution—comparison with 17O NMR data and estimation of the relative hydration numbers in the cationic and zwitterionic forms,” Journal of Magnetic Resonance, vol. 164, no. 2, pp. 294–303, 2003.
- I. P. Gerothanassis, “Oxygen-17 NMR spectroscopy: basic principles and applications (part II),” Progress in Nuclear Magnetic Resonance Spectroscopy, vol. 57, no. 1, pp. 1–110, 2010.
- I. P. Gerothanassis, “Oxygen-17 NMR spectroscopy: basic principles and applications (Part I),” Progress in Nuclear Magnetic Resonance Spectroscopy, vol. 56, no. 2, pp. 95–197, 2010.
- J. L. Hollenberg and J. B. Ifft, “Hydration numbers by near-infrared spectrophotometry. 1. Amino acids,” Journal of Physical Chemistry, vol. 86, no. 11, pp. 1938–1941, 1982.
- B. Hernández, F. Pflüger, M. Nsangou, and M. Ghomi, “Vibrational analysis of amino acids and short peptides in hydrated media. IV. amino acids with hydrophobic side chains: L-Alanine, L-Valine, and L-Isoleucine,” Journal of Physical Chemistry B, vol. 113, no. 10, pp. 3169–3178, 2009.
- R. M. Balabin, “The first step in glycine solvation: the glycine-water complex,” Journal of Physical Chemistry B, vol. 114, no. 46, pp. 15075–15078, 2010.
- M. J. Locke and R. T. McIver, “Effect of solvation on the acid/base properties of glycine,” Journal of the American Chemical Society, vol. 105, no. 13, pp. 4226–4232, 1983.
- J. L. Alonso, E. J. Cocinero, A. Lesarri, M. E. Sanz, and J. C. López, “The glycine-water complex,” Angewandte Chemie—International Edition, vol. 45, no. 21, pp. 3471–3474, 2006.
- D. Fiat, T. E. St Amour, M. I. Burgar, A. Steinschneider, B. Valentine, and D. Dhawan, “17O nuclear magnetic resonance and its biological applications,” The Bulletin of Magnetic Resonance, vol. 1, p. 18, 1980.
- J. G. Pearson and E. Oldfield, “17O NMR: applications in biochemistr,” in Encyclopedia of Nuclear Magnetic Resonance, D. M. Grant and R. K. Harris, Eds., pp. 3440–3443, John Wiley & Sons, 1995.
- D. W. Boykin, 17O NMR Spectroscopy in Organic Chemistry, CRC Press, Boston, Mass, USA, 1991.
- S. Berger, S. Braun, and H. O. Kalinowski, NMR Spectroscopy of Non-Metallic Elements, John Wiley & Sons, Chichester, UK, 1997.
- J. Lauterwein, I. P. Gerothanassis, and R. N. Hunston, “17O NMR of enriched acetic-acid, glycine, glutamic-acid and aspartic-acid in aqueous-solution.1. Chemical-shift studies,” Helvetica Chimica Acta, vol. 65, no. 6, pp. 1764–1773, 1982.
- J. Lauterwein, I. P. Gerothanassis, and R. N. Hunston, “17O NMR of enriched acetic-acid, glycine, glutamic-acid and aspartic-acid in aqueous-solution.2. Relaxation studies,” Helvetica Chimica Acta, vol. 65, no. 6, pp. 1774–1784, 1982.
- A. Steinschneider, M. I. Burgar, A. Buku, and D. Fiat, “Labeling of amino acids and peptides with isotopic oxygen as followed by 17O NMR,” International Journal of Peptide and Protein Research, vol. 18, no. 3, pp. 324–333, 1981.
- B. Valentine, T. S. Amour, R. Walter, and D. Fiat, “pH dependence of oxygen-17 chemical shifts and linewidths of l-alanine and glycine,” Journal of Magnetic Resonance, vol. 38, no. 3, pp. 413–418, 1980.
- G. W. Kabalka and N. M. Goudgaon, “17O enrichment methods,” in 17O NMR Spectroscopy in Organic Chemistry, D. W. Boykin, Ed., chapter 2, pp. 21–37, CRC Press, Boston, Mass, USA, 1991.
- T. Karayannis, I. P. Gerothanassis, M. Sakarellos-Daitsiotis, C. Sakarellos, and M. Marraud, “17O- and 14N-nmr studies of leu-enkephalin and enkephalin-related fragments in aqueous solution,” Biopolymers, vol. 29, no. 2, pp. 423–439, 1990.
- J. Reuben, “Hydrogen-bonding effects on oxygen-17 chemical shifts,” Journal of the American Chemical Society, vol. 91, no. 21, pp. 5725–5729, 1969.
- J. Tritt Goc and D. Fiat, “Determination of dynamic parameters in amino-acids from 17O NMR line-width measurements,” Magnetic Resonance in Chemistry, vol. 29, no. 2, pp. 156–163, 1991.
- D. E. Woessner, “Nuclear magnetic dipole-dipole relaxation in molecules with internal motion,” The Journal of Chemical Physics, vol. 42, no. 6, pp. 1855–1859, 1965.
- P. G. Takis, V. S. Melissas, and A. N. Troganis, private communication, 2011.
- C. H. Gorbitz, “Hydrogen-bond distances and angles in the structures of amino-acids and peptides,” Acta Crystallogrica B, vol. 45, pp. 390–395, 1989.
- E. Arunan, G. R. Desiraju, R. A. Klein et al., “Defining the hydrogen bond: an account (IUPAC Technical Report),” Pure and Applied Chemistry, vol. 83, no. 8, pp. 1619–1636, 2011.
- C. B. Aakeröy and K. R. Seddon, “The hydrogen bond and crystal engineering,” Chemical Society Reviews, vol. 22, no. 6, pp. 397–407, 1993.
- T. Steiner, “The hydrogen bond in the solid state,” Angewandte Chemie—International Edition, vol. 41, no. 1, pp. 49–76, 2002.
- R. Taylor, O. Kennard, and W. Versichel, “Geometry of the hydrogen bond. 2. Three-center (“bifurcated”) and four-center ((“trifurcated”) bonds,” Journal of the American Chemical Society, vol. 106, no. 1, pp. 244–248, 1984.
- L. Infantes and W. D. S. Motherwell, “Hydrogen bond competition between chemical groups: new methodology and the Cambridge Structural Database,” Zeitschrift fur Kristallographie, vol. 220, no. 4, pp. 333–339, 2005.
- R. Taylor, O. Kennard, and W. Versichel, “The geometry of the hydrogen-bond .3. Hydrogen-bond distances and angles,” Acta Crystallographica B, vol. 40, pp. 280–288, 1984.
- G. N. J. Port and A. Pullman, “Quantum-mechanical studies of environmental effects on biomolecules. III. Ab-initio model studies of hydration of peptides and proteins,” International Journal of Quantum Chemistry, vol. 8, supplement 1, pp. 21–32, 1974.
- G. A. Jeffrey and H. Maluszynska, “The stereochemistry of the water molecules in the hydrates of small biological molecules,” Acta Crystallographica. Section B, vol. 46, part 4, pp. 546–549, 1990.
- C. H. Görbitz and M. C. Etter, “Hydrogen bonds to carboxylate groups. Syn/anti distributions and steric effects,” Journal of the American Chemical Society, vol. 114, no. 2, pp. 627–631, 1992.
- T. F. Koetzle and M. S. Lehmann, “The hydrogen bond—recent developments,” in Theory and Experiments, P. Schuster, G. Zundel, and C. Sandorfy, Eds., chapter 2, pp. 457–469, North Holland, Amsterdam, The Netherlands, 1976.
- S. Xu, J. M. Nilles, and K. H. Bowen, “Zwitterion formation in hydrated amino acid, dipole bound anions: how many water molecules are required?” The Journal of Chemical Physics, vol. 119, no. 20, pp. 10696–10701, 2003.
- S. Tiwari, P. C. Mishra, and S. Suhai, “Solvent effect of aqueous media on properties of glycine: significance of specific and bulk solvent effects, and geometry optimization in aqueous media,” International Journal of Quantum Chemistry, vol. 108, no. 5, pp. 1004–1016, 2008.
- S. M. Bachrach, “Microsolvation of glycine: a DFT study,” Journal of Physical Chemistry A, vol. 112, no. 16, pp. 3722–3730, 2008.
- A. E. García and J. N. Onuchic, “Folding a protein in a computer: an atomic description of the folding/unfolding of protein A,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 2, pp. 13898–13903, 2003.
- A. C. De Dios, “Ab initio calculations of the NMR chemical shift,” Progress in Nuclear Magnetic Resonance Spectroscopy, vol. 29, no. 3-4, pp. 229–278, 1996.
- R. A. Klein, B. Mennucci, and J. Tomasi, “Ab initio calculations of 17O NMR-chemical shifts for water. The limits of PCM theory and the role of hydrogen-bond geometry and cooperativity,” Journal of Physical Chemistry A, vol. 108, no. 27, pp. 5851–5863, 2004.
- A. Klamt, B. Mennucci, J. Tomasi et al., “On the performance of continuum solvation methods. A comment on “Universal Approaches to Solvation Modeling”,” Accounts of Chemical Research, vol. 42, no. 4, pp. 489–492, 2009.
- V. G. Malkin, O. L. Malkina, G. Steinebrunner, and H. Huber, “Solvent effect on the NMR chemical shieldings in water calculated by a combination of molecular dynamics and density functional theory,” Chemistry, vol. 2, pp. 452–457, 1996.
- G. Wu, “Solid-state 17O NMR studies of organic and biological molecules,” Progress in Nuclear Magnetic Resonance Spectroscopy, vol. 52, no. 2-3, pp. 118–169, 2008.