Abstract
This year, 2014, marks the 100th anniversary of the first publication reporting the denaturation of proteins by high hydrostatic pressure (Bridgman 1914). Since that time a large and recently increasing number of studies of pressure effects on protein stability have been published, yet the mechanism for the action of pressure on proteins remains subject to considerable debate. This review will present an overview from this author’s perspective of where this debate stands today.
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References
Barrick D, Ferreiro DU, Komives EA (2008) Folding landscapes of ankyrin repeat proteins: experiments meet theory. Curr Opin Struct Biol 18:27–34
Bradley CM, Barrick D (2006) The notch ankyrin domain folds via a discrete, centralized pathway. Structure 14:1303–1312
Brandts JF, Oliveira RJ, Westort C (1970) Thermodynamics of protein denaturation. Effect of pressure on the denaturation of ribonuclease A. Biochemistry 9:1038–1047
Bridgman PW (1914) The coagulation of albumin by pressure. J Biol Chem 19:511–512
Frank HS, Evans MW (1945) Free volume and entropy in condensed systems. III. Entropy in binary liquid mixtures; partial molal entropy in dilute solutions; structure and thermodynamics in aqueous electrolytes. J Chem Phys 13:507–532
Frye KJ, Royer CA (1998) Probing the contribution of internal cavities to the volume change of protein unfolding under pressure. Protein Sci 7:2217–2222
Gal M, Kern T, Schanda P, Frydman L, Brutscher B (2009) An improved ultrafast 2D NMR experiment: towards atom-resolved real-time studies of protein kinetics at multi-Hz rates. J Biomol NMR 43:1–10
Galamba N (2013) Water’s structure around hydrophobic solutes and the iceberg model. J Phys Chem B 117:2153–2159
Galamba N (2014) Water tetrahedrons, hydrogen-bond dynamics, and the orientational mobility of water around hydrophobic solutes. J Phys Chem B 118:4169–4176
Gallagher KR, Sharp KA (2003) A new angle on heat capacity changes in hydrophobic solvation. J Am Chem Soc 125:9853–9860
Hawley SA (1971) Reversible pressure–temperature denaturation of chymotrypsinogen. Biochemistry 10:2436–2442
Herberhold H, Winter R (2002) Temperature- and pressure-induced unfolding and refolding of ubiquitin: a static and kinetic Fourier transform infrared spectroscopy study. Biochemistry 41:2396–2401
Huang DM, Chandler D (2000) Temperature and length scale dependence of hydrophobic effects and their possible implications for protein folding. Proc Natl Acad Sci U S A 97:8324–8327
Jacob MH, Saudan C, Holtermann G, Martin A, Perl D, Merbach AE, Schmid FX (2002) Water contributes actively to the rapid crossing of a protein unfolding barrier. J Mol Biol 318:837–845
Kitahara R, Royer C, Yamada H, Boyer M, Saldana JL, Akasaka K, Roumestand C (2002) Equilibrium and pressure-jump relaxation studies of the conformational transitions of P13MTCP1. J Mol Biol 320:609–628
Lepori L, Gianni P (2000) Partial molar volumes of ionic and nonionic organic solutes in water: a simple additivity scheme based on the intrinsic volume approach. J Solut Chem 29:405–447
Lin LN, Brandts JF, Brandts JM, Plotnikov V (2002) Determination of the volumetric properties of proteins and other solutes using pressure perturbation calorimetry. Anal Biochem 302:144–160
Meersman F, Smeller L, Heremans K (2006) Protein stability and dynamics in the pressure-temperature plane. Biochim Biophys Acta 1764:346–354
Mei G, Di VA, Campeggi FM, Gilardi G, Rosato N, De MF, Finazzi-Agro A (1999) The effect of pressure and guanidine hydrochloride on azurins mutated in the hydrophobic core. Eur J Biochem 265:619–626
Mohana-Borges R, Silva JL, Ruiz-Sanz J, de Prat-Gay G (1999) Folding of a pressure-denatured model protein. Proc Natl Acad Sci U S A 96:7888–7893
Roche J, Caro JA, Norberto DR, Barthe P, Roumestand C, Schlessman JL, Garcia AE, Garcia-Moreno BE, Royer CA (2012) Cavities determine the pressure unfolding of proteins. Proc Natl Acad Sci U S A 109:6945–6950
Roche J, Dellarole M, Caro JA, Norberto DR, Garcia AE, Garcia-Moreno EB, Roumestand C, Royer CA (2013) Effect of internal cavities on folding rates and routes revealed by real-time pressure-jump NMR spectroscopy. J Am Chem Soc 135:14610–14618
Rouget JB, Schroer MA, Jeworrek C, Puhse M, Saldana JL, Bessin Y, Tolan M, Barrick D, Winter R, Royer CA (2010) Unique features of the folding landscape of a repeat protein revealed by pressure perturbation. Biophys J 98:2712–2721
Rouget JB, Aksel T, Roche J, Saldana JL, Garcia AE, Barrick D, Royer CA (2011) Size and sequence and the volume change of protein folding. J Am Chem Soc 133:6020–6027
Sasahara K, Nitta K (1999) Pressure-induced unfolding of lysozyme in aqueous guanidinium chloride solution. Protein Sci 8:1469–1474
Schanda P, Kupce E, Brutscher B (2005) SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds. J Biomol NMR 33:199–211
Schanda P, Forge V, Brutscher B (2006) HET-SOFAST NMR for fast detection of structural compactness and heterogeneity along polypeptide chains. Magn Reson Chem 44:S177–S184
Seemann H, Winter R, Royer CA (2001) Volume, expansivity and isothermal compressibility changes associated with temperature and pressure unfolding of Staphylococcal nuclease. J Mol Biol 307:1091–1102
Street TO, Barrick D (2009) Predicting repeat protein folding kinetics from an experimentally determined folding energy landscape. Protein Sci 18:58–68
Street TO, Bradley CM, Barrick D (2007) Predicting coupling limits from an experimentally determined energy landscape. Proc Natl Acad Sci U S A 104:4907–4912
Till MS, Ullmann GM (2010) McVol – a program for calculating protein volumes and identifying cavities by a Monte Carlo algorithm. J Mol Model 16:419–429
Tripp KW, Barrick D (2008) Rerouting the folding pathway of the Notch ankyrin domain by reshaping the energy landscape. J Am Chem Soc 130:5681–5688
Zipp A, Kauzmann W (1973) Pressure denaturation of metmyoglobin. Biochemistry 12:4217–4228
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Royer, C.A. (2015). Why and How Does Pressure Unfold Proteins?. 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_4
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DOI: https://doi.org/10.1007/978-94-017-9918-8_4
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