Use of high pressure for the study of
conformational states and dynamics in biological systems


Publications


High pressure publications of the Regensburg Group

Kalbitzer, H. R. , Görler, A., Li, H., Dubovskii, P., Hengstenberg, W., Kowolik, C., Yamada, H., & Akasaka, K. (2000) 15 N and 1 H NMR Study of Histidine Containing Protein (HPr) from Staphylococcus carnosus at High Pressure. Prot. Sci. 9 , 693-703.

Huber, F., Gronwald, W., Wohlgemuth, S., Herrmann, C., Geyer, M., Wittinghofer, A. & Kalbitzer, H. R. (2000) Sequential NMR assignments of the RAS-binding domain of Byr2. J. Biomol. NMR 16 , 355-356.

Inouhe, K., Yamada, H., Akasaka, K., Herrmann, C., Kremer, W., Maurer, T., Döker, R. & Kalbitzer, H. R. (2000) Pressure-induced local unfolding of the Ras binding domain of RalGDS. Nature Struct. Biol. 7 , 547-550.

Inoue, K., Maurer,T., Yamada, H., Herrmann, C., Horn, G., Kalbitzer, H. R . & and Akasaka, K. (2001) High-pressure NMR study of the complex of a GTPase Rap1A with its effector RalGDS. A conformational switch in RalGDS revealed from non-linear pressure shifts. FEBS Lett. 506 , 180-184.

Brunner, E., Arnold, M. R., Kremer, W. & Kalbitzer, H. R. (2001) Pressure stability of phospholipid bicelles: measurements of residual dipolar couplings under extreme conditions. J. Biomol. NMR 21 , 173-176..

Akasaka, K., Li, H., Dubovskii, P., Kalbitzer, H. R. & Yamada, H. (2001)

High Resolution High-Pressure NMR Spectroscopy - Application to Protein Structure, Dynamics and Folding. In 'Dynamics, Structure and Function of Biological Macromocules´ (O. Jardetzky and M. D. Finucane, eds) IOS press, Amsterdam , Nato Science Series A 315 , 77-92.

Arnold, M.R., Kremer, W., Luedemann, H.-D. & Kalbitzer, H. R. (2002) 1 H NMR parameters of common amino acid residues measured in aqueous solutions of the linear tetrapeptides Gly-Gly-X-Ala at pressures between 0.1 and 200 MPa. Biophys. Chem. 96 , 129-140.

Kremer, W., Arnold, M. R., Brunner, E., Schuler, B., Jaenicke, R. & Kalbitzer, H. R. (2003) High pressure NMR spectroscopy and its application to the cold shock protein Tm Csp from the hyperthermophilic bacterium Thermotoga maritima . In “Advances in high pressure bioscience and biotechnology II”. (R. Winter, ed.), pp 101-112. Springer, Berlin .

Arnold, M. R. Kalbitzer, H. R. & and Werner Kremer, W. (2003) High-sensitivity sapphire cells for high pressure NMR spectroscopy on proteins. J. Magn. Reson . 61 , 127-131.

Kremer, W. & Kalbitzer, H. R. (2003) Hochdruck-NMR-Spektroskopie an Proteinen. Biospektrum 2 , 142-145.

Kremer, W., Arnold, M. R., Kachel, N. & Kalbitzer, H. R. (2004) The use of high- sensitivity sapphire cells in high pressure NMR spectroscopy and its application to proteins. Spectroscopy 18 , 271-278.

Hattori, M., Li, H., Yamada, H., Akasaka, K., Hengstenberg, W., Gronwald, W. & Kalbitzer, H. R. (2004) Infrequent cavity-forming fluctuations in HPr from Staphylococcus carnosus revealed by pressure and temperature-dependent tyrosine ring-flips. Prot. Sci. 13 , 3104-3114.

Kachel, N., Kremer, W., Zahn, R. & Kalbitzer, H. R. (2006) Observation of intermediate states of the human prion protein by high pressure NMR spectroscopy. BMC Struct. Biol. 16 , 6.

Kremer, W. (2006) High-Pressure NMR Studies in Proteins. Ann. Rep. NMR Spectroscopy , 57, 177-200

Kremer, W., Kachel, N., Kuwata, K., Akasaka, K., & Kalbitzer, H. R. (2007) Species specific differences in the intermediate states of human and hamster prion protein detected by high pressure NMR spectroscopy. J. Biol. Chem. 282, 22689–22698.

Sasaki, K., Gaikwad, J., Hashiguchi, S. Kubota, T., Sugimura, K., Kremer, W., Kalbitzer, H. R. and Akasaka, K. (2008) Reversible monomer-oligomer transition in human prion protein. Prion 2, 118-122.

Kalbitzer, H. R., Spoerner, M., Ganser, P., Hosza, C. and Kremer, W. (2009) Fundamental link between folding states and functional states of proteins. J. Am. Chem. Soc., 131, 16714-16719.

Beck Erlach, M., Munte, C. E., Kremer, W., Hartl, R., Rochelt, D., Niesner, D., Kalbitzer, H. R. (2010) Ceramic cells for high pressure NMR spectroscopy on proteins. J. Magn. Reson. 204 , 196-199.

Kremer, W., Arnold, M., Munte, C. E., Hartl, R., Beck Erlach, M., Koehler, J., Meier, A., Kalbitzer, H. R. (2011) Pulsed Pressure Perturbations, an Extra Dimension in NMR Spectroscopy of Proteins. J. Am. Chem. Soc. 133 , 13646-13651.

Koehler, J., Beck Erlach, M., Crusca Jr, E., Kremer, W., E. Munte, C., Kalbitzer, H.R. (2012) On the pressure dependence of 15 N chemical shifts in the model peptides Ac-Gly-Gly-X-Ala-NH 2 . Materials 5 , 1774-1786.

Munte, C. E., Beck Erlach, M., Kremer, W., Koehler, J., Kalbitzer, H. R. (2013) Distinct Conformational States of the Alzheimer ?-Amyloid Peptide can be Detected by High Pressure NMR Spectroscopy. Angew. Chem. Int. Ed. 52 , 8943 –8947.

Munte, C, E., Beck Erlach, M., Kremer, W., Koehler, J., Kalbitzer, H. R. (2013) Getrennte Konformationszustände des Alzheimer-?-Amyloidpeptids – Nachweis mit Hochdruck-NMR-Spektroskopie. Angew. Chem. 125 , 9111 –9116.

Kalbitzer, H. R., Kremer, W., Spoerner, M., Ramm Sander, P. (2013) NMR-Spektroskopie – Strukturanalytik von Biomolekülen in atomarer Auflösung. Blick in die Wissenschaft 27 , 13-17.

Kalbitzer, H. R. , Rosnizeck, I. C., Munte, C. E., Puthenpurackal Narayanan, S., Kropf, V., Spoerner, M. (2013) Intrinsic Allosteric Inhibition of Signaling Proteins by Targeting Rare Interaction States Detected by High-Pressure NMR Spectroscopy . Angew. Chem. Int. Ed . 52 , 14242 –14246.

Kalbitzer, H. R. , Rosnizeck, I. C., Munte, C. E., Puthenpurackal Narayanan, S., Kropf, V., Spoerner, M. (2013) Intrinsische allosterische Hemmung von Signalproteinen durch Stabilisierung gering besetzter, durch Hochdruck-NMR-Spektroskopie nachweisbarer Interaktionszustände. Angew. Chem. 125, 14492 –14496.

Kalbitzer, H. R. , Spoerner, M. (2013) State 1(T) Inhibitors of Activated Ras. In The Enzymes , Vol. 33, pp. 69-94, F. Tamanoi (ed.), Academic Press, Burlington.

Beck Erlach, M., Koehler, J., Moeser , B., Horinek, D., Kremer, W., Kalbitzer, H. R. (2014) Relationship between non-linear pressure induced chemical shift changes and thermodynamic parameters. J. Chem. Phys . B 18 , 5681-5690.

Koehler, J., Beck Erlach, M. Crusca, E. Jr, Kremer, W., Munte, C. E., Meier, A., Kalbitzer, H. R. (2014) Pressure response of amide one-bond J -couplings in model peptides and proteins. J. Biomol. NMR 60 , 45-50.

Kalbitzer, H. R. (2015) High Pressure NMR Methods for Characterizing Functional Substates of Proteins. In “ High Pressure Bioscience - Basic Concepts, Applications and Frontiers ” ( K. Akasaka and H. Matsuki, eds, pp. 179-198), Springer, Heidelberg, Germany.

Beck Erlach, M., Koehler, J., Crusca, E. Jr., Kremer, W., Munte, C. E., Kalbitzer, H. R. (2016) Pressure Dependence of Backbone Chemical Shifts in the Model Peptides Ac-Gly-Gly-Xxx-Ala-NH 2 . J. Biomol. NMR 65 , 65-77.

Beck Erlach, M., Kalbitzer H. R. , Winter, R., Kremer, W. (2016) Conformational Substates of Amyloidogenic hIAPP Revealed by High Pressure NMR Spectroscopy. ChemistrySelect 1, 3239–3243.

Frach, R., Kibies, P., Böttcher, S., Pongratz, T., Strohfeldt, S., Kurrmann, S., Koehler, J., Hofmann, M., Kremer, W., Kalbitzer, H. R. , Reiser, O., Horinek, D., Kast, S. M. (2016) The Chemical Shift Baseline for High-Pressure NMR Spectroscopy of Proteins. Angew. Chemie Int. Ed. 55 , 8757 –8760.

Puthenpurackal Narayanan, S. , Gopalakrishnan Nair, D., Schaal, D., Aguiar, M. B., Wenzel, S., Kremer., W., Schwarzinger, S., Kalbitzer, H. R. (2016) Structural transitions in full-length human prion protein detected by xenon as probe and spin labelling of the N-terminal domain. Scientific Reports , 6 (28419), 1-17.

Schummel, P., Haag, A., Kremer, W., Kalbitzer, H. R. , Winter, R. (2016) Cosolvent and Crowding Effects on the Temperature and Pressure Dependent Conformational Dynamics and Stability of Globular Actin. J. Phys. Chem . B 120, 6575 - 6586.

Frach, R., Kibies, P., Böttcher, S., Pongratz, T., Strohfeldt, S., Kurrmann, S., Koehler, J., Hofmann, M., Kremer, W., Kalbitzer, H. R. , Reiser, O., Horinek, D., Kast, S. M. (2016) Die Basislinie der chemischen Verschiebung in Hochdruck-NMRSpektren von Proteinen. Angew. Chemie 128 , 8900 –8904 .

Spoerner, M., Karl, M., Lopes, P., Hoering, M., Loeffel, K., Nuehs, A., Adelsberger, J., Kremer, W., Kalbitzer, H. R. (2017) High pressure 31 P NMR on guanine nucleotide. J. Biomol. NMR 66 , 141-157.

 

High pressure publications of the Sheffield Group

Pressure-dependent changes in the structure of the melittin -helix
determined by NMR’, M. Iwadate, T. Asakura, P. V. Dubovskii, H. Yamada, K.
Akasaka and M. P. Williamson, J. Biomol. NMR, 2001, 19, 115-124.

Pressure-dependent changes in the solution structure of lysozyme, M.
Refaee, T. Tezuka, K. Akasaka and M. P. Williamson, J. Mol. Biol. 2003, 327, 857-865.

The solution structure of BPTI at high pressure, M. P. Williamson, K.
Akasaka and M. Refaee, Protein Science 2003, 12, 1971-1979.

Pressure-induced changes in the solution structure of the GB1 domain of
protein G, D. J. Wilton, R. B. Tunnicliffe, Y. O. Kamatari, K. Akasaka and M. P.
Williamson, Proteins 2008, 71,1432-1440.

Structural change in a B-DNA helix with hydrostatic pressure, D. J. Wilton,
M. Ghosh, K. V. A. Chary, K. Akasaka and M. P. Williamson, Nucleic Acids
Research, 2008, 36, 4032-4037.

Pressure-dependent 13C chemical shifts in proteins: Origins and
applications, D. J. Wilton, R. Kitahara, K. Akasaka and M. P. Williamson, J. Biomol. NMR
2009, 44, 25-33.

Pressure-dependent structure changes in barnase reveal intermediate rate
fluctuations, D. J. Wilton, R. Kitahara, K. Akasaka, M. J. Pandya and M. P.
Williamson, Biophys. J., 2009, 97, 1482-1490.

For further information also see: http://www.nmr.group.shef.ac.uk/MPW.html.

 

High pressure publications of the INSERM CBS

Royer, C.A., G. Weber, T.J. Daly, and K.S. Matthews. (1986) Dissociation of the lactose Repressor Tetramer Using High Hydrostatic Pressure, Biochemistry 25:8308.

Scarlata, S.F., Ropp, T. and Royer, C.A. (1989). Histone Subunit Interactions as Investigated by High Pressure, Biochemistry 28:6637.

Royer, C.A., Matthews, K.S. and Chakerian, A. (1990). Macromolecular Binding Equilibria in the lac Repressor System as Studied by High Pressure Fluorescence Spectroscopy, Biochemistry 29: 959.

Pin, S., Royer, C. A., Alpert, B., Gratton, E. and Weber, G. (1990) Subunit Interactions in
Hemoglobin Probed by Fluorescence and High Pressure Techniques, Biochemistry 29:9194.

Royer, C. A. (1991). Macromolecular Assemblies Studied Using High Pressure Fluorescence
Spectroscopy, published in Time-Resolved Laser Spectroscopy in Biochemistry, J.R.
Lackowicz, editor, Vol. II, Proc. SPIE OE/LASE, 1202.

Pin, S. and Royer, C. A. (1994). Using High Pressure Fluorescence Methods to Observe Subunit
Dissociation in Hemoglobin, Methods in Enzymology,

Royer, C. A., Hinck, A., Loh, S., Prehoda, K., Xiangdong, P., Jonas, J. & Markley, J. (1993) Effect of Amino Acid Substitution on the Pressure Denaturation of Staphylococcal Nuclease as
Monitored by Fluorescence and NMR Spectroscopy, Biochemistry 32: 5222.

Vidugiris, G.A.J., Markley, J. L. & Royer, C. A. (1995). Evidence for a Molten-Globule-Like
Transition State in Protein Folding from Determination of Activation Volumes, Biochemistry
34:4909.

Royer, C. A. (1995). The Application of High Pressure to Biochemical Equilibria: What Can We
Learn from The Other Thermodynamic Variable? Methods in Enzymology, 259: 357, M.
Johnson and G. Ackers, editors.

Vidugiris, G. A. J., Truckses, D., Markley, J. L. & Royer, C. A. (1996). Proline Isomerization and the High Pressure Denaturation of Staphylococcal Nuclease, Biochemistry 35: 3857.

Vidugiris, G., Thomas, R. & Royer, C. A. (1996). Pressure-Jump Relaxation Kinetics of Unfolding
and Refolding Transitions of Staphylococcal Nuclease and Proline Isomerization Mutants, in
High Pressure Effects in Molecular Biophysics and Enzymology, J.L. Markley, D. B.
Northrup and C. A. Royer, eds., Oxford University Press, Oxford, England

Frye, K. J., Perman, C. & Royer, C. A. (1996). Correlation Between Area and Volume of Unfolding for Site Specific Mutants of Staphylococcal Nuclease, Biochemistry 31: 10234.

Frye, K. J. & Royer, C. A. (1997). The Kinetic Basis for the Stabilization of Staphylococcal
Nuclease by Xylose, Protein Science 6: 789.
Panick, G. Malessa, R., Winter, R., Rapp, G. Frye, K.J. & Royer, C.A. (1998). Structural
Characterization of the Pressure-Denatured State and the Kinetics of Folding/Unfolding of
Staphylococcal Nuclease by Synchrotron Small Angle X-ray Scattering and Fourier
Transform Infrared Spectroscopy, J. Mol. Biol. 275: 389.

Vidugiris, G.J.A. & Royer, C.A. (1998). Determination of the Volume Changes for the Pressure-Induced Transitions of Apomyoglobin between the Native, Molten Globule and Unfolded States, Biophys. J. 75: 463.

Frye, K.J. & Royer, C.A. (1998). Probing the Contribution of Internal Cavities to the Volume Change of Protein Folding Under Pressure, Protein Sci 7: 2217.

Desai, G., Panick, G., Zein, M., Winter, R. & Royer, C. A. (1999). High Pressure Studies of the Folding/Unfolding of trp repressor, J. Mol. Biol, 288: 461.

Royer, C. A. (1999) Pressure Denaturation of Proteins, High Pressure Molecular Science, NATO ASI R. Winter & J. Jonas, eds. Kluwer Academic Publishers, The Netherlands.

Panick, G., Vidugiris, GJA, Mallessa, R., Rapp, G., Winter R. & Royer C.A. (1999). Exploring the Temperature-Pressure Phase Diagram of staphylococcal Nuclease, Biochemistry 38: 4157.

Royer, C.A. (2000). Protein folding and stability, What can we learn from high pressure? in High Pressure Research, 19, Harwood Academic Publishers, London, 603.

Woenckhaus, J.,. Köhling, R., Thiyagarajan, P., Littrell, K.C., Seifert, S., Royer, C.A. & Winter, R. (2001). Pressure-Jump SAXS Detected Kinetics of Staphylococcal Nuclease Folding, Biophys. J. 80:

Seeman, H., Winter, R. & Royer, C.A. (2001) Volume, expansivity and isothermal compressibility changes associated with temperature and pressure unfolding of staphylococcal nuclease, J. Mol. Biol 307: 1091.

Roumestand, C., Boyer, M., Guignard, L., Barthes, P., & Royer, C.A. (2001). Characterization of the Folding and Unfolding Reactions of a Small -Barrel Protein of Novel Topology, the MTCP1 Oncogene Product P13, J. Mol. Biol. 312: 247.

Silva, J. L., Foguel, D. & Royer, C.A. (2001) New Insights into protein folding, dynamics and structure from high pressure studies, TiBS 26: 612.

Royer, C.A. (2002). Revisiting the volume change of protein unfolding by pressure, Biochem. Biophys. Acta 1595 (1-2): 201.

Royer, C.A. (2002). A discussion of the physical basis for the pressure unfolding of proteins, in Proceeding of the HPBB, R. Hayashi, ed. Elsevier Science, B.V., The Netherlands, pp.17.

Kitahara, R., Royer, C.A., Yamada, H., Boyer, M., Saldana, J.-L., Akasaka, K. & Roumestand, C. (2002). Equilibrium and Pressure-jump Relaxation Studies of the Conformational Transitions of P13MTCP1, J. Mol. Biol. 320: 609.

Van Uden, N.W.A., Hubel, H., Faux, D.A., Dunstan, D. J. & Royer, C.A. (2003) Negative effective pressures in liquid mixtures, High Pressure Res. 23: 205.

Herberhold H., Royer C. A, Winter R. (2004). Effects of Chaotropic and Kosmotropic Cosolvents on the Pressure-Induced Unfolding and Denaturation of Proteins: An FT-IR Study on Staphylococcal Nuclease. Biochemistry 43: 3336.

Ravindra, R., Royer, C. & Winter, R. (2004). Pressure perturbation calorimetric studies of the solvation properties and the thermal unfolding of staphylococcal nuclease, Phys. Chem. Chem. Phys. 6: 1952.

Royer, C.A. (2006). Probing Protein Folding and Conformational Transitions in Proteins with
Fluorescence, Chemical Reviews 106: 1769.

Brun, L., Isom, D. Velu, P., Garcia-Moreno, B. & Royer, C.A. (2006) Hydration of the folding transition state ensemble of a protein, Biochemistry, 45: 3473.

Mitra L, Smolin N, Ravindra R, Royer C, 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, 1249-65.

Zorrilla S, Doan T, Alfonso C, Margeat E, Ortega A, Rivas G, Aymerich S, Royer CA, Declerck N. (2007) Inducer-Modulated Cooperative Binding of the Tetrameric CggR Repressor to Operator DNA. Biophys J., 92: 3215.

Royer, C. A. (2007) The Nature of the Folding Transition State and the Mechanisms of Protein Folding: A Review, Archives of Biochemistry and Biophysics, 469: 34.

Mitra, L., Hata, K., Kono, R., Maeno, A., Isom, D., Rouget, J.B., Winter, R., Akasaka, K., Garcia-Moreno E., B. & Royer, C.A., (2007) Vi-Value Analysis: A Pressure-Based Method for Mapping the Folding Transition State Ensemble of Proteins, JACS, 129: 14108.

Mitra, L., Rouget, J.B., Royer, C.A. & Winter, R. (2008) Towards a quantitative understanding of protein hydration and volume properties, Chem Phys Chem, 9: 2715.

Krywka, C., Sternemann, C., Paulus, M., Tolan, M., Royer, C. & Winter, R. (2008) Effects of osmolytes on pressure-induced unfolding of proteins, Chem Phys Chem ,9: 2809.

Rouget, J.-B., Schroer, M. A., Jeworrek, C., Pühse, M., Saldana, J.-L., Bessin, Y., Tolan, M., Barrick, D., Winter, R. & Royer, C. A. (2010) Unique Features of the Folding Landscape of a Repeat Protein Revealed by Pressure Perturbation, Biophys. J. (in press).

 

Publications from Kazuyuki Akasaka’s group in high pressure protein study

Original papers (1997~2010)

Kazuhide Miyamoto•,aÿ Kayo Togiya,b Ryo Kitahara,c,d Kazuyuki Akasakad,e
and Yoshihiro Kurodaa , Solution structure of LC5, the CCR5-
derived peptide for HIV-1 inhibition. Journal of Peptide Science, in press (2010).

David J. Wilton, Ryo Kitahara, Kazuyuki Akasaka, Maya J. Pandya, and Mike P. Williamson, Pressure-Dependent Structure Changes in Barnase on Ligand Binding Reveal Intermediate Rate Fluctuations. Biophysical Journal 97, 1482-1490 (2009).

Kunihiko Gekko, Mariko Araga, Tadashi Kamiyama, Eiji Ohmae, Kazuyuki Akasaka:
Pressure dependence of the apparent specific volume of bovine serum albumin: insight into the difference between isothermal and adiabatic compressibilities. Biophys. Chem. 144, 67-71 (2009).

Ryohei Kono, Tetsuro Fujisawa, Kazuyuki Akasaka and Hideki Tachibana, Amyloid fibrillation rate differs greatly among single-disulfide variants of hen lysozyme. J. Biol. Macromol. 9, 23-30 (2009).

Akihiro Maeno, Hiroshi Matsuo, and Kazuyuki Akasaka, The pressure-temperature phase diagram of hen lysozyme at low pH. Biophysics 5, 1-9 (2009).

Mike P. Williamson, David J. Wilton, Mahua Ghosh, KVA Chary and Kazuyuki Akasaka, Structural change in a B-DNA helix with hydrostatic pressure, Nucleic Acids Res. 2008 July; 36(12): 4032–4037 (2008).

Ken Sasaki, Jyoti Gaikwad, Shuhei Hashiguchi, Toshiya Kubota, Kazuhisa Sugimura, Werner Kremer, Hans Robert Kalbitzer and Kazuyuki Akasaka,ÿReversible monomer-oligomer transition in human prion protein. PRION 2, 118-122 (2008).
Ryo Kitahara, Chenhua Zhao, Kohei Saito, Seizo Koshiba, Makoto Ioune, Takanori Kigawa, Shigeyuki Yokoyama, and Kazuyuki Akasaka, Basic Folded and Low-Populated Locally Disordered Conformers of SUMO-2 Characterized by NMR Spectroscopy at Varying Pressures. Biochemistry, 47 (1), 30 -39, 2008.
Web Release Date: December 15, 2007
Kazuyuki Akasaka, Harumi Nagahata, Akihiro Maeno and Ken Sasaki,,,Pressure acceleration of proteolysis: A general mechanism. Biophysics 4, 29-32 (2008).

David J. Wilton, Richard B. Tunnicklife, Yuji O. Kamatari, Kazuyuki Akasaka and Mike P. Williamson, Pressure-induced changes in the solution structure of the GBI domain of Protein G. PROTEINS: Structure, Function, and Bioinformatics, published on-line. Dec. 2007.

Lally Mitra, Kazumi Hata, Ryohei Kono, Akihiro Maeno, Daniel Isom, Jean-Baptiste Rouget, Roland Winter, Kazuyuki Akasaka, Bertrand García-Moreno and Catherine A. Royer, Vi-Value analysis. A pressure-based method for mapping the folding transition state ensemble of proteins. J. Am. Chem. Soc.129, 14108-14109 (2007)..

Kazuyuki Akasaka,, Abdul Raziq Abdul Latif,‡, Akihiro Nakamura, Koichi Matsuo, Hideki Tachibana,| and Kunihiko Gekko, Amyloid Protofibril is Highly Voluminous and Compressible. Biochemistry, 46, 10444-10450 (2007).

W. Kremer, N. Kachel, Kazuo Kuwata, Kazuyuki Akasaka, and Hans-Robert Kalbitzer, Species-specific differences in the intermediate states of human and Syrian Hamster prion protein detected by high pressure NMR spectroscopy. J. Biol. Chem. 282, 22689-22698 (2007).

Shin-ichi J. Takayama, Yo-ta Takahashi, Shin-ichi Mikami, Kiyofumi Irie, Shin Kawano, Yasuhiko Yamamoto, Hikaru Hemmi, Ryo Kitahara, Shigeyuki Yokoyama
and Kazuyuki Akasaka, Local Conformational Transition of Hydrogenobacter thermophilus Cytochrome c552 Relevant to Its Redox Potential. Biochemistry 46, 9215-9224 (2007).
Masayuki Oda, Kenji Kanaori, and Kazuyuki Akasaka, Icreased thermodynamic stability by hydrophilic amino acid substitutions on the surface of Streptomyces subtilisin inhibitorÿJ. Biol. Macromol., 7(1) 3-8 (2007)

Abdul Raziq Abdul Latif, Ryohei Kono, Hideki Tachibana and Kazuyuki Akasaka, Pressure dissociation kinetics of amyloid protofibrils. Biophys. J , 2007;92 323-329 (2007).

Ryo Kitahara, Yoshiki Yamaguchi, Eri Sakata, Takeshi Kasuya, Keiji Tanaka, Koichi Kato, Shigeyuki Yokoyama, Kazuyuki Akasaka , Evolutionally conserved intermediates between ubiquitin and NEDD8. J. Mol. Biol. 363, Issue No. 2, 395-404 (2006).

Kitahara, R., Okuno, A., Kato, M., Taniguchi, Y., Yokoyama, S., and Akasaka, K., Cold denaturation of ubiquitin at high pressure. Magnetic Resonance in Chemistry 44, S108-S113 (2006).
Y. O. Kamatari, S. Yokoyama, H. Tachibana and K. Akasaka, Pressure-jump NMR Study of Dissociation and Association of Amyloid Protofibrils. Journal of Molecular Biology 349, Issue 5, 24 June, Pages 916-921 (2005).

Ryo Kitahara, Shigeyuki Yokoyama and Kazuyuki Akasaka, NMR snapshots of a fluctuating protein structure. Ubiquitin at 30 bar – 3kbar. J. Mol. Biol. 347, 277-285 (2005).

K. Hata, R. Kono, M. Fujisawa, R. Kitahara, K. Akasaka, Xu Ying, High pressure NMR study of dihydrofolate reductase from a deep-sea bacterium Moritella Profunda. Cellular and Molecular BiologyTM 50, 311-316 (2004)

Mineyuki Hattori, Hua Li, Hiroaki Yamada, Kazuyuki Akasaka, Wolfgang Hengstenberg, Wolfram Gronwald, and Hans Robert Kalbitzer, Infrequent cavity-forming fluctuations in HPr from Staphylococcus carnosus revealed
by pressure and temperature-dependent tyrosine ring-flips. Protein Science, 13, 3104-3114 (2004).

A. Yokota, K. Hirai, H. Miyauchi, S. Iimura, Y. Noda, K. Inoue, K. Akasaka, H. Tachibana ane S. Segawa, NMR characterization of three-disulfide variants of lysozyme, C64A/C80A, C76A/C94A, and C30A/C115A- A marginally stable state in folded proteins. Biochemistry, 43, 6663-6669 (2004).

Kazuo Kuwata, Yuji O. Kamatari, Kazuyuki Akasaka, Thomas L. James, Slow conformational dynamics in the Hamster prion protein. Biochemistry, 43, 4439-4446 (2004).

Tara N. Niraula, Takashi Konno, Hua Li, Hiroaki Yamada, Kazuyuki Akasaka and Hideki Tachibana, Pressure-dissociable reversible assembly of naturally denatured lysozyme is a precursor for amyloid fibrils. Proc. Natl. Acad. Sci. USA, 101, 4089-4093 (2004).

M. P. Williamson, K. Akasaka and M. Refaee, The solution structure of bovine pancreatic trypsin inhibitor at high pressure. Protein Science, 12, 1971-1979 (2003).

M. Refaee, T. Tezuka, K. Akasaka and M. P. Williamson, Pressure-dependent changes in the solution structure of hen egg-white lysozyme. J. Mol. Biol. 327, 857-865 (2003).

R. Kitahara and K. Akasaka, Close identity of a pressure-stabilized intermediate with a kinetic intermediate in protein folding. Proc. Natl. Acad. Sci. USA 100, 3167-3172 (2003).

Michael W. Lassalle, Hua Li, Hiroaki Yamada, Kazuyuki Akasaka and Christina Redfield, Pressure-induced unfolding of the molten globule of all-Ala ÿ-lactalbumin. Protein Science 12, 66-72 (2003).

K. Kuwata, H. Li, H. Yamada, G. Legname, S. B. Prusiner, K. Akasaka and T. L. James, Locally disordered conformer of Hamster prion: A crucial intermediate to PrPSC ? Biochemistry 41, 12277-12283 (2002).
.
R. Kitahara, C. Royer, H. Yamada, M. Boyer, J. L. Saldana, K. Akasaka and C. Roumestand, Equilibrium and pressure-jump relaxation studies of the conformational transitions of P13MTCP1. J. Mol. Biol. 329, 609-628 (2002).

T. N. Niraula, K. Haraoka, Y. Ando, H. Li, H. Yamada and K. Akasaka, Decreased thermodynamic stability as a crucial factor for familial amyloidotic polyneuropathy, J. Mol. Biol. 320, 333-342 (2002).

R. Kitahara, H. Yamada, K. Akasaka and P. E. Wright, High pressure NMR reveals that apomyoglobin is an equilibrium mixture from the native to the unfolded. J. Mol. Biol. 320, 311-319 (2002).

R. Kitahara, H. Yamada and K. Akasaka, Two folded conformers of ubiquitin revealed by high pressure NMR. Biochemistry 40, 13556-13563 (2001),.

K. Kuwata, H. Li, H. Yamada, C. A. Batt, Y. Goto and K. Akasaka, High pressure NMR reveals a variety of fluctuating conformers in ÿ-lactoglobulin. J. Mol. Biol. 305, 1073-1083 (2001).

K. Akasaka and H. Li, Low-lying excited states of proteins from nonlinear pressure shifts in1H and 15N NMR. Biochemistry 40, 8665-8671 (2001).

M. Iwadate, T. Asakura, P. V. Dubovskii, H. Yamada, K. Akasaka and M. P. Williamson, Pressure-dependent changes in the structure of the melittin ÿ-helix determined by NMR, J. Biomol. NMR 19 (2):115-124 (2001).

Y. O. Kamatari, H. Yamada, K. Akasaka, J. A. Jones, C. M. Dobson and L. J. Smith, The response of native and denatured hen lysozyme to high pressure studied by 15N/1H NMR spectroscopy. Eur. J. Biochem. 268, 17821793 (2001).

M. Marchi and K. Akasaka, Simulation of hydrated BPTI at high pressure: Changes in hydrogen bonding and its relation with NMR experiments. J. Phys. Chem. B 105, 711-714 (2001).

Yamada, H, Nishikawa, K., Honda, M., Shimura, T., Akasaka, K., and Tabayashi, K. , Pressure-resisting cell for high-pressure, high-resolution nuclear magnetic resonance measurements at very high magnetic fields. Rev. Sci. Inst. 72, 1463-1471(2001).

M. W. Lassalle, H. Yamada, H. Morii, K. Ogata, A. Sarai and K. Akasaka, Filling a cavity dramatically increases pressure stability of the c-Myb R2 domain. Proteins: Structure, Function and Genetics 45, 96-101(2001).

K. Inoue, T. Maurer, H. Yamada, C. Herrmann, G. Horn, H. R. Kalbitzer, and K. Akasaka, High-pressure NMR study of the complex of a GTPase Rap1A with its effector RalGDS. A conformational switch in RalGDS revealed from non-linear pressure shifts, FEBS Letters 506, 180-184 (2001).

R. Kitahara, S. Sareth, H. Yamada, F. Ohmae, K. Gekko and K. Akasaka, High pressure NMR reveals active-site hinge motion of folate-bound Eschrichia coli dihydrofolate reductase. Biochemistry 39, 12789-12795 (2000).

K. Inoue, H. Yamada, K. Akasaka, C. Herrmann, W. Kremer, T. Maurer, R. Doeker and H. R. Kalbitzer, Pressure-induced local unfolding of the Ras-binding domain of RalGEF, Nature Structural Biology, 7, 547-550 (2000).

S. Sareth, H. Li, H. Yamada, C. K. Woodward and K. Akasaka, Rapid internal dynamics of BPTI is insensitive to pressure. 15N spin relaxation at 2 kbar. FEBS Letters 470, 11-14 (2000).

H.R. Kalbitzer, A. Goerler, P. Dubowskii, H. Li, W. Hengstenberg, C. Kowolik, H. Yamada and K. Akasaka, 15N and 1H study of histidine containingprotein (HPr) from Staphylococcus carnosus at high pressure. Protein Science 9, 693-703 (2000).

M. W. Lassalle, H. Yamada and K. Akasaka, The pressure-temperature free energy-landscape of Staphylococcal nuclease monitored by 1H NMR. J. Mol. Biol. 298, 293-302 (2000).

V. Y. Orekhov, P. V. Dubovskii, A. S. Arseniev, H. Yamada and K. Akasaka, Pressure effect on the dynamics of an isolated a-helix studied by 15N-1H NMR relaxation. J. Biol. NMR 17, 257-263 (2000).

H. Li, H. Yamada, K. Akasaka and A. M. Gronenborn, Pressure alters electronic overlap in hydrogen bonds. Journal of Biomolecular NMR 18, 207-216 (2000).

H. Li, H. Yamada, and K. Akasaka, Pressure Effect on the Tertiary Structure and Dynamics of Folded BPTI. Biophysical Journal 77, 2801-2812 (1999).

K. Akasaka, H. Li, H. Yamada, R. Li, T. Thoresen, and C. K. Woodward, Pressure Response of Protein Backbone Structure. Pressure-induced Amide 15N Chemical Shifts in BPTI. Protein Science 8, 1946-1953 (1999).

K. Inoue, H. Yamada, T. Imoto and K. Akasaka, High pressure NMR study of a small protein gurmarin. J. Biomol. NMR 12, 535-541 (1998).

Suzuki Y, Imai S, Kawakami M, Masuda Y, Akasaka K.
Identification and Determination of Low-Molecular Weight Organic Compounds in Contaminated Fog Water Using Proton Nuclear Magnetic Resonance Spectroscopy
Bull Environ Contam Toxicol. (March) 60(3):357-62 (1998).

H. Li, H. Yamada and K. Akasaka, Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatic trypsin inhibitor. Biochemistry 37, 1167-1173 (1998).

K. Akasaka, T. Tezuka and H. Yamada, Pressure-induced changes in the folded structure of lysozyme. J. Mol. Biol. 271, 671-678 (1997).

Books and reviews (1999~2006):

K. Akasaka, Probing Conformational Fluctuation of Proteins by Pressure Perturbation. Chemical Reviews Thematic Issue “Protein Dynamics and Folding” (Guest Editor: A. Joshua Wand) 108, 1814-1835(2006).

M. Lassalle and K. Akasaka,:The Use of High Pressure NMR to Study Protein Folding, in Methods in Molecular Biology vol. 350: Protein Folding Protocols in (edited by Yawen Bai and Ruth Nussinov), Humana Press Inc.21-38 (2006)..

H. Li and K. Akasaka, Conformational fluctuations of proteins revealed by variable pressure NMR. Biochimica et Biophysica Acta 1764, 331-345 (2006).

R. Kitahara, S. Yokoyama and K. Akasaka, Creating a new paradigm of protein structure through variable pressure NMR spectroscopy. Spectroscopic Research (Bunko Kenkyku) 55, 10-20 (2006). (in Japanese)

K. Akasaka, A new view of proteins emerging from variable pressure NMR studies. The Review of High Pressure Science and TechnologyÿVol. 13, No. 4 (2004). (in Japanese)

Y. O. Kamatari, R. Kitahara, H.Yamada, S.Yokoyama, and K. Akasaka, High pressure NMR spectroscopy for characterizing non-native conformers of proteins. Methods 34 133-143 (2004).

K. Akasaka, Highly fluctuating protein structures revealed by variable pressure NMR. Biochemistry (Current Topics) 42, 1875-1885 (2003). (web release on Aug 28)

K. Akasaka, Exploring the entire conformational space of proteins by high pressure NMR. Pure and Applied Chemistry 75, No.7, 927-936 (2003).

K. Akasaka, High pressure NMR spectroscopy characterizes higher energy conformers of proteins. in Advances in High Pressure Bioscience and Biotechnology II (R. Winter, ed.), Springer, 9-14 (2003).

K. Akasaka, High pressure NMR expands the protein structure world. Seibutsu-butsuri (Biophysics) 42, 206-211 (2002) (in Japanese).

K. Akasaka and H. Yamada, On-Line Cell High Pressure Nuclear Magnetic Resonance Technique: Application to Protein Studies. in Methods in Enzymology 338: Nuclear Magnetic Resonance of Biological Macromolecules Part A (T. L. James et al. , eds.), Academic Press, 134-158 (2001).
ÿÿÿÿÿÿÿÿÿÿÿ ÿÿÿ
K. Akasaka, H. Li, P. Dubovskii, H. R. Kalbitzer, and H. Yamada, High resolution-High pressure NMR spectroscopy. Application to protein structure, dynamics and folding. in Structure, Dynamics and Function of Biological Macromolecules. (O. Jardetzky and M. D. Finucane, eds.) IOS Press, Amsterdam, Netherlands (2001) 77-92.

K. Akasaka and H. Li, A novel picture of protein from high pressure NMR 1. How soft is the native structure ? Tampakushitsu Kakusan Koso (Protein, Nucleic Acid and Enzyme) (2001)46, 208-219 (in Japanese).

K. Akasaka, The high pressure, high magnetic field NMR facility at Kobe University, Tampakushitsu Kakusan Koso (Protein, Nucleic Acid and Enzyme) 45, 1383-1388 (2000) (in Japanese).

K. Akasaka, High pressure NMR study on protein dynamics and folding. in Old and New Views of Protein Folding (K. Kuwajima and M. Arai, eds.) Elsevier Science B.V., Amsterdam (1999).

K. Akasaka, High pressure NMR: A novel tool for studying protein structure and dynamics. in Trends, Graduate School of Science and Technology, Kobe University, Springer-Verlg, 51-61 (1999).




© 2006 - 2014 Institut für Biophysik und physikalische Biochemie / Universität Regensburg
webmaster / Impressum