메뉴 건너뛰기




Volumn 110, Issue 49, 2013, Pages

Circular dichroism and site-directed spin labeling reveal structural and dynamical features of high-pressure states of myoglobin

Author keywords

[No Author keywords available]

Indexed keywords

APOMYOGLOBIN; HOLOMYOGLOBIN; MYOGLOBIN; UNCLASSIFIED DRUG;

EID: 84889671229     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1320124110     Document Type: Article
Times cited : (45)

References (79)
  • 1
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • Henzler-Wildman K, Kern D (2007) Dynamic personalities of proteins. Nature 450(7172):964-972
    • (2007) Nature , vol.450 , Issue.7172 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 2
    • 70350348011 scopus 로고    scopus 로고
    • NMR spectroscopy brings invisible protein states into focus
    • Baldwin AJ, Kay LE (2009) NMR spectroscopy brings invisible protein states into focus. Nat Chem Biol 5(11):808-814
    • (2009) Nat Chem Biol , vol.5 , Issue.11 , pp. 808-814
    • Baldwin, A.J.1    Kay, L.E.2
  • 3
    • 0026723063 scopus 로고
    • Protein folding funnels: A kinetic approach to the sequence-structure relationship
    • Leopold PE, Montal M, Onuchic JN (1992) Protein folding funnels: A kinetic approach to the sequence-structure relationship. Proc Natl Acad Sci USA 89(18):8721-8725
    • (1992) Proc Natl Acad Sci USA , vol.89 , Issue.18 , pp. 8721-8725
    • Leopold, P.E.1    Montal, M.2    Onuchic, J.N.3
  • 5
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • Boehr DD, Nussinov R, Wright PE (2009) The role of dynamic conformational ensembles in biomolecular recognition. Nat Chem Biol 5(11):789-796
    • (2009) Nat Chem Biol , vol.5 , Issue.11 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 6
    • 0036147568 scopus 로고    scopus 로고
    • Multiple diverse ligands binding at a single protein site: A matter of pre-existing populations
    • Ma B, Shatsky M, Wolfson HJ, Nussinov R (2002) Multiple diverse ligands binding at a single protein site: A matter of pre-existing populations. Protein Sci 11(2):184-197
    • (2002) Protein Sci , vol.11 , Issue.2 , pp. 184-197
    • Ma, B.1    Shatsky, M.2    Wolfson, H.J.3    Nussinov, R.4
  • 7
    • 80052401629 scopus 로고    scopus 로고
    • Solution structure of a minor and transiently formed state of a T4 lysozyme mutant
    • Bouvignies G, et al. (2011) Solution structure of a minor and transiently formed state of a T4 lysozyme mutant. Nature 477(7362):111-114
    • (2011) Nature , vol.477 , Issue.7362 , pp. 111-114
    • Bouvignies, G.1
  • 8
    • 77649266958 scopus 로고    scopus 로고
    • Capillarity theory for the fly-casting mechanism
    • Trizac E, Levy Y, Wolynes PG (2010) Capillarity theory for the fly-casting mechanism. Proc Natl Acad Sci USA 107(7):2746-2750
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.7 , pp. 2746-2750
    • Trizac, E.1    Levy, Y.2    Wolynes, P.G.3
  • 9
    • 84867743873 scopus 로고    scopus 로고
    • High-pressure macromolecular crystallography and NMR: Status, achievements and prospects
    • Fourme R, Girard E, Akasaka K (2012) High-pressure macromolecular crystallography and NMR: Status, achievements and prospects. Curr Opin Struct Biol 22(5):636-642
    • (2012) Curr Opin Struct Biol , vol.22 , Issue.5 , pp. 636-642
    • Fourme, R.1    Girard, E.2    Akasaka, K.3
  • 10
    • 0034711091 scopus 로고    scopus 로고
    • High pressure NMR reveals active-site hinge motion of folatebound Escherichia coli dihydrofolate reductase
    • Kitahara R, et al. (2000) High pressure NMR reveals active-site hinge motion of folatebound Escherichia coli dihydrofolate reductase. Biochemistry 39(42):12789-12795
    • (2000) Biochemistry , vol.39 , Issue.42 , pp. 12789-12795
    • Kitahara, R.1
  • 11
    • 14644424521 scopus 로고    scopus 로고
    • NMR snapshots of a fluctuating protein structure: Ubiquitin at 30 bar-3 kbar
    • Kitahara R, Yokoyama S, Akasaka K (2005) NMR snapshots of a fluctuating protein structure: Ubiquitin at 30 bar-3 kbar. J Mol Biol 347(2):277-285
    • (2005) J Mol Biol , vol.347 , Issue.2 , pp. 277-285
    • Kitahara, R.1    Yokoyama, S.2    Akasaka, K.3
  • 12
    • 77956639145 scopus 로고    scopus 로고
    • Structure-function perturbation and dissociation of tetrameric urate oxidase by high hydrostatic pressure
    • Girard E, et al. (2010) Structure-function perturbation and dissociation of tetrameric urate oxidase by high hydrostatic pressure. Biophys J 98(10):2365-2373
    • (2010) Biophys J , vol.98 , Issue.10 , pp. 2365-2373
    • Girard, E.1
  • 13
    • 84884638449 scopus 로고    scopus 로고
    • Volumetric properties underlying ligand binding in a monomeric hemoglobin: A high-pressure NMR study
    • Dellarole M, Roumestand C, Royer C, Lecomte JT (2013) Volumetric properties underlying ligand binding in a monomeric hemoglobin: A high-pressure NMR study. Biochim Biophys Acta 1834(9):1910-1922
    • (2013) Biochim Biophys Acta , vol.1834 , Issue.9 , pp. 1910-1922
    • Dellarole, M.1    Roumestand, C.2    Royer, C.3    Lecomte, J.T.4
  • 14
    • 84856005311 scopus 로고    scopus 로고
    • Revealing conformational substates of lipidated N-Ras protein by pressure modulation
    • Kapoor S, et al. (2012) Revealing conformational substates of lipidated N-Ras protein by pressure modulation. Proc Natl Acad Sci USA 109(2):460-465
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.2 , pp. 460-465
    • Kapoor, S.1
  • 15
    • 84876518318 scopus 로고    scopus 로고
    • Exploring the folding energy landscape with pressure
    • Akasaka K, Kitahara R, Kamatari YO (2013) Exploring the folding energy landscape with pressure. Arch Biochem Biophys 531(1-2):110-115
    • (2013) Arch Biochem Biophys , vol.531 , Issue.1-2 , pp. 110-115
    • Akasaka, K.1    Kitahara, R.2    Kamatari, Y.O.3
  • 16
    • 71149088976 scopus 로고    scopus 로고
    • Resolving conformational and rotameric exchange in spin-labeled proteins using saturation recovery EPR
    • Bridges MD, Hideg K, Hubbell WL (2010) Resolving conformational and rotameric exchange in spin-labeled proteins using saturation recovery EPR. Appl Magn Reson 37(1-4):363
    • (2010) Appl Magn Reson , vol.37 , Issue.1-4 , pp. 363
    • Bridges, M.D.1    Hideg, K.2    Hubbell, W.L.3
  • 17
    • 67749124074 scopus 로고    scopus 로고
    • Osmolyte perturbation reveals conformational equilibria in spin-labeled proteins
    • López CJ, Fleissner MR, Guo Z, Kusnetzow AK, HubbellWL (2009) Osmolyte perturbation reveals conformational equilibria in spin-labeled proteins. Protein Sci 18(8):1637-1652
    • (2009) Protein Sci , vol.18 , Issue.8 , pp. 1637-1652
    • López, C.J.1    Fleissner, M.R.2    Guo, Z.3    Kusnetzow, A.K.4    Hubbell, W.L.5
  • 18
    • 84865410842 scopus 로고    scopus 로고
    • Mapping molecular flexibility of proteins with site-directed spin labeling: A case study of myoglobin
    • López CJ, Oga S, Hubbell WL (2012) Mapping molecular flexibility of proteins with site-directed spin labeling: A case study of myoglobin. Biochemistry 51(33):6568-6583
    • (2012) Biochemistry , vol.51 , Issue.33 , pp. 6568-6583
    • López, C.J.1    Oga, S.2    Hubbell, W.L.3
  • 19
    • 0024974071 scopus 로고
    • Structural studies on transmembrane proteins. 2. Spin labeling of bacteriorhodopsin mutants at unique cysteines
    • Altenbach C, Flitsch SL, Khorana HG, Hubbell WL (1989) Structural studies on transmembrane proteins. 2. Spin labeling of bacteriorhodopsin mutants at unique cysteines. Biochemistry 28(19):7806-7812
    • (1989) Biochemistry , vol.28 , Issue.19 , pp. 7806-7812
    • Altenbach, C.1    Flitsch, S.L.2    Khorana, H.G.3    Hubbell, W.L.4
  • 20
    • 84885863331 scopus 로고    scopus 로고
    • Technological advances in sitedirected spin labeling of proteins
    • Hubbell WL, López CJ, Altenbach C, Yang Z (2013) Technological advances in sitedirected spin labeling of proteins. Curr Opin Struct Biol 23(5):725-733
    • (2013) Curr Opin Struct Biol , vol.23 , Issue.5 , pp. 725-733
    • Hubbell, W.L.1    López, C.J.2    Altenbach, C.3    Yang, Z.4
  • 21
    • 34249794011 scopus 로고    scopus 로고
    • Structural determinants of nitroxide motion in spin-labeled proteins: Tertiary contact and solvent-inaccessible sites in helix G of T4 lysozyme
    • Guo Z, Cascio D, Hideg K, Kálái T, Hubbell WL (2007) Structural determinants of nitroxide motion in spin-labeled proteins: Tertiary contact and solvent-inaccessible sites in helix G of T4 lysozyme. Protein Sci 16(6):1069-1086
    • (2007) Protein Sci , vol.16 , Issue.6 , pp. 1069-1086
    • Guo, Z.1    Cascio, D.2    Hideg, K.3    Kálái, T.4    Hubbell, W.L.5
  • 22
    • 0029905422 scopus 로고    scopus 로고
    • Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics
    • Mchaourab HS, Lietzow MA, Hideg K, Hubbell WL (1996) Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics. Biochemistry 35(24):7692-7704
    • (1996) Biochemistry , vol.35 , Issue.24 , pp. 7692-7704
    • McHaourab, H.S.1    Lietzow, M.A.2    Hideg, K.3    Hubbell, W.L.4
  • 23
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • Hubbell WL, Cafiso DS, Altenbach C (2000) Identifying conformational changes with site-directed spin labeling. Nat Struct Biol 7(9):735-739
    • (2000) Nat Struct Biol , vol.7 , Issue.9 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 25
    • 2942527068 scopus 로고    scopus 로고
    • Mapping backbone dynamics in solution with sitedirected spin labeling: GCN4-58 bZip free and bound to DNA
    • Columbus L, Hubbell WL (2004) Mapping backbone dynamics in solution with sitedirected spin labeling: GCN4-58 bZip free and bound to DNA. Biochemistry 43(23): 7273-7287
    • (2004) Biochemistry , vol.43 , Issue.23 , pp. 7273-7287
    • Columbus, L.1    Hubbell, W.L.2
  • 26
    • 79952144525 scopus 로고    scopus 로고
    • High-pressure EPR reveals conformational equilibria and volumetric properties of spin-labeled proteins
    • McCoy J, Hubbell WL (2011) High-pressure EPR reveals conformational equilibria and volumetric properties of spin-labeled proteins. Proc Natl Acad Sci USA 108(4): 1331-1336
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.4 , pp. 1331-1336
    • McCoy, J.1    Hubbell, W.L.2
  • 27
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N, Woody RW (2000) Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal Biochem 287(2):252-260
    • (2000) Anal Biochem , vol.287 , Issue.2 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 29
    • 33646900712 scopus 로고    scopus 로고
    • Probing conformational fluctuation of proteins by pressure perturbation
    • Akasaka K (2006) Probing conformational fluctuation of proteins by pressure perturbation. Chem Rev 106(5):1814-1835
    • (2006) Chem Rev , vol.106 , Issue.5 , pp. 1814-1835
    • Akasaka, K.1
  • 30
    • 0017195182 scopus 로고
    • A high-pressure sample cell for circular dichroism studies
    • Harris RD, Jacobs M, Long MM, Urry DW (1976) A high-pressure sample cell for circular dichroism studies. Anal Biochem 73(2):363-368
    • (1976) Anal Biochem , vol.73 , Issue.2 , pp. 363-368
    • Harris, R.D.1    Jacobs, M.2    Long, M.M.3    Urry, D.W.4
  • 31
    • 79955059819 scopus 로고    scopus 로고
    • Characterization of monomeric substates of ascorbate oxidase
    • Di Venere A, et al. (2011) Characterization of monomeric substates of ascorbate oxidase. FEBS J 278(9):1585-1593
    • (2011) FEBS J , vol.278 , Issue.9 , pp. 1585-1593
    • Di Venere, A.1
  • 32
    • 77954459632 scopus 로고    scopus 로고
    • Refolding of the recombinant protein OmpA70 from Leptospira interrogans from inclusion bodies using high hydrostatic pressure and partial characterization of its immunological properties
    • Fraga TR, et al. (2010) Refolding of the recombinant protein OmpA70 from Leptospira interrogans from inclusion bodies using high hydrostatic pressure and partial characterization of its immunological properties. J Biotechnol 148(2-3):156-162
    • (2010) J Biotechnol , vol.148 , Issue.2-3 , pp. 156-162
    • Fraga, T.R.1
  • 33
    • 41149114074 scopus 로고    scopus 로고
    • The proapoptotic protein Smac/DIABLO dimer has the highest stability as measured by pressure and urea denaturation
    • Gonçalves RB, Sanches D, Souza TL, Silva JL, Oliveira AC (2008) The proapoptotic protein Smac/DIABLO dimer has the highest stability as measured by pressure and urea denaturation. Biochemistry 47(12):3832-3841
    • (2008) Biochemistry , vol.47 , Issue.12 , pp. 3832-3841
    • Gonçalves, R.B.1    Sanches, D.2    Souza, T.L.3    Silva, J.L.4    Oliveira, A.C.5
  • 34
    • 33645456647 scopus 로고    scopus 로고
    • Structural changes of microbial transglutaminase during thermal and high-pressure treatment
    • Menéndez O, Rawel H, Schwarzenbolz U, Henle T (2006) Structural changes of microbial transglutaminase during thermal and high-pressure treatment. J Agric Food Chem 54(5):1716-1721
    • (2006) J Agric Food Chem , vol.54 , Issue.5 , pp. 1716-1721
    • Menéndez, O.1    Rawel, H.2    Schwarzenbolz, U.3    Henle, T.4
  • 35
    • 0034850884 scopus 로고    scopus 로고
    • Pressure-induced denaturation of monomer beta-lactoglobulin is partially irreversible: Comparison of monomer form (highly acidic pH) with dimmer form (neutral pH)
    • Ikeuchi Y, et al. (2001) Pressure-induced denaturation of monomer beta-lactoglobulin is partially irreversible: Comparison of monomer form (highly acidic pH) with dimmer form (neutral pH). J Agric Food Chem 49(8):4052-4059
    • (2001) J Agric Food Chem , vol.49 , Issue.8 , pp. 4052-4059
    • Ikeuchi, Y.1
  • 37
    • 84873526289 scopus 로고    scopus 로고
    • Molten globules, entropy-driven conformational change and protein folding
    • Baldwin RL, Rose GD (2013) Molten globules, entropy-driven conformational change and protein folding. Curr Opin Struct Biol 23(1):4-10
    • (2013) Curr Opin Struct Biol , vol.23 , Issue.1 , pp. 4-10
    • Baldwin, R.L.1    Rose, G.D.2
  • 38
    • 0025212107 scopus 로고
    • Evidence for amolten globule state as a general intermediate in protein folding
    • Ptitsyn OB, Pain RH, Semisotnov GV, Zerovnik E, Razgulyaev OI (1990) Evidence for amolten globule state as a general intermediate in protein folding. FEBS Lett 262(1):20-24
    • (1990) FEBS Lett , vol.262 , Issue.1 , pp. 20-24
    • Ptitsyn, O.B.1    Pain, R.H.2    Semisotnov, G.V.3    Zerovnik, E.4    Razgulyaev, O.I.5
  • 39
    • 79959326174 scopus 로고    scopus 로고
    • Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion
    • Meinhold DW, Wright PE (2011) Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion. Proc Natl Acad Sci USA 108(22):9078-9083
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.22 , pp. 9078-9083
    • Meinhold, D.W.1    Wright, P.E.2
  • 40
  • 41
    • 0030726758 scopus 로고    scopus 로고
    • Populating the equilibrium molten globule state of apomyoglobin under conditions suitable for structural characterization by NMR
    • Eliezer D, Jennings PA, Dyson HJ, Wright PE (1997) Populating the equilibrium molten globule state of apomyoglobin under conditions suitable for structural characterization by NMR. FEBS Lett 417(1):92-96
    • (1997) FEBS Lett , vol.417 , Issue.1 , pp. 92-96
    • Eliezer, D.1    Jennings, P.A.2    Dyson, H.J.3    Wright, P.E.4
  • 42
    • 0031932824 scopus 로고    scopus 로고
    • Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding
    • Eliezer D, Yao J, Dyson HJ, Wright PE (1998) Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. Nat Struct Biol 5(2):148-155
    • (1998) Nat Struct Biol , vol.5 , Issue.2 , pp. 148-155
    • Eliezer, D.1    Yao, J.2    Dyson, H.J.3    Wright, P.E.4
  • 43
    • 52949091532 scopus 로고    scopus 로고
    • Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H/D exchange coupled with 2D NMR
    • Uzawa T, et al. (2008) Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H/D exchange coupled with 2D NMR. Proc Natl Acad Sci USA 105(37): 13859-13864
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.37 , pp. 13859-13864
    • Uzawa, T.1
  • 44
    • 0031837399 scopus 로고    scopus 로고
    • Determination of the volume changes for pressureinduced transitions of apomyoglobin between the native, molten globule, and unfolded states
    • Vidugiris GJ, Royer CA (1998) Determination of the volume changes for pressureinduced transitions of apomyoglobin between the native, molten globule, and unfolded states. Biophys J 75(1):463-470
    • (1998) Biophys J , vol.75 , Issue.1 , pp. 463-470
    • Vidugiris, G.J.1    Royer, C.A.2
  • 45
    • 0030048876 scopus 로고    scopus 로고
    • Pressure-induced perturbation of apomyoglobin structure: Fluorescence studies on native and acidic compact forms
    • Bismuto E, Sirangelo I, Irace G, Gratton E (1996) Pressure-induced perturbation of apomyoglobin structure: Fluorescence studies on native and acidic compact forms. Protein Sci, 35(4):1173-1178
    • (1996) Protein Sci , vol.35 , Issue.4 , pp. 1173-1178
    • Bismuto, E.1    Sirangelo, I.2    Irace, G.3    Gratton, E.4
  • 46
    • 0030048876 scopus 로고    scopus 로고
    • Pressure-induced perturbation of apomyoglobin structure: Fluorescence studies on native and acidic compact forms
    • Bismuto E, Sirangelo I, Irace G, Gratton E (1996) Pressure-induced perturbation of apomyoglobin structure: Fluorescence studies on native and acidic compact forms. Biochemistry 35(4):1173-1178
    • (1996) Biochemistry , vol.35 , Issue.4 , pp. 1173-1178
    • Bismuto, E.1    Sirangelo, I.2    Irace, G.3    Gratton, E.4
  • 47
    • 0034647650 scopus 로고    scopus 로고
    • High-pressure denaturation of apomyoglobin
    • Bondos SE, Sligar S, Jonas J (2000) High-pressure denaturation of apomyoglobin. Biochim Biophys Acta 1480(1-2):353-364
    • (2000) Biochim Biophys Acta , vol.1480 , Issue.1-2 , pp. 353-364
    • Bondos, S.E.1    Sligar, S.2    Jonas, J.3
  • 48
    • 0036291143 scopus 로고    scopus 로고
    • High pressure NMR reveals that apomyoglobin is an equilibrium mixture from the native to the unfolded
    • Kitahara R, Yamada H, Akasaka K, Wright PE (2002) High pressure NMR reveals that apomyoglobin is an equilibrium mixture from the native to the unfolded. J Mol Biol 320(2):311-319
    • (2002) J Mol Biol , vol.320 , Issue.2 , pp. 311-319
    • Kitahara, R.1    Yamada, H.2    Akasaka, K.3    Wright, P.E.4
  • 49
    • 0034601786 scopus 로고    scopus 로고
    • Pressure effect on the conformational fluctuation of apomyoglobin in the native state
    • Tanaka N, et al. (2000) Pressure effect on the conformational fluctuation of apomyoglobin in the native state. Biochemistry 39(39):12063-12068
    • (2000) Biochemistry , vol.39 , Issue.39 , pp. 12063-12068
    • Tanaka, N.1
  • 50
    • 0015820466 scopus 로고
    • Pressure denaturation of metmyoglobin
    • Zipp A, Kauzmann W (1973) Pressure denaturation of metmyoglobin. Biochemistry 12(21):4217-4228
    • (1973) Biochemistry , vol.12 , Issue.21 , pp. 4217-4228
    • Zipp, A.1    Kauzmann, W.2
  • 51
    • 0030575785 scopus 로고    scopus 로고
    • Is apomyoglobin a molten globule? Structural characterization by NMR
    • Eliezer D, Wright PE (1996) Is apomyoglobin a molten globule? Structural characterization by NMR. J Mol Biol 263(4):531-538
    • (1996) J Mol Biol , vol.263 , Issue.4 , pp. 531-538
    • Eliezer, D.1    Wright, P.E.2
  • 52
    • 0025186451 scopus 로고
    • Structural characterization of a partly folded apomyoglobin intermediate
    • Hughson FM, Wright PE, Baldwin RL (1990) Structural characterization of a partly folded apomyoglobin intermediate. Science 249(4976):1544-1548
    • (1990) Science , vol.249 , Issue.4976 , pp. 1544-1548
    • Hughson, F.M.1    Wright, P.E.2    Baldwin, R.L.3
  • 53
    • 0029986887 scopus 로고    scopus 로고
    • Crystal structures of CO-, deoxy- and met-myoglobins at various pH values
    • Yang F, Phillips GN, Jr. (1996) Crystal structures of CO-, deoxy- and met-myoglobins at various pH values. J Mol Biol 256(4):762-774
    • (1996) J Mol Biol , vol.256 , Issue.4 , pp. 762-774
    • Yang, F.1    Phillips, Jr.G.N.2
  • 54
    • 0028243107 scopus 로고
    • Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding
    • Nishii I, Kataoka M, Tokunaga F, Goto Y (1994) Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding. Biochemistry 33(16): 4903-4909
    • (1994) Biochemistry , vol.33 , Issue.16 , pp. 4903-4909
    • Nishii, I.1    Kataoka, M.2    Tokunaga, F.3    Goto, Y.4
  • 55
    • 0035799354 scopus 로고    scopus 로고
    • Molecular motion of spin labeled side chains in alpha-helices: Analysis by variation of side chain structure
    • Columbus L, Kálai T, Jekö J, Hideg K, Hubbell WL (2001) Molecular motion of spin labeled side chains in alpha-helices: Analysis by variation of side chain structure. Biochemistry 40(13):3828-3846
    • (2001) Biochemistry , vol.40 , Issue.13 , pp. 3828-3846
    • Columbus, L.1    Kálai, T.2    Jekö, J.3    Hideg, K.4    Hubbell, W.L.5
  • 56
    • 0023652260 scopus 로고
    • Thermal expansion of a protein
    • Frauenfelder H, et al. (1987) Thermal expansion of a protein. Biochemistry 26(1): 254-261
    • (1987) Biochemistry , vol.26 , Issue.1 , pp. 254-261
    • Frauenfelder, H.1
  • 57
    • 0030834054 scopus 로고    scopus 로고
    • Pressure effects on the proximal heme pocket in myoglobin probed by Raman and near-infrared absorption spectroscopy
    • Galkin O, Buchter S, Tabirian A, Schulte A (1997) Pressure effects on the proximal heme pocket in myoglobin probed by Raman and near-infrared absorption spectroscopy. Biophys J 73(5):2752-2763
    • (1997) Biophys J , vol.73 , Issue.5 , pp. 2752-2763
    • Galkin, O.1    Buchter, S.2    Tabirian, A.3    Schulte, A.4
  • 58
    • 0036154017 scopus 로고    scopus 로고
    • Probing substates in sperm whale myoglobin using high-pressure crystallography
    • Urayama P, Phillips GN, Jr., Gruner SM (2002) Probing substates in sperm whale myoglobin using high-pressure crystallography. Structure 10(1):51-60
    • (2002) Structure , vol.10 , Issue.1 , pp. 51-60
    • Urayama, P.1    Phillips, Jr.G.N.2    Gruner, S.M.3
  • 59
    • 0028290594 scopus 로고
    • Acid-induced folding of heme proteins
    • Goto Y, Fink AL (1994) Acid-induced folding of heme proteins. Methods Enzymol 232: 3-15
    • (1994) Methods Enzymol , vol.232 , pp. 3-15
    • Goto, Y.1    Fink, A.L.2
  • 60
    • 33751289801 scopus 로고    scopus 로고
    • Assessing induced folding of an intrinsically disordered protein by site-directed spin-labeling electron paramagnetic resonance spectroscopy
    • Morin B, et al. (2006) Assessing induced folding of an intrinsically disordered protein by site-directed spin-labeling electron paramagnetic resonance spectroscopy. J Phys Chem B 110(41):20596-20608
    • (2006) J Phys Chem B , vol.110 , Issue.41 , pp. 20596-20608
    • Morin, B.1
  • 61
    • 58149279796 scopus 로고    scopus 로고
    • Mapping alpha-helical induced folding within the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by site-directed spin-labeling EPR spectroscopy
    • Belle V, et al. (2008) Mapping alpha-helical induced folding within the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by site-directed spin-labeling EPR spectroscopy. Proteins 73(4):973-988
    • (2008) Proteins , vol.73 , Issue.4 , pp. 973-988
    • Belle, V.1
  • 63
    • 0015882223 scopus 로고
    • The equilibrium unfolding parameters of horse and sperm whale myoglobin. Effects of guanidine hydrochloride, urea, and acid
    • Puett D (1973) The equilibrium unfolding parameters of horse and sperm whale myoglobin. Effects of guanidine hydrochloride, urea, and acid. J Biol Chem 248(13): 4623-4634
    • (1973) J Biol Chem , vol.248 , Issue.13 , pp. 4623-4634
    • Puett, D.1
  • 64
    • 34248159499 scopus 로고    scopus 로고
    • Met-myoglobin association in dilute solution during pressureinduced denaturation: An analysis at pH 4.5 by high-pressure small-angle X-ray scattering
    • Spinozzi F, et al. (2007) Met-myoglobin association in dilute solution during pressureinduced denaturation: An analysis at pH 4.5 by high-pressure small-angle X-ray scattering. J Phys Chem B 111(14):3822-3830
    • (2007) J Phys Chem B , vol.111 , Issue.14 , pp. 3822-3830
    • Spinozzi, F.1
  • 65
    • 0029400889 scopus 로고
    • Overexpression of myoglobin and assignment of its amide, C alpha and C beta resonances
    • Jennings PA, Stone MJ, Wright PE (1995) Overexpression of myoglobin and assignment of its amide, C alpha and C beta resonances. J Biomol NMR 6(3):271-276
    • (1995) J Biomol NMR , vol.6 , Issue.3 , pp. 271-276
    • Jennings, P.A.1    Stone, M.J.2    Wright, P.E.3
  • 66
    • 77951596391 scopus 로고    scopus 로고
    • Multifrequency electron spin resonance study of the dynamics of spin labeled T4 lysozyme
    • Zhang Z, et al. (2010) Multifrequency electron spin resonance study of the dynamics of spin labeled T4 lysozyme. J Phys Chem B 114(16):5503-5521
    • (2010) J Phys Chem B , vol.114 , Issue.16 , pp. 5503-5521
    • Zhang, Z.1
  • 68
    • 0027245421 scopus 로고
    • Three-state analysis of sperm whale apomyoglobin folding
    • Barrick D, Baldwin RL (1993) Three-state analysis of sperm whale apomyoglobin folding. Biochemistry 32(14):3790-3796
    • (1993) Biochemistry , vol.32 , Issue.14 , pp. 3790-3796
    • Barrick, D.1    Baldwin, R.L.2
  • 69
    • 0032549072 scopus 로고    scopus 로고
    • Two forms of the pH 4 folding intermediate of apomyoglobin
    • Jamin M, Baldwin RL (1998) Two forms of the pH 4 folding intermediate of apomyoglobin. J Mol Biol 276(2):491-504
    • (1998) J Mol Biol , vol.276 , Issue.2 , pp. 491-504
    • Jamin, M.1    Baldwin, R.L.2
  • 70
    • 84860829715 scopus 로고    scopus 로고
    • Cavities determine the pressure unfolding of proteins
    • Roche J, et al. (2012) Cavities determine the pressure unfolding of proteins. Proc Natl Acad Sci USA 109(18):6945-6950
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.18 , pp. 6945-6950
    • Roche, J.1
  • 71
    • 79955975933 scopus 로고    scopus 로고
    • Cavity hydration as a gateway to unfolding: An NMR study of hen lysozyme at high pressure and low temperature
    • Kamatari YO, Smith LJ, Dobson CM, Akasaka K (2011) Cavity hydration as a gateway to unfolding: An NMR study of hen lysozyme at high pressure and low temperature. Biophys Chem 156(1):24-30
    • (2011) Biophys Chem , vol.156 , Issue.1 , pp. 24-30
    • Kamatari, Y.O.1    Smith, L.J.2    Dobson, C.M.3    Akasaka, K.4
  • 72
    • 0032539604 scopus 로고    scopus 로고
    • The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins
    • Hummer G, Garde S, García AE, Paulaitis ME, Pratt LR (1998) The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins. Proc Natl Acad Sci USA 95(4):1552-1555
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.4 , pp. 1552-1555
    • Hummer, G.1    Garde, S.2    García, A.E.3    Paulaitis, M.E.4    Pratt, L.R.5
  • 73
    • 0029882171 scopus 로고    scopus 로고
    • Structural and energetic responses to cavitycreating mutations in hydrophobic cores: Observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities
    • Buckle AM, Cramer P, Fersht AR (1996) Structural and energetic responses to cavitycreating mutations in hydrophobic cores: Observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities. Biochemistry 35(14):4298-4305
    • (1996) Biochemistry , vol.35 , Issue.14 , pp. 4298-4305
    • Buckle, A.M.1    Cramer, P.2    Fersht, A.R.3
  • 74
    • 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(1):158-177
    • (1998) Protein Sci , vol.7 , Issue.1 , pp. 158-177
    • Xu, J.1    Baase, W.A.2    Baldwin, E.3    Matthews, B.W.4
  • 76
    • 49749199032 scopus 로고
    • Cleavage of the haem-protein link by acid methylethylketone
    • Teale FW (1959) Cleavage of the haem-protein link by acid methylethylketone. Biochim Biophys Acta 35:543
    • (1959) Biochim Biophys Acta , vol.35 , pp. 543
    • Teale, F.W.1
  • 77
    • 0000714183 scopus 로고
    • A comparison of the conformation of sperm whale metmyoglobin with that of apomyoglobin
    • Crumpton MJ, Polson A (1965) A comparison of the conformation of sperm whale metmyoglobin with that of apomyoglobin. J Mol Biol 11:722-729
    • (1965) J Mol Biol , vol.11 , pp. 722-729
    • Crumpton, M.J.1    Polson, A.2
  • 78
    • 42149139254 scopus 로고    scopus 로고
    • Biomedical EPR, part B: Methodology, instrumentation, and dynamics
    • eds Eaton SR, Eaton GR, Berliner LJ New York), Springer
    • Rinard GA, Eaton GR (2005) Biomedical EPR, part B: Methodology, instrumentation, and dynamics. Biological Magnetic Resonance, eds Eaton SR, Eaton GR, Berliner LJ (Springer, New York), Vol 24, p 28
    • (2005) Biological Magnetic Resonance , vol.24 , pp. 28
    • Rinard, G.A.1    Eaton, G.R.2
  • 79
    • 0029795404 scopus 로고    scopus 로고
    • High resolution crystal structures of the deoxy, oxy, and aquomet forms of cobalt myoglobin
    • Brucker EA, Olson JS, Phillips GN, Jr., Dou Y, Ikeda-Saito M (1996) High resolution crystal structures of the deoxy, oxy, and aquomet forms of cobalt myoglobin. J Biol Chem 271(41):25419-25422
    • (1996) J Biol Chem , vol.271 , Issue.41 , pp. 25419-25422
    • Brucker, E.A.1    Olson, J.S.2    Phillips, Jr.G.N.3    Dou, Y.4    Ikeda-Saito, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.