Pressure response of protein backbone structure. Pressure-induced amide 15N chemical shifts in BPTI

Protein Science

Volumn 8, Issue 10, 1999, Pages 1946-1953

  Akasaka, Kazuyuki ^a   Li, Hua ^a   Yamada, Hiroaki ^a   Li, Renhao ^b   Thoresen, Todd ^b   Woodward, Clare K ^b  

^a KOBE UNIVERSITY   (Japan)

^b UNIVERSITY OF MINNESOTA   (United States)

Author keywords

( , ) angles; 15N chemical shift; Basic pancreatic trypsin inhibitor; Compressibility; High pressure NMR; Hydrogen bond; Volume fluctuation

Indexed keywords

APROTININ; CARBONYL DERIVATIVE; POLYPEPTIDE; WATER;

ARTICLE; CONTROLLED STUDY; HYDROGEN BOND; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PRESSURE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE;

EID: 0032869077     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.10.1946     Document Type: Article

References (68)

1. Akasaka K, Tezuka T, Yamada H. 1997. Pressure-induced changes in the folded structure of lysozyme. J Mol Biol 271:671-678.
2. Asakawa N, Kameda T, Kuroki S, Kurosu H, Ando S, Ando I, Shoji A. 1998. Structural studies of hydrogen-bonded peptides and polypeptides by solid-state NMR. Ann Rep NMR Spectroscopy 35:55-137.
3. Asakura T, Taoka K, Demura M, Williamson MP. 1995. The relationship between amide proton chemical shifts and secondary structure in proteins. J Biomol NMR 6:227-236.
4. Berndt KD, Guntert P, Orbons LPM, Wüthrich K. 1992. Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures. J Mol Biol 227:757-775.
5. Bodenhausen G, Ruben DJ. 1980. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem Phys Lett 69:185-189.
6. Brunne RM, van Gunsteren WF. 1993. Dynamical properties of bovine pancreatic trypsin inhibitor from a molecular dynamics simulation at 5000 atm. FEBS Lett 323:215-217.
7. Cavanagh J, Fairbrother WJ, Palmer AG III, Skelton NJ. 1996. Protein NMR spectroscopy principles and practice. San Diego: Academic Press, Inc. pp 175-176.
8. Cioni P, Strambini GB. 1996. Pressure-induced dissociation of yeast glyceraldehyde-3-phosphate dehydrogenase: Heterogeneous kinetics and perturbations of subunit structure. J Mol Biol 263:789-799.
9. Cooper A. 1976. Thermodynamic fluctuations in protein molecules. Proc Natl Acad Sci USA 73:2740-2741.
10. Deisenhofer J, Steigemann W. 1975. Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at 1.5 Å resolution. Acta Crystallogr B 31:238-250.
11. 562 examined by the dependence of hydrogen exchange on hydrostatic pressure. Biochemistry 37:9877-9883.
12. Gekko K, Hasegawa Y. 1986. Compressibility-structure relationship of globular proteins. Biochemistry 25:6563-6571.
13. Gekko K, Noguchi H. 1979. Compressibility of globular proteins in water at 25°C. J Phys Chem 53:2706-2714.
14. 15N chemical shifts of backbone amides in bovine pancreatic trypsin inhibitor and apamin. J Am Chem Soc 111:7716-7722.
15. Gross M, Jaenicke R. 1994. Proteins under pressure. The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes. Eur J Biochem 221:617-630.
16. Hawley SA. 1971. Reversible pressure-temperature denaturation of chymotrypsinogen. Biochemistry 10:2436-2442.
17. Heremans K, Smeller L. 1998. Protein structure and dynamics at high pressure. Biochim Biophys Acta 1386:353-370.
18. Hitchens TK, Bryant RG. 1998. Pressure dependence of amide hydrogen-deuterium exchange rates for individual sites in T4 lysozyme. Biochemistry 37:5878-5887.
19. Huang J, Ridsdale A, Wang J, Friedman JM. 1997. Kinetic hole burning, hole filling, and conformational relaxation in heme proteins: Direct evidence for the functional significance of a hierarchy of dynamical processes. Biochemistry 36:14353-14365.
20. Inoue K, Yamada H, Imoto T, Akasaka K. 1998. High pressure NMR study of a small protein, gurmarin. J Biomol NMR 12:535-541.
21. Isaacs NS. 1981. Liquid phase high pressure chemistry. New York: John Wiley & Sons. pp 155-180.
22. Iwanaga S, Morita T, Kato H, Harada T, Adachi N, Sugo T, Muruyama K, Takada K, Kimura T, Sakakibara S. 1979. In: Fujii S, Moriya H, Suzuki T, eds. Kinins II: Biochemistry, pathophysiology, and clinical aspects. New York: Plenum Press. pp 147-163.
23. Jonas J, Jonas A. 1994. High-pressure NMR spectroscopy of proteins and membranes. Annu Rev Biophys Biomol Struct 23:287-318.
24. Kay LE, Keifer P, Saarinen T. 1992. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J Am Chem Soc 114:10663-10665.
25. Kharakoz DP. 1997. Partial volumes and compressibilities of extended polypeptide chains in aqueous solution: Additivity scheme and implication of protein unfolding at normal and high pressure. Biochemistry 36:10276-10285.
26. Kharakoz DP, Sarvazyan AP. 1993. Hydrational and intrinsic compressibilities of globular proteins. Biopolymers 33:11-26.
27. Kim KS, Fuchs J, Woodward C. 1993. Hydrogen exchange identifies native-state motional domains important in protein folding. Biochemistry 32:9600-9608.
28. Kitchen DB, Reed LH, Levy RM. 1992. Molecular dynamics simulation of solvated protein at high pressure. Biochemistry 31:10083-10093.
29. Kobayashi N, Yamato T, Go N. 1997. Mechanical property of a TIM-barrel protein. Proteins Struct Funct Genet 28:109-116.
30. Kowalski JM, Parekh RN, Wittrup KD. 1998. Secretion efficiency in Saccharomyces cerevisiae of bovine pancreatic trypsin inhibitor mutants lacking disulfide bonds is correlated with thermodynamic stability. Biochemistry 37:1264-1273.
31. Kundrot CE, Richards FM. 1987. Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres. J Mol Biol 193:157-170.
32. Kunugi S. 1993. Modification of biopolymer functions by high-pressure. Prog Polym Sci 18:805-838.
33. 15N NMR chemical shifts in proteins and secondary structure. J Biomol NMR 4:341-348.
34. Li H, Yamada H, Akasaka K. 1998. Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatic trypsin inhibitor. Biochemistry 37:1167-1173.
35. 15N NMR study of Gramicidin S in water and organic solvents. J Am Chem Soc 106:1939-1941.
36. Llinas M, Horsley WJ, Klein MP. 1976. Nitrogen-15 nuclear magnetic resonance spectrum of alumichrome. Detection by a double resonance Fourier transform technique. J Am Chem Soc 24:7554-7558.
37. Makhatadze G, Kim KS, Woodward C, Privalov P. 1993. Thermodynamics of BPTI folding. Protein Sci 2:2028-2036.
38. Morishima I. 1987. Current perspectives of high pressure biology. London: Academic Press. pp 315-333.
39. Mozhaev VV, Heremans K, Frank J, Masson P, Balny C. 1996. High pressure effects on protein structure and function. Proteins Struct Funct Genet 24: 81-91.
40. Paladini AA Jr, Weber G. 1981. Pressure-induced reversible dissociation of enolase. Biochemistry 20:2587-2593.
41. Palmer AG III, Cavanagh PE, Wright PE, Rance M. 1991. Sensitivity improvement in proton-detected 2-dimensional heteronuclear correlation NMR-spectroscopy. J Magn Reson 93:151-170.
42. Panick G, Malessa R, Winter R, Rapp G, Frye K, Royer C. 1998. Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy. J Mol Biol 275:389-402.
43. Parekh RN, Shaw MR, Wittrup KD. 1996. An interesting vector for tunable, high copy, stable integration into the dispersed Ty δ sites of Saccharomyces cerevisiae. Biotechnol Prog 12:16-21.
44. Parkin S, Rupp B, Hope H. 1995. Protein Data Bank (IBPI). Upton, NY: Brookhaven National Laboratory.
45. Prehoda KE, Mooberry S, Markley JL. 1998. Pressure denaturation of proteins: Evaluation of compressibility effects. Biochemistrv 37:5785-5790.
46. Royer CA, Hinck AP, Loh SN, Prehoda KE, Peng X, Jonas J, Markley JL. 1993. Effects of amino acid substitutions on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy. Biochemistry 52:5222-5232.
47. Saito H, Nukada K. 1971. The hydrogen bond studied by nitrogen-14 nuclear magnetic resonance. II. Heteronuclear magnetic double resonance study of nitrogen-14 hydrogen-bond shifts of pyrroles and indole. J Am Chem Soc 95:1072-1081.
48. Shaka AJ, Baker PB, Freeman R. 1985. Computer-optimized decoupling scheme for wideband applications and low-level operation. J Magn Reson 64:547-553.
49. Sitkoff D, Case DA. 1998. Theories of chemical shift anisotropies in proteins and nucleic acids. Prog Nucl Magn Res Spectrosc 32:165-190.
50. Smith PE, Schaik RC, Szyperski T. Wüthrich K, Gunsteren WF. 1995. Internal mobility of the basic pancreatic trypsin inhibitor in solution: A comparison of NMR spin relaxation measurements and molecular dynamics simulations. J Mol Biol 246:356-365.
51. Takeda N, Kato M, Taniguchi Y. 1995. Pressure-and thermally-induced reversible changes in the secondary structure of ribonuclease A studied by FT-IR spectroscopy. Biochemistry 34:5980-5987.
52. Taniguchi Y, Suzuki K. 1983. Studies of polymer effects under pressure. 7. Pressure inactivation of alpha-chymotrypsin. J Phys Chem 87:5185-5193.
53. 1H resonance of glycine-37 in basic pancreatic trypsin inhibitor. Biochemistry 26:1918-1925.
54. 1H NMR at variable pressure. FEBS Lett 112:280-284.
55. Wagner G, Braun W, Havel TF, Schaumann T, Go N, Wüthrich K. 1987. Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN. J Mol Biol 196:611-639.
56. Wagner G, Pardi A, Wüthrich K. 1983. Protein conformation and proton nuclear-magnetic-resonance chemical shifts. J Am Chem Soc 105:5948.
57. Williamson MP, Asakura T. 1993. Empirical comparisons of models for chemical-shift calculation in proteins. J Magn Reson B 101:63-71.
58. 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J Biomol NMR 5:67-81.
59. 15N chemical shift referencing in biomolecular NMR. J Biomol NMR 6:135-140.
60. Wlodawer A, Nachman J, Gilliland GL, Gallagher W, Woodward C. 1987. Structure of form III crystals of bovine pancreatic trypsin inhibitor. J Mol Biol 198:469-480.
61. Wlodawer A, Walter J, Huber R, Sjolin L. 1984. Structure of bovine pancreatic trypsin inhibitor. Results of joint neutron and X-ray refinement of crystal form II. J Mol Biol 193:145-156.
62. Wroblowski B, Fernando D, Heremans K, Engelborghs Y. 1996. Molecular mechanisms of pressure induced conformational changes in BPTI. Proteins Struct Funct Genet 25:446-455.
63. Yamada H. 1974. Pressure-resisting glass cell for high pressure, high resolution NMR measurement. Rev Sci Instrum 45:640-642.
64. Yamaguchi T, Yamada H, Akasaka K. 1995. Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton NMR. J Mol Biol 250:689-694.
65. Zhang J, Peng X, Jonas A, Jonas J. 1995. NMR study of the cold, heat, and pressure unfolding of ribonuclease A. Biochemistry 34:8631-8641.
66. Zipp A, Kauzmann W. 1973. Pressure denaturation of metmyoglobin. Biochemistry 12:4217-4228.
67. Zollfrank J, Friedrich J, Fidy J, Vanderkooi JM. 1991a. Photochemical holes under pressure - Compressibility and volume fluctuations of a protein. J Chem Phys 94:8600-8603.
68. Zollfrank J, Friedrich J, Vanderkooi JM, Fidy J. 1991b. Conformational relaxation of a low-temperature protein as probed by photochemical hole burning. Horseradish peroxidase. Biophys J 59:305-312.