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Volumn 40, Issue 1, 2011, Pages 81-98

High-pressure protein crystallography and NMR to explore protein conformations

Author keywords

conformational substates; energy landscape; pressure cryocooling; protein thermodynamics

Indexed keywords

BERYLLIUM; DIAMOND; DIHYDROFOLATE REDUCTASE; ENHANCED GREEN FLUORESCENT PROTEIN; HISTIDINE; LIQUID NITROGEN; MYOGLOBIN; UBIQUITIN; URATE OXIDASE;

EID: 79955806443     PISSN: 1936122X     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev-biophys-042910-155304     Document Type: Article
Times cited : (56)

References (59)
  • 1
    • 33748604768 scopus 로고    scopus 로고
    • + Transporter: Multiple Conformations of an Octameric Ring
    • DOI 10.1016/j.cell.2006.08.028, PII S009286740601097X
    • Albright RA, Ibar JL, Kim CU, Gruner SM, Morais-Cabral JH. 2006. The RCK domain of the KtrAB K+ transporter: multiple conformations of an octameric ring. Cell 126:1147-59 (Pubitemid 44380292)
    • (2006) Cell , vol.126 , Issue.6 , pp. 1147-1159
    • Albright, R.A.1    Ibar, J.-L.V.2    Kim, C.U.3    Gruner, S.M.4    Morais-Cabral, J.H.5
  • 2
    • 54349114270 scopus 로고    scopus 로고
    • Structural and thermodynamic characterization of T4 lysozyme mutants and the contribution of internal cavities to pressure denaturation
    • Ando N, Barstow B, Baase WA, Fields A, Matthews BW, Gruner SM. 2008. Structural and thermodynamic characterization of T4 lysozyme mutants and the contribution of internal cavities to pressure denaturation. Biochemistry 47:11097-109
    • (2008) Biochemistry , vol.47 , pp. 11097-109
    • Ando, N.1    Barstow, B.2    Baase, W.A.3    Fields, A.4    Matthews, B.W.5    Gruner, S.M.6
  • 3
    • 51649104603 scopus 로고    scopus 로고
    • Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift
    • Barstow B, Ando N, Kim CU, Gruner SM. 2008. Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift. Proc. Natl. Acad. Sci. USA 105:13362-66
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 13362-13366
    • Barstow, B.1    Ando, N.2    Kim, C.U.3    Gruner, S.M.4
  • 4
    • 70350028297 scopus 로고    scopus 로고
    • Coupling of pressure-induced structural shifts to spectral changes in a yellow fluorescent protein
    • Barstow B, Ando N, Kim CU, Gruner SM. 2009. Coupling of pressure-induced structural shifts to spectral changes in a yellow fluorescent protein. Biophys. J. 97:1719-27
    • (2009) Biophys. J. , vol.97 , pp. 1719-1727
    • Barstow, B.1    Ando, N.2    Kim, C.U.3    Gruner, S.M.4
  • 5
    • 0001435569 scopus 로고
    • The coagulation of albumin by pressure
    • Bridgman PW. 1914. The coagulation of albumin by pressure. J. Biol. Chem. 19:511-12
    • (1914) J. Biol. Chem. , vol.19 , pp. 511-512
    • Bridgman, P.W.1
  • 6
    • 0003166498 scopus 로고    scopus 로고
    • Protein folding in the landscape perspective: Chevron plots and non- rrhenius kinetics
    • DOI 10.1002/(SICI)1097-0134(19980101)30:1<2::AID-PROT2>3.0.CO;2-R
    • Chan HS, Dill KA. 1998. Protein folding in the landscape perspective: chevron plots and non-Arrhenius kinetics. Proteins 30:2-33 (Pubitemid 28036107)
    • (1998) Proteins: Structure, Function and Genetics , vol.30 , Issue.1 , pp. 2-33
    • Chan, H.S.1    Dill, K.A.2
  • 7
    • 0033535981 scopus 로고    scopus 로고
    • Effects of pressure on the kinetics of capture by yeast alcohol dehydrogenase
    • Cho YK, Northrop DB. 1999. Effects of pressure on the kinetics of capture by yeast alcohol dehydrogenase. Biochemistry 38:7470-75
    • (1999) Biochemistry , vol.38 , pp. 7470-7475
    • Cho, Y.K.1    Northrop, D.B.2
  • 8
    • 0033609806 scopus 로고    scopus 로고
    • Pressure/temperature effects on protein flexibilty from acrylamide quenching of protein phosphorescence
    • DOI 10.1006/jmbi.1999.3010
    • Cioni P, Strambini GB. 1999. Pressure/temperature effects on protein flexibilty from acrylamide quenching of protein phosphorescence. J. Mol. Biol. 291:955-64 (Pubitemid 29403623)
    • (1999) Journal of Molecular Biology , vol.291 , Issue.4 , pp. 955-964
    • Cioni, P.1    Strambini, G.B.2
  • 10
    • 33847308554 scopus 로고    scopus 로고
    • Structural Rigidity of a Large Cavity-containing Protein Revealed by High-pressure Crystallography
    • DOI 10.1016/j.jmb.2006.12.021, PII S0022283606016962
    • Collins MD, Quillin ML, Hummer G, Matthews BW, Gruner SM. 2007. Structural rigidity of a large cavity-containing protein revealed by high-pressure crystallography. J. Mol. Biol. 367:752-63 (Pubitemid 46330369)
    • (2007) Journal of Molecular Biology , vol.367 , Issue.3 , pp. 752-763
    • Collins, M.D.1    Quillin, M.L.2    Hummer, G.3    Matthews, B.W.4    Gruner, S.M.5
  • 11
    • 33646490977 scopus 로고    scopus 로고
    • High pressure macromolecular crystallography: The 140-MPa crystal structure at 2.3 A resolution of urate oxidase, a 135-kDa tetrameric assembly
    • Colloc'h N, Girard E, Dhaussy AC, Kahn R, Ascone I, et al. 2006. High pressure macromolecular crystallography: the 140-MPa crystal structure at 2.3 A resolution of urate oxidase, a 135-kDa tetrameric assembly. Biochim. Biophys. Acta 1764:391-97
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 391-397
    • Colloc'H, N.1    Girard, E.2    Dhaussy, A.C.3    Kahn, R.4    Ascone, I.5
  • 13
    • 48349141173 scopus 로고    scopus 로고
    • Oxygen pressurized X-ray crystallography: Probing the dioxygen binding site in cofactorless urate oxidase and implications for its catalytic mechanism
    • Colloc'h N, Gabison L, Monard G, Altarsha M, Chiadmi M, et al. 2008. Oxygen pressurized X-ray crystallography: probing the dioxygen binding site in cofactorless urate oxidase and implications for its catalytic mechanism. Biophys. J. 95:2415-22
    • (2008) Biophys. J. , vol.95 , pp. 2415-2422
    • Colloc'H, N.1    Gabison, L.2    Monard, G.3    Altarsha, M.4    Chiadmi, M.5
  • 14
    • 34347326224 scopus 로고    scopus 로고
    • Allosteric mechanisms in cytochrome P450 3A4 studied by high-pressure spectroscopy: Pivotal role of substrate-induced changes in the accessibility and degree of hydration of the heme pocket
    • DOI 10.1021/bi602400y
    • Davydov DR, Baas BJ, Sligar SG, Halpert JR. 2007. Allosteric mechanisms in cytochrome P450 3A4 studied by high-pressure spectroscopy: pivotal role of substrate-induced changes in the accessibility and degree of hydration of the heme pocket. Biochemistry 46:7852-64 (Pubitemid 47016068)
    • (2007) Biochemistry , vol.46 , Issue.26 , pp. 7852-7864
    • Davydov, D.R.1    Baas, B.J.2    Sligar, S.G.3    Halpert, J.R.4
  • 15
    • 39749155117 scopus 로고    scopus 로고
    • Water penetration in the low and high pressure native states of ubiquitin
    • DOI 10.1002/prot.21562
    • Day R, Garcia AE. 2008. Water penetration in the low and high pressure native states of ubiquitin. Proteins 70:1175-84 (Pubitemid 351304078)
    • (2008) Proteins: Structure, Function and Genetics , vol.70 , Issue.4 , pp. 1175-1184
    • Day, R.1    Garcia, A.E.2
  • 16
    • 67650319011 scopus 로고    scopus 로고
    • Advances in high-pressure biophysics: Status and prospects of macromolecular crystallography
    • Fourme R, Girard E, Kahn R, Dhaussy AC, Ascone I. 2009. Advances in high-pressure biophysics: status and prospects of macromolecular crystallography. Annu. Rev. Biophys. 38:153-71
    • (2009) Annu. Rev. Biophys. , vol.38 , pp. 153-171
    • Fourme, R.1    Girard, E.2    Kahn, R.3    Dhaussy, A.C.4    Ascone, I.5
  • 18
    • 0033695467 scopus 로고    scopus 로고
    • Energy landscape and fluctuations in proteins
    • Frauenfelder H, McMahon BH. 2000. Energy landscape and fluctuations in proteins. Ann. Phys. 9:665-67
    • (2000) Ann. Phys. , vol.9 , pp. 665-667
    • Frauenfelder, H.1    McMahon, B.H.2
  • 19
    • 77956639145 scopus 로고    scopus 로고
    • Structure-function perturbation and dissociation of tetrameric urate oxidase by high hydrostatic pressure
    • Girard E, Marchal S, Perez J, Finet S, Kahn R, et al. 2010. Structure-function perturbation and dissociation of tetrameric urate oxidase by high hydrostatic pressure. Biophys. J. 98:2365-73
    • (2010) Biophys. J. , vol.98 , pp. 2365-2373
    • Girard, E.1    Marchal, S.2    Perez, J.3    Finet, S.4    Kahn, R.5
  • 20
    • 68749107059 scopus 로고    scopus 로고
    • Protein sectors: Evolutionary units of three-dimensional structure
    • Halabi N, Rivoire O, Leibler S, Ranganathan R. 2009. Protein sectors: evolutionary units of three-dimensional structure. Cell 138:774-86
    • (2009) Cell , vol.138 , pp. 774-786
    • Halabi, N.1    Rivoire, O.2    Leibler, S.3    Ranganathan, R.4
  • 22
    • 67650325176 scopus 로고    scopus 로고
    • The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: Insights from type II diabetes
    • Hebda JA, Miranker AD. 2009. The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: insights from type II diabetes. Annu. Rev. Biophys. 38:125-52
    • (2009) Annu. Rev. Biophys. , vol.38 , pp. 125-152
    • Hebda, J.A.1    Miranker, A.D.2
  • 23
    • 0020017199 scopus 로고
    • High pressure effects on proteins and other biomolecules
    • Heremans K. 1982. High pressure effects on proteins and other biomolecules. Annu. Rev. Biophys. Bioeng. 11:1-21
    • (1982) Annu. Rev. Biophys. Bioeng. , vol.11 , pp. 1-21
    • Heremans, K.1
  • 26
    • 0035850833 scopus 로고    scopus 로고
    • 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
    • DOI 10.1016/S0014-5793(01)02809-5, PII S0014579301028095
    • Inoue K, Maurer T, Yamada H, Herrmann C, Horn G, et al. 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. 506:180-84 (Pubitemid 32964809)
    • (2001) FEBS Letters , vol.506 , Issue.3 , pp. 180-184
    • Inoue, K.1    Maurer, T.2    Yamada, H.3    Herrmann, C.4    Horn, G.5    Kalbitzer, H.R.6    Akasaka, K.7
  • 31
    • 34247524718 scopus 로고    scopus 로고
    • High-pressure cryocooling for capillary sample cryoprotection and diffraction phasing at long wavelengths
    • DOI 10.1107/S0907444907011924, PII S0907444907011924, sx5068
    • Kim CU, Hao Q, Gruner SM. 2007. High-pressure cryocooling for capillary sample cryoprotection and diffraction phasing at long wavelengths. Acta Crystallogr. D 63:653-59 (Pubitemid 46661537)
    • (2007) Acta Crystallographica Section D: Biological Crystallography , vol.63 , Issue.5 , pp. 653-659
    • Kim, C.U.1    Hao, Q.2    Gruner, S.M.3
  • 33
    • 63849244643 scopus 로고    scopus 로고
    • Evidence for liquid water during the high-density to low-density amorphous ice transition
    • Kim CU, Barstow B, Tate MW, Gruner SM. 2009. Evidence for liquid water during the high-density to low-density amorphous ice transition. Proc. Natl. Acad. Sci. USA 106:4596-600
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 4596-600
    • Kim, C.U.1    Barstow, B.2    Tate, M.W.3    Gruner, S.M.4
  • 34
    • 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. 2000. High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase. Biochemistry 39:12789-95
    • (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
  • 35
    • 0035856546 scopus 로고    scopus 로고
    • Two folded conformers of ubiquitin revealed by high-pressure NMR
    • DOI 10.1021/bi010922u
    • Kitahara R, Yamada H, Akasaka K. 2001. Two folded conformers of ubiquitin revealed by high-pressure NMR. Biochemistry 40:13556-63 (Pubitemid 33130783)
    • (2001) Biochemistry , vol.40 , Issue.45 , pp. 13556-13563
    • Kitahara, R.1    Yamada, H.2    Akasaka, K.3
  • 36
    • 14644424521 scopus 로고    scopus 로고
    • NMR snapshots of a fluctuating protein structure: Ubiquitin at 30 bar-3 kbar
    • DOI 10.1016/j.jmb.2005.01.052
    • Kitahara R, Yokoyama S, Akasaka K. 2005. NMR snapshots of a fluctuating protein structure: ubiquitin at 30 bar-3 kbar. J. Mol. Biol. 347:277-85 (Pubitemid 40312458)
    • (2005) Journal of Molecular Biology , vol.347 , Issue.2 , pp. 277-285
    • Kitahara, R.1    Yokoyama, S.2    Akasaka, K.3
  • 37
    • 0022769706 scopus 로고
    • Collection and processing of X-ray diffraction data from protein crystals at high pressure
    • Kundrot CE, Richards FM. 1986. Collection and processing of X-ray diffraction data from protein crystals at high pressure. J. Appl. Crystallogr. 19:208-13
    • (1986) J. Appl. Crystallogr. , vol.19 , pp. 208-213
    • Kundrot, C.E.1    Richards, F.M.2
  • 38
    • 0023644307 scopus 로고
    • Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres
    • Kundrot CE, Richards FM. 1987. Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres. J. Mol. Biol. 193:157-70
    • (1987) J. Mol. Biol. , vol.193 , pp. 157-170
    • Kundrot, C.E.1    Richards, F.M.2
  • 39
    • 0035793220 scopus 로고    scopus 로고
    • High pressure NMR reveals a variety of fluctuating conformers in β-lactoglobulin
    • DOI 10.1006/jmbi.2000.4350
    • Kuwata K, Li H, Yamada H, Batt CA, Goto Y, Akasaka K. 2001. High pressure NMR reveals a variety of fluctuating conformers in beta-lactoglobulin. J. Mol. Biol. 305:1073-83 (Pubitemid 33027744)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.5 , pp. 1073-1083
    • Kuwata, K.1    Li, H.2    Yamada, H.3    Batt, C.A.4    Goto, Y.5    Akasaka, K.6
  • 40
    • 0037171143 scopus 로고    scopus 로고
    • Experiments on ion channels at high pressure
    • Macdonald AG. 2002. Experiments on ion channels at high pressure. Biochim. Biophys. Acta 1595:387-89
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 387-389
    • MacDonald, A.G.1
  • 41
    • 0030670857 scopus 로고    scopus 로고
    • + channel N- and C-type inactivation
    • DOI 10.1007/s002490050098
    • Meyer R, Heinemann SH. 1997. Temperature and pressure dependence of Shaker K+ channel N- and C-type inactivation. Eur. Biophys. J. 26:433-45 (Pubitemid 27509260)
    • (1997) European Biophysics Journal , vol.26 , Issue.6 , pp. 433-445
    • Meyer, R.1    Heinemann, S.H.2
  • 42
    • 11244296117 scopus 로고    scopus 로고
    • Solution structure of the active-centre mutant I14A of the histidine-containing phosphocarrier protein from Staphylococcus carnosus
    • DOI 10.1111/j.1432-1033.2004.04447.x
    • Moglich A, Koch B, Gronwald W, Hengstenberg W, Brunner E, Kalbitzer HR. 2004. Solution structure of the active-centre mutant I14A of the histidine-containing phosphocarrier protein from Staphylococcus carnosus. Eur. J. Biochem. 271:4815-24 (Pubitemid 40065584)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.23-24 , pp. 4815-4824
    • Moglich, A.1    Koch, B.2    Gronwald, W.3    Hengstenberg, W.4    Brunner, E.5    Kalbitzer, H.R.6
  • 44
    • 16344381007 scopus 로고    scopus 로고
    • Pressure denaturation of staphylococcal nuclease studied by neutron small-angle scattering and molecular simulation
    • DOI 10.1529/biophysj.104.050526
    • Paliwal A, Asthagiri D, Bossev DP, Paulaitis ME. 2004. Pressure denaturation of staphylococcal nuclease studied by neutron small-angle scattering and molecular simulation. Biophys. J. 87:3479-92 (Pubitemid 40468601)
    • (2004) Biophysical Journal , vol.87 , Issue.5 , pp. 3479-3492
    • Paliwal, A.1    Asthagiri, D.2    Bossev, D.P.3    Paulaitis, M.E.4
  • 45
    • 0032536156 scopus 로고    scopus 로고
    • 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
    • DOI 10.1006/jmbi.1997.1454
    • Panick G, Malessa R, Winter R, Rapp G, Frye KJ, Royer CA. 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 (Pubitemid 28030012)
    • (1998) Journal of Molecular Biology , vol.275 , Issue.2 , pp. 389-402
    • Panick, G.1    Malessa, R.2    Winter, R.3    Rapp, G.4    Frye, K.J.5    Royer, C.A.6
  • 46
    • 67651148171 scopus 로고    scopus 로고
    • Parallel pathways and free-energy landscapes for enzymatic hydride transfer probed by hydrostatic pressure
    • Pudney CR, McGrory T, Lafite P, Pang J, Hay S,et al. 2009. Parallel pathways and free-energy landscapes for enzymatic hydride transfer probed by hydrostatic pressure. Chembiochem 10:1379-84
    • (2009) Chembiochem , vol.10 , pp. 1379-1384
    • Pudney, C.R.1    McGrory, T.2    Lafite, P.3    Pang, J.4    Hay, S.5
  • 47
    • 0023051843 scopus 로고
    • Internal cavities and buried waters in globular proteins
    • Rashin AA, Iofin M, Honig B. 1986. Internal cavities and buried waters in globular proteins. Biochemistry 25:3619-25
    • (1986) Biochemistry , vol.25 , pp. 3619-3625
    • Rashin, A.A.1    Iofin, M.2    Honig, B.3
  • 48
    • 0344406172 scopus 로고    scopus 로고
    • Pressure-dependent changes in the solution structure of hen egg-white lysozyme
    • DOI 10.1016/S0022-2836(03)00209-2
    • Refaee M, Tezuka T, Akasaka K, Williamson MP. 2003. Pressure-dependent changes in the solution structure of hen egg-white lysozyme. J. Mol. Biol. 327:857-65 (Pubitemid 36315924)
    • (2003) Journal of Molecular Biology , vol.327 , Issue.4 , pp. 857-865
    • Refaee, M.1    Tezuka, T.2    Akasaka, K.3    Williamson, M.P.4
  • 49
    • 0016616012 scopus 로고
    • High pressure effects on the activity of glycolytic enzymes
    • Schmid G, Ludemann HD, Jaenicke R. 1975. High pressure effects on the activity of glycolytic enzymes. Biophys. Chem. 3:90-98
    • (1975) Biophys. Chem. , vol.3 , pp. 90-98
    • Schmid, G.1    Ludemann, H.D.2    Jaenicke, R.3
  • 50
    • 0026583113 scopus 로고
    • Adaptations to high hydrostatic pressure
    • Somero GN. 1992. Adaptations to high hydrostatic pressure. Annu. Rev. Physiol. 54:557-77
    • (1992) Annu. Rev. Physiol. , vol.54 , pp. 557-577
    • Somero, G.N.1
  • 52
    • 0028021650 scopus 로고
    • High-pressure flash photolysis study of hemoprotein: Effects of substrate analogues on the recombination of carbon monoxide to cytochrome P450(CAM)
    • Unno M, Ishimori K, Ishimura Y, Morishima I. 1994. High-pressure flash photolysis study of hemopro-tein: effects of substrate analogues on the recombination of carbon monoxide to cytochrome P450CAM. Biochemistry 33:9762-68 (Pubitemid 24272937)
    • (1994) Biochemistry , vol.33 , Issue.32 , pp. 9762-9768
    • Unno, M.1    Ishimori, K.2    Ishimura, Y.3    Morishima, I.4
  • 53
    • 0036154017 scopus 로고    scopus 로고
    • Probing substates in sperm whale myoglobin using high-pressure crystallography
    • DOI 10.1016/S0969-2126(01)00699-2, PII S0969212601006992
    • Urayama P, Phillips GN, Gruner SM. 2002. Probing substates in sperm whale myoglobin using high-pressure crystallography. Structure 10:51-60 (Pubitemid 34112610)
    • (2002) Structure , vol.10 , Issue.1 , pp. 51-60
    • Urayama, P.1    Phillips Jr., G.N.2    Gruner, S.M.3
  • 54
    • 0029117029 scopus 로고
    • Effects of hydrostatic pressure on the kinetics reveal a volume increase during the bacteriorhodopsin photocycle
    • Varo G, Lanyi JK. 1995. Effects of hydrostatic pressure on the kinetics reveal a volume increase during the bacteriorhodopsin photocycle. Biochemistry 34:12161-69
    • (1995) Biochemistry , vol.34 , pp. 12161-12169
    • Varo, G.1    Lanyi, J.K.2
  • 55
    • 0028095182 scopus 로고
    • Buried waters and internal cavities in monomeric proteins
    • Williams MA, Goodfellow JM, Thornton JM. 1994. Buried waters and internal cavities in monomeric proteins. Protein Sci. 3:1224-35 (Pubitemid 24278203)
    • (1994) Protein Science , vol.3 , Issue.8 , pp. 1224-1235
    • Williams, M.A.1    Goodfellow, J.M.2    Thornton, J.M.3
  • 56
    • 0042511922 scopus 로고    scopus 로고
    • The solution structure of bovine pancreatic trypsin inhibitor at high pressure
    • DOI 10.1110/ps.0242103
    • Williamson MP, Akasaka K, Refaee M. 2003. The solution structure of bovine pancreatic trypsin inhibitor at high pressure. Protein Sci. 12:1971-79 (Pubitemid 37022819)
    • (2003) Protein Science , vol.12 , Issue.9 , pp. 1971-1979
    • Williamson, M.P.1    Akasaka, K.2    Refaee, M.3
  • 59
    • 0031893269 scopus 로고    scopus 로고
    • The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect
    • Xu J, Baase WA, Baldwin E, Matthews BW. 1998. The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. Protein Sci. 7:158-77 (Pubitemid 28133757)
    • (1998) Protein Science , vol.7 , Issue.1 , pp. 158-177
    • Xu, J.1    Baase, W.A.2    Baldwin, E.3    Matthews, B.W.4


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