High-resolution nuclear magnetic resonance studies of proteins.

The combination of advanced high-resolution nuclear magnetic resonance (NMR) techniques with high-pressure capability represents a powerful experimental tool in studies of protein folding. This review is organized as follows: after a general introduction of high-pressure, high-resolution NMR spectroscopy of proteins, the experimental part deals with instrumentation. The main section of the review is devoted to NMR studies of reversible pressure unfolding of proteins with special emphasis on pressure-assisted cold denaturation and the detection of folding intermediates. Recent studies investigating local perturbations in proteins and the experiments following the effects of point mutations on pressure stability of proteins are also discussed. Ribonuclease A, lysozyme, ubiquitin, apomyoglobin, alpha-lactalbumin and troponin C were the model proteins investigated.

[1]  H. Yamada,et al.  Pressure-resisting cell for high-pressure, high-resolution nuclear magnetic resonance measurements at very high magnetic fields , 2001 .

[2]  D. Shortle.  The denatured state (the other half of the folding equation) and its role in protein stability , 1996, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[3]  J. Jonas,et al.  A high-pressure, high-resolution NMR probe for experiments at 500 MHz. , 1998, Journal of magnetic resonance.

[4]  H. Yamada.  Pressure‐resisting glass cell for high pressure, high resolution NMR measurement , 1974 .

[5]  C. Kay,et al.  Ca2+, Mg2+, and troponin I inhibitory peptide binding to a Phe-154 to Trp mutant of chicken skeletal muscle troponin C. , 1994, Biochemistry.

[6]  J. Silva,et al.  High-pressure NMR study of the dissociation of Arc repressor. , 1994, Biochemistry.

[7]  M. C. Gough,et al.  Pressure and temperature dependence of proton spin relaxation in liquid n-heptane , 1969 .

[8]  A. Hinck,et al.  Effects of amino acid substitutions on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy. , 1993, Biochemistry.

[9]  I. Artaki,et al.  Pressure effect on the coupling between rotational and translational motions of supercooled viscous fluids , 1985 .

[10]  J. Jonas.  Nuclear Magnetic Resonance at High Pressure , 1982, Science.

[11]  A. Fink,et al.  Discrete intermediates versus molten globule models for protein folding: characterization of partially folded intermediates of apomyoglobin. , 1998, Folding & design.

[12]  H. G. Drickamer,et al.  Systems under Pressure. (Book Reviews: Electronic Transitions and the High Pressure Chemistry and Physics of Solids) , 1973 .

[13]  J. Jonas,et al.  Hydrogen-exchange kinetics in the cold denatured state of ribonuclease A. , 1996, Biochimica et biophysica acta.

[14]  P. Prevelige,et al.  The use of hydrostatic pressure as a tool to study viruses and other macromolecular assemblages. , 1996, Current opinion in structural biology.

[15]  H. Yamada,et al.  Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton NMR. , 1995, Journal of molecular biology.

[16]  A. Jonas,et al.  Effects of high pressure and temperature on the wild-type and F29W mutant forms of the N-domain of avian troponin C. , 1999, Biochimica et biophysica acta.

[17]  J. Jonas.  High-Pressure Raman Scattering Studies of Fluids , 1999 .

[18]  P. S. Kim,et al.  Intermediates in the folding reactions of small proteins. , 1990, Annual review of biochemistry.

[19]  P. A. Evans,et al.  Structure of very early protein folding intermediates: new insights through a variant of hydrogen exchange labelling. , 1996, Folding & design.

[20]  H. Yamada,et al.  The pressure-temperature free energy-landscape of staphylococcal nuclease monitored by (1)H NMR. , 2000, Journal of molecular biology.

[21]  J. Jonas,et al.  High-resolution, high-pressure NMR studies of proteins. , 1998, Biophysical journal.

[22]  J. Jonas.  Nuclear Magnetic Resonance Measurements at High Pressure , 1972 .

[23]  J. Silva,et al.  Molten-globule conformation of Arc repressor monomers determined by high-pressure 1H NMR spectroscopy. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[24]  R. L. Baldwin,et al.  Alternative models for describing the acid unfolding of the apomyoglobin folding intermediate. , 1998, Biochemistry.

[25]  A. Fink,et al.  Cold denaturation and 2H2O stabilization of a staphylococcal nuclease mutant. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[26]  A. Wand,et al.  High-Resolution Triple-Resonance NMR Spectroscopy of a Novel Calmodulin·Peptide Complex at Kilobar Pressures , 1996 .

[27]  R. L. Baldwin,et al.  Molecular mechanisms of acid denaturation. The role of histidine residues in the partial unfolding of apomyoglobin. , 1994, Journal of molecular biology.

[28]  C. Woodward,et al.  Rapid internal dynamics of BPTI is insensitive to pressure , 2000, FEBS letters.

[29]  P. Masson,et al.  High pressure effects on protein structure and function , 1996, Proteins.

[30]  H. Yamada,et al.  Pressure-induced changes in the folded structure of lysozyme. , 1997, Journal of molecular biology.

[31]  J. Moult,et al.  Construction and characterization of a spectral probe mutant of troponin C: application to analyses of mutants with increased Ca2+ affinity. , 1992, Biochemistry.

[32]  A. Jonas,et al.  NMR study of the cold, heat, and pressure unfolding of ribonuclease A. , 1995, Biochemistry.

[33]  E. Purcell,et al.  Nuclear Magnetic Resonance in Liquids under High Pressure , 1954 .

[34]  L Mayne,et al.  Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR. , 1992, Annual review of biophysics and biomolecular structure.

[35]  A. Jonas,et al.  High-pressure NMR spectroscopy of proteins and membranes. , 1994, Annual review of biophysics and biomolecular structure.

[36]  R. L. Baldwin,et al.  Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[37]  H. Yamada,et al.  Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatic trypsin inhibitor. , 1998, Biochemistry.

[38]  G Weber,et al.  The effect of high pressure upon proteins and other biomolecules , 1983, Quarterly Reviews of Biophysics.

[39]  J. Jonas,et al.  Structure of pressure-assisted cold denatured lysozyme and comparison with lysozyme folding intermediates. , 1997, Biochemistry.

[40]  J. Jonas,et al.  Structure of the pressure-assisted cold denatured state of ubiquitin. , 1997, Biochemical and biophysical research communications.

[41]  H. Jane Dyson,et al.  Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding , 1998, Nature Structural Biology.

[42]  S. Sligar,et al.  High-pressure denaturation of apomyoglobin. , 2000, Biochimica et biophysica acta.

[43]  R. L. Baldwin,et al.  Nuclear magnetic resonance evidence for a structural intermediate at an early stage in the refolding of ribonuclease A. , 1978, Journal of molecular biology.

[44]  G. Trigo-Gonzalez,et al.  A comparative spectroscopic study of tryptophan probes engineered into high- and low-affinity domains of recombinant chicken troponin C. , 1992, Biochemistry.

[45]  C. Kay,et al.  Properties of isolated recombinant N and C domains of chicken troponin C. , 1994, Biochemistry.