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Volumn 71, Issue 3, 2008, Pages 1057-1065

Direct insight into insulin aggregation by 2D NMR complemented by PFGSE NMR

Author keywords

Association constants; Diffusion coefficients; Human insulin aggregates; Oligomer distribution; PFGSE NMR

Indexed keywords

INSULIN;

EID: 42449086712     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21969     Document Type: Article
Times cited : (20)

References (46)
  • 2
    • 0033869084 scopus 로고    scopus 로고
    • Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry
    • Nettleton EJ, Tito P, Sunde M, Bouchard M, Dobson CM, Robinson CV. Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry. Biophys J 2000;79:1053-1065.
    • (2000) Biophys J , vol.79 , pp. 1053-1065
    • Nettleton, E.J.1    Tito, P.2    Sunde, M.3    Bouchard, M.4    Dobson, C.M.5    Robinson, C.V.6
  • 4
    • 0035663205 scopus 로고    scopus 로고
    • In situ study of insulin aggregation induced by water-organic solvent interface
    • Kwon YM, Baudys M, Knutson K, Kim SW. In situ study of insulin aggregation induced by water-organic solvent interface. Pharm Res 2001;1:1754-1759.
    • (2001) Pharm Res , vol.1 , pp. 1754-1759
    • Kwon, Y.M.1    Baudys, M.2    Knutson, K.3    Kim, S.W.4
  • 5
    • 0026787112 scopus 로고
    • Studies of the association and conformational properties of metal-free insulin in alkaline sodium chloride solutions by one- and two-dimensional 1H NMR
    • Kadima W, Roy M, Lee RW, Kaarsholm NC, Dunn MF. Studies of the association and conformational properties of metal-free insulin in alkaline sodium chloride solutions by one- and two-dimensional 1H NMR. J Biol Chem 1992;267:8963-8970.
    • (1992) J Biol Chem , vol.267 , pp. 8963-8970
    • Kadima, W.1    Roy, M.2    Lee, R.W.3    Kaarsholm, N.C.4    Dunn, M.F.5
  • 6
    • 0025195235 scopus 로고
    • 1H NMR spectrum of the native human insulin monomer. Evidence for conformational differences between the monomer and aggregated forms
    • Roy M, Lee RW, Brange J, Dunn MF. 1H NMR spectrum of the native human insulin monomer. Evidence for conformational differences between the monomer and aggregated forms. J Biol Chem 1990;265:5448-5452.
    • (1990) J Biol Chem , vol.265 , pp. 5448-5452
    • Roy, M.1    Lee, R.W.2    Brange, J.3    Dunn, M.F.4
  • 7
    • 0041642321 scopus 로고    scopus 로고
    • Diffusion-based studies of aggregation, binding, and conformation of biomolecules: Theory and practice
    • Grant DM, Harris RK, editors, supplementary ed. New York: Wiley;
    • Price WS. Diffusion-based studies of aggregation, binding, and conformation of biomolecules: theory and practice. In: Grant DM, Harris RK, editors. Encyclopedia of nuclear magnetic resonance, supplementary ed. New York: Wiley; 2002. Vol. 9, pp 364-374.
    • (2002) Encyclopedia of nuclear magnetic resonance , vol.9 , pp. 364-374
    • Price, W.S.1
  • 8
    • 0142125805 scopus 로고    scopus 로고
    • Translational diffusion measured by PFG-NMR on full length and fragments of the Alzheimer Aβ (1-40) peptide. Determination of hydrodynamic radii of random coil peptides of varying length
    • Danielsson J, Jarvet J, Damberg P, Gräslund A. Translational diffusion measured by PFG-NMR on full length and fragments of the Alzheimer Aβ (1-40) peptide. Determination of hydrodynamic radii of random coil peptides of varying length. Mag Reson Chem 2002;40:S89-S97.
    • (2002) Mag Reson Chem , vol.40
    • Danielsson, J.1    Jarvet, J.2    Damberg, P.3    Gräslund, A.4
  • 9
    • 0033572679 scopus 로고    scopus 로고
    • Lysosyme Aggregation and Solution Properties Studied Using PGSE NMR Diffusion Measurements
    • Price WS, Tsuchiya F, Arata Y. Lysosyme Aggregation and Solution Properties Studied Using PGSE NMR Diffusion Measurements. J Am Chem Soc 1999;121:11503-11512.
    • (1999) J Am Chem Soc , vol.121 , pp. 11503-11512
    • Price, W.S.1    Tsuchiya, F.2    Arata, Y.3
  • 10
    • 0033057675 scopus 로고    scopus 로고
    • Characterization of the solution properties of Pichia Farinosa killer toxin using PGSE NMR diffusion measurements
    • Price WS, Tsuchiya F, Suzuki C, Arata Y. Characterization of the solution properties of Pichia Farinosa killer toxin using PGSE NMR diffusion measurements. J Biomol NMR 1999;13:113-117.
    • (1999) J Biomol NMR , vol.13 , pp. 113-117
    • Price, W.S.1    Tsuchiya, F.2    Suzuki, C.3    Arata, Y.4
  • 11
    • 0030893784 scopus 로고    scopus 로고
    • A pulsed-field gradient NMR study of bovine pancreatic trypsin inhibitor self-association
    • Ilyina E, Roongta V, Pan H, Woodward C, Mayo KH. A pulsed-field gradient NMR study of bovine pancreatic trypsin inhibitor self-association. Biochemistry 1997;36:3383-3388.
    • (1997) Biochemistry , vol.36 , pp. 3383-3388
    • Ilyina, E.1    Roongta, V.2    Pan, H.3    Woodward, C.4    Mayo, K.H.5
  • 12
    • 0030864810 scopus 로고    scopus 로고
    • Reduced BPTI is collapsed. A pulsed field gradient NMR study of unfolded and partially folded bovine pancreatic trypsin inhibitor
    • Pan H, Barany G, Woodward C. Reduced BPTI is collapsed. A pulsed field gradient NMR study of unfolded and partially folded bovine pancreatic trypsin inhibitor. Protein Sci 1997;6:1985-1992.
    • (1997) Protein Sci , vol.6 , pp. 1985-1992
    • Pan, H.1    Barany, G.2    Woodward, C.3
  • 13
    • 0028857598 scopus 로고
    • Association of biomolecular systems via pulsed field gradient nmr self-diffusion measurements
    • Altieri AS, Hinton DP, Byrd RA. Association of biomolecular systems via pulsed field gradient nmr self-diffusion measurements. J Am Chem Soc 1995;117:7566-7567.
    • (1995) J Am Chem Soc , vol.117 , pp. 7566-7567
    • Altieri, A.S.1    Hinton, D.P.2    Byrd, R.A.3
  • 14
    • 0029068735 scopus 로고
    • Detection of insulin aggregates with pulsed-field gradient nuclear magnetic resonance spectroscopy
    • Lin M, Larive CK. Detection of insulin aggregates with pulsed-field gradient nuclear magnetic resonance spectroscopy. Anal Biochem 1995;229:214-220.
    • (1995) Anal Biochem , vol.229 , pp. 214-220
    • Lin, M.1    Larive, C.K.2
  • 17
    • 0033556328 scopus 로고    scopus 로고
    • Characterization of allosteric insulin hexamers by electrospray ionization mass spectrometry
    • Fabris D, Fenselau C. Characterization of allosteric insulin hexamers by electrospray ionization mass spectrometry. Anal Chem 1999;71:384-387.
    • (1999) Anal Chem , vol.71 , pp. 384-387
    • Fabris, D.1    Fenselau, C.2
  • 19
  • 22
    • 0015172777 scopus 로고
    • The banting memorial lecture 1971. Physiology of insulin in man
    • Cahill GF, Jr. The banting memorial lecture 1971. Physiology of insulin in man. Diabetes 1971;20:785-799.
    • (1971) Diabetes , vol.20 , pp. 785-799
    • Cahill Jr., G.F.1
  • 24
    • 0029644942 scopus 로고
    • Role of C-terminal B-chain residues in insulin assembly: The structure of hexameric LysB28ProB29-human insulin
    • Ciszak E, Beals JM, Frank BH, Baker JC, Carter ND, Smith GD. Role of C-terminal B-chain residues in insulin assembly: the structure of hexameric LysB28ProB29-human insulin. Structure 1995;3:615-622.
    • (1995) Structure , vol.3 , pp. 615-622
    • Ciszak, E.1    Beals, J.M.2    Frank, B.H.3    Baker, J.C.4    Carter, N.D.5    Smith, G.D.6
  • 26
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism
    • Nielsen L, Khurana R, Coats A, Frokjaer S, Brange J, Vyas S, Uversky VN, Fink AL. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 2001;40:6036-6046.
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Coats, A.3    Frokjaer, S.4    Brange, J.5    Vyas, S.6    Uversky, V.N.7    Fink, A.L.8
  • 27
    • 0035902492 scopus 로고    scopus 로고
    • Probing the mechanism of insulin fibril formation with insulin mutants
    • Nielsen L, Frokjaer S, Brange J, Uversky VN, Fink AL. Probing the mechanism of insulin fibril formation with insulin mutants. Biochemistry 2001;40:8397-8409.
    • (2001) Biochemistry , vol.40 , pp. 8397-8409
    • Nielsen, L.1    Frokjaer, S.2    Brange, J.3    Uversky, V.N.4    Fink, A.L.5
  • 28
    • 42449163164 scopus 로고    scopus 로고
    • Insulin, Human monograph no. 1999:0838 European Pharmacopoeia, 3rd ed. Suppl. 2000, Council of Europe, Strasbourg. p 823.
    • Insulin, Human monograph no. 1999:0838 European Pharmacopoeia, 3rd ed. Suppl. 2000, Council of Europe, Strasbourg. p 823.
  • 29
    • 0343359244 scopus 로고
    • Investigation of exchange processes by 2-dimensional NMR-spectroscopy
    • Jeener J, Meier BH, Bachmann P, Ernst RR. Investigation of exchange processes by 2-dimensional NMR-spectroscopy. J Chem Phys 1979;71:4546-4553.
    • (1979) J Chem Phys , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 30
    • 48549112001 scopus 로고
    • Selection of coherence-transfer pathways in NMR pulse experiments
    • Bodenhausen G, Kogler H, Ernst RR. Selection of coherence-transfer pathways in NMR pulse experiments. J Magn Reson 1984;58:370-388.
    • (1984) J Magn Reson , vol.58 , pp. 370-388
    • Bodenhausen, G.1    Kogler, H.2    Ernst, R.R.3
  • 31
    • 0024282849 scopus 로고
    • Clean TOCSY for proton spin system identification in macromolecules
    • Griesinger C, Otting G, Wüthrich K, Ernst RR. Clean TOCSY for proton spin system identification in macromolecules. J Am Chem Soc 1988;110:7870-7872.
    • (1988) J Am Chem Soc , vol.110 , pp. 7870-7872
    • Griesinger, C.1    Otting, G.2    Wüthrich, K.3    Ernst, R.R.4
  • 32
    • 43949151247 scopus 로고
    • Self-Compensating pulsed magnetic-field gradients for short recovery times
    • Wider G, Detsch V, Wüthrich K. Self-Compensating pulsed magnetic-field gradients for short recovery times. J Magn Reson A 1994;108:255-258.
    • (1994) J Magn Reson A , vol.108 , pp. 255-258
    • Wider, G.1    Detsch, V.2    Wüthrich, K.3
  • 33
    • 58149362694 scopus 로고
    • An improved diffusion-ordered spectroscopy experiment incorporating bipolar-gradient pulses
    • Wu DH, Chen AD, Johnson CS. An improved diffusion-ordered spectroscopy experiment incorporating bipolar-gradient pulses. J Magn Reson A 1995;115:260-264.
    • (1995) J Magn Reson A , vol.115 , pp. 260-264
    • Wu, D.H.1    Chen, A.D.2    Johnson, C.S.3
  • 34
    • 0011685496 scopus 로고
    • Application de l'auto diffusien 'a l'étude des solutions micellaives en milieu organique.
    • Kamenka N, Fabre MH, Lindman B. Application de l'auto diffusien 'a l'étude des solutions micellaives en milieu organique. CR Acad Sc Paris 1975;281:1045-1047.
    • (1975) CR Acad Sc Paris , vol.281 , pp. 1045-1047
    • Kamenka, N.1    Fabre, M.H.2    Lindman, B.3
  • 35
    • 0042936805 scopus 로고
    • Self-diffusion in normal and heavy water in the range 1-45°C
    • Mills R. Self-diffusion in normal and heavy water in the range 1-45°C. J Phys Chem 1973;77:685-688.
    • (1973) J Phys Chem , vol.77 , pp. 685-688
    • Mills, R.1
  • 36
    • 0035744178 scopus 로고    scopus 로고
    • Accurate measurement of translational diffusion coefficients: A practical method to account for non-linear gradients
    • Damberg P, Jarvet J, Graslund A. Accurate measurement of translational diffusion coefficients: a practical method to account for non-linear gradients. J Magn Reson 2001;148:343-348.
    • (2001) J Magn Reson , vol.148 , pp. 343-348
    • Damberg, P.1    Jarvet, J.2    Graslund, A.3
  • 37
    • 0013227077 scopus 로고    scopus 로고
    • Using pulsed gradient spin echo NMR for chemical mixture analysis: How to obtain optimum results
    • Antalek B. Using pulsed gradient spin echo NMR for chemical mixture analysis: how to obtain optimum results. Concepts Magn Reson 2002;14:225-258.
    • (2002) Concepts Magn Reson , vol.14 , pp. 225-258
    • Antalek, B.1
  • 38
    • 0347359145 scopus 로고    scopus 로고
    • Diffusion ordered NMR spectroscopy: Principles and applications
    • Johnson CS. Diffusion ordered NMR spectroscopy: principles and applications. Prog Nucl Magn Reson 1999;34:203.
    • (1999) Prog Nucl Magn Reson , vol.34 , pp. 203
    • Johnson, C.S.1
  • 39
    • 0029905872 scopus 로고    scopus 로고
    • Generalized rank annihilation method applied to a single multicomponent pulsed gradient spin echo NMR data set
    • Antalek B, Windig W. Generalized rank annihilation method applied to a single multicomponent pulsed gradient spin echo NMR data set. J Am Chem Soc 1996;118:10331-10332.
    • (1996) J Am Chem Soc , vol.118 , pp. 10331-10332
    • Antalek, B.1    Windig, W.2
  • 40
    • 0030754619 scopus 로고    scopus 로고
    • Direct exponential curve resolution algorithm (DECRA): A novel application of the generalized rank annihilation method for a single spectral mixture data set with exponentially decaying contribution profiles
    • Windig W, Antalek B. Direct exponential curve resolution algorithm (DECRA): a novel application of the generalized rank annihilation method for a single spectral mixture data set with exponentially decaying contribution profiles. Chemom Intell Lab Syst 1997;37:241-254.
    • (1997) Chemom Intell Lab Syst , vol.37 , pp. 241-254
    • Windig, W.1    Antalek, B.2
  • 41
    • 0023643824 scopus 로고
    • Stereospecific assignments of side-chain protons and characterization of torsion angles in Eglin c
    • Hyberts SG, Marki W, Wagner G. Stereospecific assignments of side-chain protons and characterization of torsion angles in Eglin c. Eur J Biochem 1987;164:625-635.
    • (1987) Eur J Biochem , vol.164 , pp. 625-635
    • Hyberts, S.G.1    Marki, W.2    Wagner, G.3
  • 42
    • 0019860250 scopus 로고
    • Self-association of insulin and the role of hydrophobic bonding: A thermodynamic model of insulin dimerization
    • Pocker Y, Biswas SB. Self-association of insulin and the role of hydrophobic bonding: a thermodynamic model of insulin dimerization. Biochemistry 1981;20:4354-4361.
    • (1981) Biochemistry , vol.20 , pp. 4354-4361
    • Pocker, Y.1    Biswas, S.B.2
  • 43
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • Garcia De La Torre J, Huertas ML, Carrasco B. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys J 2000;78:719-730.
    • (2000) Biophys J , vol.78 , pp. 719-730
    • Garcia De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 44
    • 33745700267 scopus 로고    scopus 로고
    • Accounting for spin relaxation in quantitative pulse gradient spin echo NMR mixture analysis
    • Antalek B. Accounting for spin relaxation in quantitative pulse gradient spin echo NMR mixture analysis. J Am Chem Soc 2006;128:8402-8403.
    • (2006) J Am Chem Soc , vol.128 , pp. 8402-8403
    • Antalek, B.1
  • 45
    • 0027333642 scopus 로고
    • The influence of ionic strength and pH on the aggregation properties of zinc-free insulin studied by static and dynamic laser light scattering
    • Kadima W, Øgendal L, Bauer R, Kaarsholm N, Brodersen K, Hansen JF, Porting P. The influence of ionic strength and pH on the aggregation properties of zinc-free insulin studied by static and dynamic laser light scattering. Biopolymers 1993;33:1643-1657.
    • (1993) Biopolymers , vol.33 , pp. 1643-1657
    • Kadima, W.1    Øgendal, L.2    Bauer, R.3    Kaarsholm, N.4    Brodersen, K.5    Hansen, J.F.6    Porting, P.7
  • 46
    • 0015819501 scopus 로고
    • Insulin self-association. Spectrum changes and thermodynamics
    • Lord RS, Gubensek F, Rupley JA. Insulin self-association. Spectrum changes and thermodynamics. Biochemistry 1973;12:4385-4391.
    • (1973) Biochemistry , vol.12 , pp. 4385-4391
    • Lord, R.S.1    Gubensek, F.2    Rupley, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.