메뉴 건너뛰기




Volumn 327, Issue 4, 2003, Pages 857-865

Pressure-dependent changes in the solution structure of hen egg-white lysozyme

Author keywords

Buried water; Chemical shift; Compression; Lysozyme; Pressure

Indexed keywords

EGG WHITE; GLOBULAR PROTEIN; LYSOZYME; WATER;

EID: 0344406172     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00209-2     Document Type: Article
Times cited : (133)

References (38)
  • 1
    • 0039116206 scopus 로고    scopus 로고
    • Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comprehensive survey
    • Szilágyi A., Závodszky P. Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey. Struct. Fold. Des. 8:2000;493-504.
    • (2000) Struct. Fold. Des. , vol.8 , pp. 493-504
    • Szilágyi, A.1    Závodszky, P.2
  • 2
    • 0005492283 scopus 로고    scopus 로고
    • Structural comparison of psychrophilic and mesophilic trypsins - Elucidating the molecular basis of cold adaptation
    • Leiros H.K.S., Willassen N.P., Smalås A.O. Structural comparison of psychrophilic and mesophilic trypsins - elucidating the molecular basis of cold adaptation. Eur. J. Biochem. 267:2000;1039-1049.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1039-1049
    • Leiros, H.K.S.1    Willassen, N.P.2    Smalås, A.O.3
  • 3
    • 0034734270 scopus 로고    scopus 로고
    • Halophilic enzymes: Proteins with a grain of salt
    • Mevarech M., Frolow F., Gloss L.M. Halophilic enzymes: proteins with a grain of salt. Biophys. Chem. 86:2000;155-164.
    • (2000) Biophys. Chem. , vol.86 , pp. 155-164
    • Mevarech, M.1    Frolow, F.2    Gloss, L.M.3
  • 4
    • 0029859688 scopus 로고    scopus 로고
    • Intrinsic compressibility and volume compression in solvated proteins by molecular dynamics simulation at high pressure
    • Paci E., Marchi M. Intrinsic compressibility and volume compression in solvated proteins by molecular dynamics simulation at high pressure. Proc. Natl Acad. Sci. USA. 93:1996;11609-11614.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 11609-11614
    • Paci, E.1    Marchi, M.2
  • 5
    • 0023644307 scopus 로고
    • Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres
    • Kundrot C.E., Richards F.M. Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres. J. Mol. Biol. 193:1987;157-170.
    • (1987) J. Mol. Biol. , vol.193 , pp. 157-170
    • Kundrot, C.E.1    Richards, F.M.2
  • 6
    • 0036154017 scopus 로고    scopus 로고
    • Probing substates in sperm whale myoglobin using high-pressure crystallography
    • Urayama P., Phillips G.N., Gruner S.M. Probing substates in sperm whale myoglobin using high-pressure crystallography. Struct. Fold. Des. 10:2002;51-60.
    • (2002) Struct. Fold. Des. , vol.10 , pp. 51-60
    • Urayama, P.1    Phillips, G.N.2    Gruner, S.M.3
  • 7
    • 0037171119 scopus 로고    scopus 로고
    • High-resolution nuclear magnetic resonance studies of proteins
    • Jonas J. High-resolution nuclear magnetic resonance studies of proteins. Biochim. Biophys. Acta. 1595:2002;145-159.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 145-159
    • Jonas, J.1
  • 8
    • 0028220701 scopus 로고
    • Proteins under pressure: The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes
    • Gross M., Jaenicke R. Proteins under pressure: the influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes. Eur. J. Biochem. 221:1994;617-630.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 617-630
    • Gross, M.1    Jaenicke, R.2
  • 9
    • 0031714901 scopus 로고    scopus 로고
    • Protein structure and dynamics at high pressure
    • Heremans K., Smeller L. Protein structure and dynamics at high pressure. Biochim. Biophys. Acta. 1386:1998;353-370.
    • (1998) Biochim. Biophys. Acta , vol.1386 , pp. 353-370
    • Heremans, K.1    Smeller, L.2
  • 10
    • 0000725483 scopus 로고
    • Thermodynamic fluctuations in protein molecules
    • Cooper A. Thermodynamic fluctuations in protein molecules. Proc. Natl Acad. Sci. USA. 73:1976;2740-2741.
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 2740-2741
    • Cooper, A.1
  • 11
    • 0022999267 scopus 로고
    • Compressibility-structure relationship of globular proteins
    • Gekko K., Hasegawa Y. Compressibility-structure relationship of globular proteins. Biochemistry. 25:1986;6563-6571.
    • (1986) Biochemistry , vol.25 , pp. 6563-6571
    • Gekko, K.1    Hasegawa, Y.2
  • 13
    • 0028988451 scopus 로고
    • 1H NMR chemical shifts to measure the quality of protein structures
    • 1H NMR chemical shifts to measure the quality of protein structures. J. Mol. Biol. 247:1995;541-546.
    • (1995) J. Mol. Biol. , vol.247 , pp. 541-546
    • Williamson, M.P.1    Kikuchi, J.2    Asakura, T.3
  • 14
    • 0035939953 scopus 로고    scopus 로고
    • Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate
    • Vocadlo D.J., Davies G.J., Laine R., Withers S.G. Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. Nature. 412:2001;835-838.
    • (2001) Nature , vol.412 , pp. 835-838
    • Vocadlo, D.J.1    Davies, G.J.2    Laine, R.3    Withers, S.G.4
  • 15
    • 0035079181 scopus 로고    scopus 로고
    • A refined solution structure of hen lysozyme determined using residual dipolar coupling data
    • Schwalbe H., Grimshaw S.B., Spencer A., Buck M., Boyd J., Dobson C.M., et al. A refined solution structure of hen lysozyme determined using residual dipolar coupling data. Protein Sci. 10:2001;677-688.
    • (2001) Protein Sci. , vol.10 , pp. 677-688
    • Schwalbe, H.1    Grimshaw, S.B.2    Spencer, A.3    Buck, M.4    Boyd, J.5    Dobson, C.M.6
  • 16
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt G.J., Jones T.A. Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallog. sect. D. 50:1994;178-185.
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 18
    • 0032477750 scopus 로고    scopus 로고
    • Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatric trypsin inhibitor
    • Li H., Yamada H., Akasaka K. Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatric trypsin inhibitor. Biochemistry. 37:1998;1167-1173.
    • (1998) Biochemistry , vol.37 , pp. 1167-1173
    • Li, H.1    Yamada, H.2    Akasaka, K.3
  • 19
    • 0001385140 scopus 로고
    • High-pressure Raman study of the hydrogen-bonded crystalline formamide
    • Shimizu H., Nagata K., Sasaki S. High-pressure Raman study of the hydrogen-bonded crystalline formamide. J. Chem. Phys. 89:1988;2743-2747.
    • (1988) J. Chem. Phys. , vol.89 , pp. 2743-2747
    • Shimizu, H.1    Nagata, K.2    Sasaki, S.3
  • 21
    • 0028013478 scopus 로고
    • Thermal expansion of hen egg-white lysozyme
    • Young A.C.M., Tilton R.F., Dewan J.C. Thermal expansion of hen egg-white lysozyme. J. Mol. Biol. 235:1994;302-317.
    • (1994) J. Mol. Biol. , vol.235 , pp. 302-317
    • Young, A.C.M.1    Tilton, R.F.2    Dewan, J.C.3
  • 22
    • 0026606219 scopus 로고
    • Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease-A at nine different temperatures from 98 to 320 K
    • Tilton R.F., Dewan J.C., Petsko G.A. Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease-A at nine different temperatures from 98 to 320 K. Biochemistry. 31:1992;2469-2481.
    • (1992) Biochemistry , vol.31 , pp. 2469-2481
    • Tilton, R.F.1    Dewan, J.C.2    Petsko, G.A.3
  • 24
    • 0036293397 scopus 로고    scopus 로고
    • Temperature-dependence of protein hydrogen bond properties as studied by high-resolution NMR
    • doi: 10.1006/jmbi.2002.5446
    • Cordier F., Grzesiek S. Temperature-dependence of protein hydrogen bond properties as studied by high-resolution NMR. J. Mol. Biol. 317:2002;739-752. doi: 10.1006/jmbi.2002.5446.
    • (2002) J. Mol. Biol. , vol.317 , pp. 739-752
    • Cordier, F.1    Grzesiek, S.2
  • 26
    • 0033578333 scopus 로고    scopus 로고
    • Binding of buried structural water increases the flexibility of proteins
    • Fischer S., Verma C.S. Binding of buried structural water increases the flexibility of proteins. Proc. Natl Acad. Sci. USA. 96:1999;9613-9615.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 9613-9615
    • Fischer, S.1    Verma, C.S.2
  • 29
    • 0016056448 scopus 로고
    • Pressure-resisting glass cell for high pressure, high resolution NMR measurement
    • Yamada H. Pressure-resisting glass cell for high pressure, high resolution NMR measurement. Rev. Sci. Instrum. 45:1974;640-642.
    • (1974) Rev. Sci. Instrum. , vol.45 , pp. 640-642
    • Yamada, H.1
  • 30
    • 0031554921 scopus 로고    scopus 로고
    • Pressure-induced changes in the folded structure of lysozyme
    • Akasaka K., Tezuka T., Yamada H. Pressure-induced changes in the folded structure of lysozyme. J. Mol. Biol. 271:1997;671-678.
    • (1997) J. Mol. Biol. , vol.271 , pp. 671-678
    • Akasaka, K.1    Tezuka, T.2    Yamada, H.3
  • 31
    • 0034711091 scopus 로고    scopus 로고
    • High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase
    • Kitahara R., Sareth S., Yamada H., Ohmae E., Gekko K., Akasaka K. High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase. Biochemistry. 39:2000;12789-12795.
    • (2000) Biochemistry , vol.39 , pp. 12789-12795
    • Kitahara, R.1    Sareth, S.2    Yamada, H.3    Ohmae, E.4    Gekko, K.5    Akasaka, K.6
  • 33
    • 0029314335 scopus 로고
    • The impact of direct refinement against proton chemical shifts on protein structure determination by NMR
    • Kuszewski J., Gronenborn A.M., Clore G.M. The impact of direct refinement against proton chemical shifts on protein structure determination by NMR. J. Magn. Reson. 107:1995;293-297.
    • (1995) J. Magn. Reson. , vol.107 , pp. 293-297
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 34
    • 44949269218 scopus 로고
    • Empirical comparisons of models for chemical shift calculation in proteins
    • Williamson M.P., Asakura T. Empirical comparisons of models for chemical shift calculation in proteins. J. Magn. Reson., Ser. B. 101:1993;63-71.
    • (1993) J. Magn. Reson., Ser. B , vol.101 , pp. 63-71
    • Williamson, M.P.1    Asakura, T.2
  • 35
    • 0000635348 scopus 로고
    • The relationship between amide proton chemical shifts and secondary structure in proteins
    • Asakura T., Taoka K., Demura M., Williamson M.P. The relationship between amide proton chemical shifts and secondary structure in proteins. J. Biomol. NMR. 6:1995;227-236.
    • (1995) J. Biomol. NMR , vol.6 , pp. 227-236
    • Asakura, T.1    Taoka, K.2    Demura, M.3    Williamson, M.P.4
  • 38
    • 0029004611 scopus 로고
    • The volume of atoms on the protein surface calculated from simulation, using Voronoi polyhedra
    • Gerstein M., Tsai J., Levitt M. The volume of atoms on the protein surface calculated from simulation, using Voronoi polyhedra. J. Mol. Biol. 249:1995;955-966.
    • (1995) J. Mol. Biol. , vol.249 , pp. 955-966
    • Gerstein, M.1    Tsai, J.2    Levitt, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.