Abstract
Defining the physical-chemical determinants of protein folding and stability, under normal and pathological conditions has constituted a major subfield in biophysical chemistry for over 50 years. Although a great deal of progress has been made in recent years towards this goal, a number of important questions remain. These include characterizing the structural, thermodynamic and dynamic properties of the barriers between conformational states on the protein energy landscape, understanding the sequence dependence of folding cooperativity, defining more clearly the role of solvation in controlling protein stability and dynamics and probing the high energy thermodynamic states in the native state basin and their role in misfolding and aggregation. Fundamental to the elucidation of these questions is a complete thermodynamic parameterization of protein folding determinants. In this chapter, we describe the use of high-pressure coupled to Nuclear Magnetic Resonance (NMR) spectroscopy to reveal unprecedented details on the folding energy landscape of proteins.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Akasaka K, Kitahara R, Kamatari YO (2013) Exploring the folding energy landscape with pressure. Arch Biochem Biophys 531:110–115
Balbach J, Forge V, Lau WS, van Nuland NA, Brew K, Dobson CM (1996) Protein folding monitored at individual residues during a two-dimensional NMR experiment. Science 274:1161–1163
Bodenhausen G, Ruben DJ (1980) Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem Phys Lett 69:185–189
Chalikian TV, Macgregor RB Jr (2009) Origins of pressure-induced protein transitions. J Mol Biol 394:834–842
Dellarole M, Royer C (2013) High-pressure fluorescence applications. In: Engelborghs Y, Visser T (eds) Methods in molecular biology, Springer, pp 53–74
Dill KA, MacCallum JL (2012) The protein-folding problem, 50 years on. Science 338:1042–1046
Dobson CM (2005) An overview of protein misfolding diseases. In: Buchner J, Kiefhaber T (eds) Protein folding handbook. Wiley-VCH Verlag GMBH & Co. KgaA, Weinheim, pp 1093–1113
Fourme R, Hamel G, Loupiac C, Perrier-Cornet J-M, Pin S, Roche J (2012) La biologie sous pression: de la molecule au procédé. Hautes Pressions: les Nouveaux Enjeux. Ed.: Publications Mission Ressources et Compétences Technologiques 2012.
Frydman L, Scherf T, Lupulescu A (2002) The acquisition of multidimensional NMR spectra within a single scan. Proc Natl Acad Sci U S A 99:15858–15862
Fuentes EJ, Wand AJ (1998) Local stability and dynamics of apocytochrome b562 examined by the dependence of hydrogen exchange on hydrostatic pressure. Biochemistry 37:9877–9883
Gal M, Schanda P, Brutscher B, Frydman L (2007) UtraSOFAST HMQC NMR and repetitive acquisition of 2D protein spectra at Hz rates. J Am Chem Soc 129:1372–1377
Grigera JR, McCarthy AN (2010) The behavior of the hydrophobic effect under pressure and protein denaturation. Biophys J 98:1626–1631
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
Kauzmann W (1959) Some factors in the interpretation of protein denaturation. Adv Protein Chem 14:1–63
Mitra L, Smolin N, Ravindra R, Royer CA, Winter R (2006) Pressure perturbation calorimetric studies of the solvation properties and the thermal unfolding of proteins in solution: experiments and theoretical interpretation. Phys Chem Chem Phys 8:1249–1265
Murphy KP, Privalov PL, Gill SJ (1990) Common features of protein unfolding and dissolution of hydrophobic compounds. Science 247:559–561
Privalov PL, Gill SJ (1988) Stability of protein structure and hydrophobic interaction. Adv Protein Chem 39:191–234
Roche J, Caro JA, Norberto DR, Barthe P, Roumestand C, Schlessman JL, Garcia AE, Garcia-Moreno B, Royer CA (2012a) Cavities determine the pressure unfolding of proteins. Proc Natl Acad Sci U S A 109:6945–6950
Roche J, Dellarole M, Caro JA, Guca E, Norberto DR, Yang YS, Garcia AE, Roumestand C, GarcÃa-Moreno B, Royer CA (2012b) Remodeling of the folding free-energy landscape of staphylococcal nuclease by cavity-creating mutations. Biochemistry 51:9535–9546
Roche J, Caro JA, Dellarole M, Guca E, Royer CA, GarcÃa-Moreno B, Garcia AE, Roumestand C (2013a) Structural, energetic and dynamic responses of the native state ensemble of staphylococcal nuclease to cavity-creating mutations. Proteins 81:1069–1080
Roche J, Dellarole M, Caro JA, Norberto DR, Garcia AE, GarcÃa-Moreno B, Roumestand C, Royer CA (2013b) J Am Chem Soc 135:14610–14618
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
Royer CA (2002) Revisiting volume changes in pressure-induced protein unfolding. Biochim Biophys Acta 1595:201–209
Schanda P, Brutscher B (2005) Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. J Am Chem Soc 127:8014–8015
Wolynes PG, Eaton WA, Fersht AR (2012) Chemical physics of protein folding. Proc Natl Acad Sci U S A 109:17770–17771
Acknowledgements
Authors are indebted to our long and ongoing collaborations with J.A. Caro, B. Garcia-Moreno (John Hopkins University, Baltimore, USA) and Angel E. Garcia (Rensselaer Polytechnic Institute, Troy, U.S.A.), in the work that led to the publications reviewed here. High-pressure NMR equipment (except the spectrometers) used in the work of the original manuscripts cited here was funded by the French National Agency for Research (ANR, PiriBio 09–455024; Project Coordinator: C.A. Royer). This work was also supported by the French Infrastructure for Integrated Structural Biology (FRISBI) ANR-10-INSB-05-01.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2015 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Roche, J., Dellarole, M., Royer, C.A., Roumestand, C. (2015). Exploring the Protein Folding Pathway with High-Pressure NMR: Steady-State and Kinetics Studies. 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_13
Download citation
DOI: https://doi.org/10.1007/978-94-017-9918-8_13
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-017-9917-1
Online ISBN: 978-94-017-9918-8
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)