Abstract
The combination of high-resolution NMR spectroscopy with pressure perturbation, known as variable-pressure NMR spectroscopy or simply high pressure NMR spectroscopy, is a relatively recent accomplishment, but is a technique expanding rapidly with high promise in future. The importance of the method is that it allows, for the first time in history, a systematic means of detecting and analyzing the structures and thermodynamic stability of high-energy sub-states in proteins. High-energy sub-states have been only vaguely known so far, as normally their populations are too low to be detected by conventional spectroscopic techniques including NMR spectroscopy. By now, however, high pressure NMR spectroscopy has established unequivocally that high-energy conformers are universally present in proteins in equilibrium with their stable folded counterparts. This chapter describes briefly the techniques of high pressure NMR spectroscopy and its unique and novel aspects as a method to explore protein structure in its high-energy paradigm with illustrative examples. It is now well established that high pressure NMR spectroscopy is a method to study intrinsic fluctuations of proteins, rather than those forced by pressure, by detecting structural changes amplified by pressure. Extension of the method to other bio-macromolecular systems is considered fairly straightforward.
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References
Abdul Latif AR, Kono R, Tachibana H, Akasaka K (2007) Kinetic analysis of amyloid protofibril dissociation and volumetric properties of the transition state. Biophys J 92:323–329
Akasaka K (2003) Highly fluctuating protein structures revealed by variable-pressure nuclear magnetic resonance. Biochemistry 42:10875–10885
Akasaka K (2006) Probing conformational fluctuation of proteins by pressure perturbation. Chem Rev 106:1814–1835
Akasaka K (2010) High pressure NMR study of proteins – seeking roots for function, evolution, disease and food applications. High Pressure Res 30:453–457
Akasaka K (2014) Pressure and protein dynamism. High Pressure Res 34:222–235
Akasaka K, Li H (2001) Low-lying excited states of proteins revealed from nonlinear pressure shifts in 1H and 15N NMR. Biochemistry 40:8665–8671
Akasaka K, Yamada H (2001) On-line cell high-pressure nuclear magnetic resonance technique: application to protein studies. Methods Enzymol 338:134–158
Akasaka K, Tezuka T, Yamada H (1997) Pressure-induced changes in the folded structure of lysozyme. J Mol Biol 271:671–678
Akasaka K, Li H, Yamada H, Li R, Thoresen T, Woodward CK (1999) Pressure response of protein backbone structure. Pressure-induced amide 15N chemical shifts in BPTI. Protein Sci 8:1946–1953
Akasaka K, Maeno A, Murayama T, Tachibana H, Fujita Y, Yamanaka H, Nishida N, Atarashi R (2014) Pressure-assisted dissociation and degradation of “proteinase K-resistant” fibrils prepared by seeding with scrapie-infected hamster prion protein. Prion 8:314–318
Benedek GB, Purcell EM (1954) Nuclear magnetic resonance in liquids under high pressure. J Chem Phys 22:2003–2012
Cooper A (1976) Thermodynamic fluctuations in protein molecules. Proc Natl Acad Sci U S A 73:2740–2741
Fourme R, Girard E, Akasaka K (2012) High-pressure macromolecular crystallography and NMR: status, achievements and prospects. Curr Opin Struct Biol 22:636–642
Hirata F, Akasaka K (2015) Structural fluctuation of proteins induced by thermodynamic perturbation. J Chem Phys 142, 044110.
Inoue K, Yamada H, Akasaka K, Herrmann C, Kremer W, Maurer T, Döker R, Kalbitzer HR (2000) Pressure-induced local unfolding of the Ras binding domain of RalGDS. Nat Struct Biol 7:547–550
Jonas J (2002) High-resolution nuclear magnetic resonance studies of proteins. Biochim Biophys Acta 1595:145–159
Kalbitzer HR, Spoerner M, Ganser P, Hosza C, Kremer W (2009) Fundamental link between folding states and functional states of proteins. J Am Chem Soc 131:16714–16719
Kamatari YO, Yamada H, Akasaka K, Jones JA, Dobson CM, Smith LJ (2001) Response of native and denatured hen lysozyme to high pressure studied by 15N/1H NMR spectroscopy. Eur J Biochem 268:1782–1793
Kamatari YO, Kitahara R, Yamada H, Yokoyama S, Akasaka K (2004) High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins. Methods 34:133–143
Kamatari YO, Yokoyama S, Tachibana H, Akasaka K (2005) Pressure-jump NMR study of dissociation and association of amyloid protofibrils. J Mol Biol 349:916–921
Kamatari YO, Smith LJ, Dobson CM, Akasaka K (2011) Cavity hydration as a gateway to unfolding: an NMR study of hen lysozyme at high pressure and low temperature. Biophys Chem 156:24–30
Kitahara R, Yamada H, Akasaka K, Wright PE (2002) High pressure NMR reveals that apomyoglobin is an equilibrium mixture from the native to the unfolded. J Mol Biol 320:311–319
Kitahara R, Yokoyama S, Akasaka K (2005) NMR snapshots of a fluctuating protein structure: ubiquitin at 30 bar–3 kbar. J Mol Biol 347:277–285
Kitahara R, Hata K, Li H, Williamson M, Akasaka K (2013) Pressure-induced chemical shifts as probes for conformational fluctuations in proteins. Prog Nucl Mag Res Sp 71:35–58
Kitamura Y, Itoh T (1987) Reaction volume of protonic ionization for buffering agents. Prediction of pressure dependence of pH and pOH. J Solution Chem 16:715–725
Kremer W, Arnold MR, Kachel N, Kalbitzer HR (2004) The use of high-sensitivity sapphire cells in high pressure NMR spectroscopy and its application to proteins. Spectroscopy 18:271–278
Lassalle MW, Li H, Yamada H, Akasaka K, Redfield C (2003) Pressure-induced unfolding of the molten globule of all-Ala alpha-lactalbumin. Protein Sci 12:66–72
Li H, Yamada H, Akasaka K (1998) Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatic trypsin inhibitor. Biochemistry 37:1167–1173
Maeno A, Matsuo H, Akasaka K (2009) The pressure-temperature phase diagram of hen lysozyme at low pH. Biophysics 5:1–9
Niraula TN, Konno T, Li H, Yamada H, Akasaka K, Tachibana H (2004) Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils. Proc Natl Acad Sci U S A 101:4089–4093
Peterson RW, Lefebvre BG, Wand J (2005) High resolution NMR studies of encapsulated proteins in liquid ethane. J Am Chem Soc 127:10176–10177
Refaee M, Tezuka T, Akasaka K, Williamson MP (2003) Pressure-dependent changes in the solution structure of hen egg-white lysozyme. J Mol Biol 327:857–865
Sasaki K, Gaikwad J, Hashiguchi S, Kubota T, Sugimura K, Kremer W, Kalbitzer HR, Akasaka K (2008) Reversible monomer-oligomer transition in human prion protein. Prion 2:118–122
Williamson MP, Akasaka K, Refaee M (2003) The solution structure of bovine pancreatic trypsin inhibitor at high pressure. Protein Sci 12:1971–1979
Yamada H (1974) Pressure-resisting glass cell for high pressure, high resolution NMR measurement. Rev Sci Instrum 45:640–642
Yamada H, Nishikawa K, Honda N, Shimura T, Aksaka K, Tabayashi K (2001) Pressure-resisting cell for high-pressure, high-resolution nuclear magnetic resonance measurement at very high magnetic fields. Rev Sci Instrum 72:1463–1471
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Akasaka, K. (2015). High Pressure NMR Spectroscopy. In: Akasaka, K., Matsuki, H. (eds) High Pressure Bioscience. Subcellular Biochemistry, vol 72. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-9918-8_33
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DOI: https://doi.org/10.1007/978-94-017-9918-8_33
Publisher Name: Springer, Dordrecht
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