Hofmeister ions control protein dynamics

Biochimica et Biophysica Acta - General Subjects

Volumn 1830, Issue 10, 2013, Pages 4564-4572

  Szalontai, Balázs ^a   Nagy, Gergely ^a,b,d   Krumova, Sashka ^c   Fodor, Elfrieda ^a   Páli, Tibor ^a   Taneva, Stefka G ^c,e   Garab, Gyozo ^a   Peters, Judith ^b,f,g   Dér, András ^a  

^a INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^b INSTITUT LAUE LANGEVIN   (France)

^c INSTITUTE OF BIOPHYSICS AND BIOMEDICAL ENGINEERING   (Bulgaria)

^d Laboratory for Neutron Scattering Villigen   (Switzerland)

^e UNIVERSITY OF THE BASQUE COUNTRY UPV EHU   (Spain)

^f UNIV GRENOBLE ALPES   (France)

^g INSTITUT DE BIOLOGIE STRUCTURALE   (France)

Author keywords

Bacteriorhodopsin; Differential scanning calorimetry; Fourier transform infrared spectroscopy; Hofmeister effect; Neutron scattering; Protein structural fluctuation

Indexed keywords

ACETIC ACID; PERCHLORATE;

ARTICLE; CHEMICAL PHENOMENA; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; EXPERIMENTAL TEST; HOFMEISTER EFFECT; HYDROPHILICITY; HYDROPHOBICITY; INFRARED SPECTROSCOPY; MEMBRANE TRANSPORT; MICROCALORIMETRY; NEUTRON SCATTERING; PHYSICAL PARAMETERS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN WATER INTERFACIAL TENSION; TEMPERATURE DEPENDENCE;

BACTERIORHODOPSIN; DIFFERENTIAL SCANNING CALORIMETRY; FOURIER TRANSFORM INFRARED SPECTROSCOPY; HOFMEISTER EFFECT; NEUTRON SCATTERING; PROTEIN STRUCTURAL FLUCTUATION;

CALORIMETRY, DIFFERENTIAL SCANNING; IONS; NEUTRONS; PROTEINS; SCATTERING, RADIATION; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; THERMODYNAMICS;

EID: 84879491513     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2013.05.036     Document Type: Article

References (45)

1. F. Hofmeister Zur Lehre von der Wirkung der Salze. II Arch. Exp. Pathol. Pharmacol. 24 1888 247 260
2. P. Lo Nostro, and B.W. Ninham Hofmeister phenomena: an update on ion specificity in biology Chem. Rev. 112 2012 2286 2322
3. M.G. Cacace, E.M. Landau, and J.J. Ramsden The Hofmeister series: salt and solvent effects on interfacial phenomena Q. Rev. Biophys. 30 1997 241 277 (Pubitemid 27491348)
4. K.D. Collins, and M.W. Washabaugh The Hofmeister effect and the behaviour of water at interfaces Q. Rev. Biophys. 18 1985 323 422
5. P. Khoroshyy, A. Dér, and L. Zimányi Effect of Hofmeister cosolutes on the photocycle of photoactive yellow protein at moderately alkaline pH J. Photochem. Photobiol. B. 120 2013 111 119
6. +-ATPase Biophys. J. 77 1999 267 281 (Pubitemid 29305227)
7. R.M. Davidson, and S. Seneff The initial common pathway of inflammation, disease, and sudden death Entropy 14 2012 1399 1442
8. W. Kunz, P. Lo Nostro, and B.W. Ninham The present state of affairs with Hofmeister effects Curr. Opin. Colloid Interface Sci. 9 2004 1 18 (Pubitemid 39194130)
9. W. Melander, and C. Horvath Salt effects on hydrophobic interactions in precipitation and chromatography of proteins - interpretation of lyotropic series Arch. Biochem. Biophys. 183 1977 200 215 (Pubitemid 8200028)
10. M.C. Gurau, S.M. Lim, E.T. Castellana, F. Albertorio, S. Kataoka, and P.S. Cremer On the mechanism of the Hofmeister effect J. Am. Chem. Soc. 126 2004 10522 10523 (Pubitemid 39129138)
11. A. Dér, L. Kelemen, L. Fábián, S.G. Taneva, E. Fodor, T. Páli, A. Cupane, M.G. Cacace, and J.J. Ramsden Interfacial water structure controls protein conformation J. Phys. Chem. B 111 2007 5344 5350 (Pubitemid 46854526)
12. T.J. Richmond Solvent accessible surface area and excluded volume in proteins: analytical equations for overlapping spheres and implications for the hydrophobic effect J. Mol. Biol. 178 1984 63 89
13. A. Dér Salts, interfacial water and protein conformation Biotechnol. Biotechnol. Equip. 22 2008 629 633 (Pubitemid 351422066)
14. Y. Zhang, and P.S. Cremer The inverse and direct Hofmeister series for lysozyme Proc. Natl. Acad. Sci. U. S. A. 106 2010 15249 15253
15. A. Neagu, M. Neagu, and A. Dér Fluctuations and the Hofmeister effect Biophys. J. 81 2001 1285 1294 (Pubitemid 32783573)
16. W. Stoeckenius, R.H. Lozier, and R.A. Bogomolni Bacteriorhodopsin and the purple membrane of halobacteria Biochim. Biophys. Acta Rev. Bioenerg. 505 1979 215 278
17. A. Dér, and J.J. Ramsden Evidence for loosening of a protein mechanism Naturwissenschaften 85 1998 353 355 (Pubitemid 28360052)
18. S. Krimm, and A.M. Dwivedi Infrared spectrum of the purple membrane: clue to a proton conduction mechanism? Science 216 1982 407 708
19. J. Wang, and M.A. El-Sayed The effect of protein conformation change from α(II) to α(I) on the bacteriorhodopsin photocycle Biophys. J. 78 2000 2031 2036 (Pubitemid 30183597)
20. S.M. Barnett, C.M. Edwards, I.S. Butler, and I.W. Levin Pressure-induced transmembrane αII- to αI-helical conversion in bacteriorhodopsin: an infrared spectroscopic study J. Phys. Chem. B 101 1997 9421 9424
21. D. Oesterhelt, and W. Stoeckenius Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane Methods Enzymol. 31 1974 667 678
22. M. Bée Quasielastic Neutron Scattering: Principles and Applications in Solid State Chemistry, Biology, and Materials Science 1988 Adam Hilger Bristol, England and Philadelphia
23. F. Gabel, D. Bicout, U. Lehnert, M. Tehei, M. Weik, and G. Zaccai Protein dynamics studied by neutron scattering Q. Rev. Biophys. 35 2002 327 367 (Pubitemid 36207228)
24. J.C. Smith Protein dynamics: comparison of simulations with inelastic neutron scattering experiments Q. Rev. Biophys. 24 1991 227 291 (Pubitemid 121000389)
25. H.H. Paalman, and C.J. Pings Numerical evaluation of X-ray absorption factors for cylindrical samples and annular sample cells J. Appl. Phys. 33 1962 2635 2639
26. D. Richard, M. Ferrand, and G.J. Kearley Analysis and visualisation of neutron-scattering data J. Neutron Res. 4 1996 33 39
27. N.V. Prabhu, and K.A. Sharp Heat capacity in proteins Annual Review of Physical Chemistry 2005 521 548 (Pubitemid 41156887)
28. S.G. Taneva, J.M.M. Caaveiro, A. Muga, and F.M. Goni A pathway for the thermal destabilization of bacteriorhodopsin FEBS Lett. 367 1995 297 300
29. Z.A. Tokaji, E.A.B. Fodor, A.A. Szabó-Nagy, and T.A. Páli Hydroxylamine as a thermal destabiliser of bacteriorhodopsin Eur. Biophys. J. 39 2010 1605 1611
30. C. Zscherp, and A. Barth Reaction-induced infrared difference spectroscopy for the study of protein reaction mechanisms Biochemistry 40 2001 1875 1883 (Pubitemid 32165654)
31. P. Zavodszky, J.T. Johansen, and A. Hvidt Hydrogen-exchange study of conformational stability of human carbonic-anhydrase-B and its metallocomplexes Eur. J. Biochem. 56 1975 67 72
32. E. Goormaghtigh, V. Cabiaux, and J.M. Ruysschaert Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. II. Experimental aspects, side chain structure, and H/D exchange Subcell. Biochem. 23 1994 363 403
33. E.R. Henry, and J. Hofrichter Singular value decomposition: application to analysis of experimental data Methods Enzymol. 210 1992 129 192
34. H.A. Laczkó-Dobos, and B.b Szalontai Lipids, proteins, and their interplay in the dynamics of temperature-stressed membranes of a cyanobacterium, Synechocystis PCC 6803 Biochemistry 48 2009 10120 10128
35. K. Wood, U. Lehnert, B. Kessler, G. Zaccai, and D. Oesterhelt Hydration dependence of active core fluctuations in bacteriorhodopsin Biophys. J. 95 2008 194 202
36. G. Zaccai Moist and soft, dry and stiff: a review of neutron experiments on hydration-dynamics-activity relations in the purple membrane of Halobacterium salinarum Biophys. Chem. 86 2000 249 257 (Pubitemid 30665613)
37. U. Lehnert, V. Réat, M. Weik, G. Zaccaï, and C. Pfister Thermal motions in bacteriorhodopsin at different hydration levels studied by neutron scattering: correlation with kinetics and light-induced conformational changes Biophys. J. 75 1998 1945 1952 (Pubitemid 28455189)
38. M. Ferrand, A.J. Dianoux, W. Petry, and G. Zaccai Thermal motions and function of bacteriorhodopsin in purple membranes - effects of temperature and hydration studied by neutron scattering Proc. Natl. Acad. Sci. U. S. A. 90 1993 9668 9672 (Pubitemid 23315847)
39. J. Fitter, R.E. Lechner, G. Buldt, and N.A. Dencher Internal molecular motions of bacteriorhodopsin: hydration-induced flexibility studied by quasielastic incoherent neutron scattering using oriented purple membranes Proc. Natl. Acad. Sci. U. S. A. 93 1996 7600 7605 (Pubitemid 26277082)
40. H.B. Callen, and T.A. Welton Irreversibility and generalized noise Phys. Rev. 83 1951 34 40
41. D.J. Bicout, and G. Zaccai Protein flexibility from the dynamical transition: a force constant analysis Biophys. J. 80 2001 1115 1123 (Pubitemid 32182140)
42. G.A.B. Zaccai How soft is a protein? A protein dynamics force constant measured by neutron scattering Science 288 2000 1604 1607
43. I. Jelesarov, and H.R. Bosshard Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition J. Mol. Recognit. 12 1999 3 18 (Pubitemid 29160432)
44. J.L. Arrondo, A. Muga, J. Castresana, and F.M. Goni Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy Prog. Biophys. Mol. Biol. 59 1993 23 56
45. I.H. van Stokkum, H. Linsdell, J.M. Hadden, P.I. Haris, D. Chapman, and M. Bloemendal Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis Biochemistry 34 1995 10508 10518