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Volumn 100, Issue 3, 2011, Pages 747-755

High-resolution conformation and backbone dynamics of a soluble aggregate of apomyoglobin119

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PHYSETERIDAE;

EID: 79551668313     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.12.3722     Document Type: Article
Times cited : (4)

References (72)
  • 1
    • 77953417539 scopus 로고    scopus 로고
    • Basic mechanisms of neurodegeneration: A critical update
    • Jellinger, K. A. 2010. Basic mechanisms of neurodegeneration: a critical update. J. Cell. Mol. Med. 14:457-487.
    • (2010) J. Cell. Mol. Med. , vol.14 , pp. 457-487
    • Jellinger, K.A.1
  • 2
    • 77954358960 scopus 로고    scopus 로고
    • Mysterious oligomerization of the amyloidogenic proteins
    • Uversky, V. N. 2010. Mysterious oligomerization of the amyloidogenic proteins. FEBS J. 277:2940-2953.
    • (2010) FEBS J. , vol.277 , pp. 2940-2953
    • Uversky, V.N.1
  • 4
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • Bucciantini, M., E. Giannoni, M. Stefani. 2002. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature. 416:507-511.
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Stefani, M.3
  • 5
    • 33845248270 scopus 로고    scopus 로고
    • Amyloidosis-associated kidney disease
    • Dember, L. M. 2006. Amyloidosis-associated kidney disease. J. Am. Soc. Nephrol. 17:3458-3471.
    • (2006) J. Am. Soc. Nephrol. , vol.17 , pp. 3458-3471
    • Dember, L.M.1
  • 6
    • 77749308402 scopus 로고    scopus 로고
    • Amyloid oligomers: Formation and toxicity of Ab oligomers
    • Sakono, M., and T. Zako. 2010. Amyloid oligomers: formation and toxicity of Ab oligomers. FEBS J. 277:1348-1358.
    • (2010) FEBS J. , vol.277 , pp. 1348-1358
    • Sakono, M.1    Zako, T.2
  • 7
    • 77749316908 scopus 로고    scopus 로고
    • Amyloid oligomers: Dynamics and toxicity in the cytosol and nucleus
    • Kitamura, A., and H. Kubota. 2010. Amyloid oligomers: dynamics and toxicity in the cytosol and nucleus. FEBS J. 277:1369-1379.
    • (2010) FEBS J. , vol.277 , pp. 1369-1379
    • Kitamura, A.1    Kubota, H.2
  • 8
    • 59649087258 scopus 로고    scopus 로고
    • Structure, formation and propagation of amyloid fibrils
    • Goto, Y., H. Yagi, T. Ban. 2008. Structure, formation and propagation of amyloid fibrils. Curr. Pharm. Des. 14:3205-3218.
    • (2008) Curr. Pharm. Des. , vol.14 , pp. 3205-3218
    • Goto, Y.1    Yagi, H.2    Ban, T.3
  • 9
    • 33750017513 scopus 로고    scopus 로고
    • Molecular structure of amyloid fibrils: Insights from solid-state NMR
    • Tycko, R. 2006. Molecular structure of amyloid fibrils: insights from solid-state NMR. Q. Rev. Biophys. 39:1-55.
    • (2006) Q. Rev. Biophys. , vol.39 , pp. 1-55
    • Tycko, R.1
  • 10
    • 33645995764 scopus 로고    scopus 로고
    • Recent atomic models of amyloid fibril structure
    • Nelson, R., and D. Eisenberg. 2006. Recent atomic models of amyloid fibril structure. Curr. Opin. Struct. Biol. 16:260-265.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 260-265
    • Nelson, R.1    Eisenberg, D.2
  • 11
    • 21044431809 scopus 로고    scopus 로고
    • Structure of β-amyloid fibrils and its relevance to their neurotoxicity: Implications for the pathogenesis of Alzheimer's disease
    • Irie, K., K. Murakami, T. Shirasawa. 2005. Structure of β-amyloid fibrils and its relevance to their neurotoxicity: implications for the pathogenesis of Alzheimer's disease. J. Biosci. Bioeng. 99:437-447.
    • (2005) J. Biosci. Bioeng. , vol.99 , pp. 437-447
    • Irie, K.1    Murakami, K.2    Shirasawa, T.3
  • 12
    • 63849197629 scopus 로고    scopus 로고
    • Amyloidβ-protein assembly and Alzheimer disease
    • Roychaudhuri, R., M. Yang, D. B. Teplow. 2009. Amyloidβ-protein assembly and Alzheimer disease. J. Biol. Chem. 284:4749-4753.
    • (2009) J. Biol. Chem. , vol.284 , pp. 4749-4753
    • Roychaudhuri, R.1    Yang, M.2    Teplow, D.B.3
  • 13
    • 33749832945 scopus 로고    scopus 로고
    • Elucidating amyloid β-protein folding and assembly: A multidisciplinary approach
    • Teplow, D. B., N. D. Lazo, H. E. Stanley. 2006. Elucidating amyloid β-protein folding and assembly: a multidisciplinary approach. Acc. Chem. Res. 39:635-645.
    • (2006) Acc. Chem. Res. , vol.39 , pp. 635-645
    • Teplow, D.B.1    Lazo, N.D.2    Stanley, H.E.3
  • 14
    • 22444449900 scopus 로고    scopus 로고
    • On the nucleation of amyloid β-protein monomer folding
    • Lazo, N. D., M. A. Grant, D. B. Teplow. 2005. On the nucleation of amyloid β-protein monomer folding. Protein Sci. 14:1581-1596.
    • (2005) Protein Sci. , vol.14 , pp. 1581-1596
    • Lazo, N.D.1    Grant, M.A.2    Teplow, D.B.3
  • 15
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid β protein assembly in the brain impairs memory
    • Lesné, S., M. T. Koh, K. H. Ashe. 2006. A specific amyloid β protein assembly in the brain impairs memory. Nature. 440:352-357.
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesné, S.1    Koh, M.T.2    Ashe, K.H.3
  • 16
    • 33645505550 scopus 로고    scopus 로고
    • Effects of secreted oligomers of amyloid β-protein on hippocampal synaptic plasticity: A potent role for trimers
    • Townsend, M., G. M. Shankar, D. J. Selkoe. 2006. Effects of secreted oligomers of amyloid β-protein on hippocampal synaptic plasticity: a potent role for trimers. J. Physiol. 572:477-492.
    • (2006) J. Physiol. , vol.572 , pp. 477-492
    • Townsend, M.1    Shankar, G.M.2    Selkoe, D.J.3
  • 17
    • 67249087641 scopus 로고    scopus 로고
    • Soluble oligomers of amyloid β protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake
    • Li, S. M., S. Y. Hong, D. Selkoe. 2009. Soluble oligomers of amyloid β protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake. Neuron. 62:788-801.
    • (2009) Neuron , vol.62 , pp. 788-801
    • Li, S.M.1    Hong, S.Y.2    Selkoe, D.3
  • 18
    • 5344277556 scopus 로고    scopus 로고
    • Deciphering the molecular basis of memory failure in Alzheimer's disease
    • Walsh, D. M., and D. J. Selkoe. 2004. Deciphering the molecular basis of memory failure in Alzheimer's disease. Neuron. 44:181-193.
    • (2004) Neuron , vol.44 , pp. 181-193
    • Walsh, D.M.1    Selkoe, D.J.2
  • 19
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins
    • Lambert, M. P., A. K. Barlow, W. L. Klein. 1998. Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins. Proc. Natl. Acad. Sci. USA. 95:6448-6453.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Klein, W.L.3
  • 20
    • 13044287361 scopus 로고    scopus 로고
    • Plaque-independent disruption of neural circuits in Alzheimer's disease mouse models
    • Hsia, A. Y., E. Masliah, L. Mucke. 1999. Plaque-independent disruption of neural circuits in Alzheimer's disease mouse models. Proc. Natl. Acad. Sci. USA. 96:3228-3233.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3228-3233
    • Hsia, A.Y.1    Masliah, E.2    Mucke, L.3
  • 21
    • 9444245809 scopus 로고    scopus 로고
    • Morphology and toxicity of Aβ-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease
    • Roher, A. E., M. O. Chaney, M. R. Emmerling. 1996. Morphology and toxicity of Aβ-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease. J. Biol. Chem. 271:20631-20635.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20631-20635
    • Roher, A.E.1    Chaney, M.O.2    Emmerling, M.R.3
  • 22
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fändrich, M., M. A. Fletcher, and C. M. Dobson. 2001. Amyloid fibrils from muscle myoglobin. Nature. 410:165-166.
    • (2001) Nature , vol.410 , pp. 165-166
    • Fändrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 23
    • 4143097041 scopus 로고    scopus 로고
    • Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin
    • Pallarès, I., J. Vendrell, S. Ventura. 2004. Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin. J. Mol. Biol. 342:321-331.
    • (2004) J. Mol. Biol. , vol.342 , pp. 321-331
    • Pallarès, I.1    Vendrell, J.2    Ventura, S.3
  • 25
    • 29244450505 scopus 로고    scopus 로고
    • Partitioning conformational intermediates between competing refolding and aggregation pathways: Insights into transthyretin amyloid disease
    • Wiseman, R. L., E. T. Powers, and J. W. Kelly. 2005. Partitioning conformational intermediates between competing refolding and aggregation pathways: insights into transthyretin amyloid disease. Biochemistry. 44:16612-16623.
    • (2005) Biochemistry , vol.44 , pp. 16612-16623
    • Wiseman, R.L.1    Powers, E.T.2    Kelly, J.W.3
  • 26
    • 33646139168 scopus 로고    scopus 로고
    • Structural characterization of apomyoglobin self-associated species in aqueous buffer and urea solution
    • Chow, C., N. Kurt, S. Cavagnero. 2006. Structural characterization of apomyoglobin self-associated species in aqueous buffer and urea solution. Biophys. J. 90:298-309.
    • (2006) Biophys. J. , vol.90 , pp. 298-309
    • Chow, C.1    Kurt, N.2    Cavagnero, S.3
  • 27
    • 28444454101 scopus 로고    scopus 로고
    • Amyloid fibril formation can proceed from different conformations of a partially unfolded protein
    • Calamai, M., F. Chiti, and C. M. Dobson. 2005. Amyloid fibril formation can proceed from different conformations of a partially unfolded protein. Biophys. J. 89:4201-4210.
    • (2005) Biophys. J. , vol.89 , pp. 4201-4210
    • Calamai, M.1    Chiti, F.2    Dobson, C.M.3
  • 28
    • 71649100480 scopus 로고    scopus 로고
    • Searching for conditions to form stable protein oligomers with amyloid-like characteristics: The unexplored basic pH
    • Ahmad, B., J. Winkelmann, F. Chiti. 2010. Searching for conditions to form stable protein oligomers with amyloid-like characteristics: the unexplored basic pH. Biochim. Biophys. Acta. 1804:223-234.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 223-234
    • Ahmad, B.1    Winkelmann, J.2    Chiti, F.3
  • 29
    • 39349110541 scopus 로고    scopus 로고
    • Molecular mechanisms of polypeptide aggregation in human diseases
    • Khare, S. D., and N. V. Dokholyan. 2007. Molecular mechanisms of polypeptide aggregation in human diseases. Curr. Protein Pept. Sci. 8:573-579.
    • (2007) Curr. Protein Pept. Sci. , vol.8 , pp. 573-579
    • Khare, S.D.1    Dokholyan, N.V.2
  • 30
    • 64549140676 scopus 로고    scopus 로고
    • Structural characterization of a soluble amyloid β-peptide oligomer
    • Yu, L. P., R. Edalji, E. T. Olejniczak. 2009. Structural characterization of a soluble amyloid β-peptide oligomer. Biochemistry. 48:1870-1877.
    • (2009) Biochemistry , vol.48 , pp. 1870-1877
    • Yu, L.P.1    Edalji, R.2    Olejniczak, E.T.3
  • 31
    • 43049131763 scopus 로고    scopus 로고
    • Aβ-globulomers are formed independently of the fibril pathway
    • Gellermann, G. P., H. Byrnes, S. Barghorn. 2008. Aβ-globulomers are formed independently of the fibril pathway. Neurobiol. Dis. 30:212-220.
    • (2008) Neurobiol. Dis. , vol.30 , pp. 212-220
    • Gellermann, G.P.1    Byrnes, H.2    Barghorn, S.3
  • 32
    • 42449086712 scopus 로고    scopus 로고
    • Direct insight into insulin aggregation by 2D NMR complemented by PFGSE NMR
    • Bocian, W., J. Sitkowski, L. Kozerski. 2008. Direct insight into insulin aggregation by 2D NMR complemented by PFGSE NMR. Proteins. 71:1057-1065.
    • (2008) Proteins , vol.71 , pp. 1057-1065
    • Bocian, W.1    Sitkowski, J.2    Kozerski, L.3
  • 33
    • 27644493692 scopus 로고    scopus 로고
    • Globular amyloid β-peptide oligomer-a homogenous and stable neuropathological protein in Alzheimer's disease
    • Barghorn, S., V. Nimmrich, H. Hillen. 2005. Globular amyloid β-peptide oligomer-a homogenous and stable neuropathological protein in Alzheimer's disease. J. Neurochem. 95:834-847.
    • (2005) J. Neurochem. , vol.95 , pp. 834-847
    • Barghorn, S.1    Nimmrich, V.2    Hillen, H.3
  • 34
    • 33645034619 scopus 로고    scopus 로고
    • Structural characterization of the large soluble oligomers of the GTPase effector domain of dynamin
    • Chugh, J., A. Chatterjee, R. V. Hosur. 2006. Structural characterization of the large soluble oligomers of the GTPase effector domain of dynamin. FEBS J. 273:388-397.
    • (2006) FEBS J. , vol.273 , pp. 388-397
    • Chugh, J.1    Chatterjee, A.2    Hosur, R.V.3
  • 35
    • 48249102645 scopus 로고    scopus 로고
    • NMR insights into a megaDalton-size protein self-assembly
    • Chugh, J., S. Sharma, and R. V. Hosur. 2008. NMR insights into a megaDalton-size protein self-assembly. Protein Sci. 17:1319-1325.
    • (2008) Protein Sci. , vol.17 , pp. 1319-1325
    • Chugh, J.1    Sharma, S.2    Hosur, R.V.3
  • 36
    • 0037031291 scopus 로고    scopus 로고
    • NMR identification and characterization of the flexible regions in the 160 kDa molten globule-like aggregate of barstar at low pH
    • Juneja, J., N. S. Bhavesh, R. V. Hosur. 2002. NMR identification and characterization of the flexible regions in the 160 kDa molten globule-like aggregate of barstar at low pH. Biochemistry. 41:9885-9899.
    • (2002) Biochemistry , vol.41 , pp. 9885-9899
    • Juneja, J.1    Bhavesh, N.S.2    Hosur, R.V.3
  • 37
    • 0038131090 scopus 로고    scopus 로고
    • Chain length dependence of apomyoglobin folding: Structural evolution from misfolded sheets to native helices
    • Chow, C. C., C. Chow, S. Cavagnero. 2003. Chain length dependence of apomyoglobin folding: structural evolution from misfolded sheets to native helices. Biochemistry. 42:7090-7099.
    • (2003) Biochemistry , vol.42 , pp. 7090-7099
    • Chow, C.C.1    Chow, C.2    Cavagnero, S.3
  • 38
    • 85031272461 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 39
    • 29144440075 scopus 로고    scopus 로고
    • Effect of Hsp70 chaperone on the folding and misfolding of polypeptides modeling an elongating protein chain
    • Kurt, N., S. Rajagopalan, and S. Cavagnero. 2006. Effect of Hsp70 chaperone on the folding and misfolding of polypeptides modeling an elongating protein chain. J. Mol. Biol. 355:809-820.
    • (2006) J. Mol. Biol. , vol.355 , pp. 809-820
    • Kurt, N.1    Rajagopalan, S.2    Cavagnero, S.3
  • 40
    • 33947294445 scopus 로고
    • Calibration of methanol nuclear magnetic resonance thermometer at low temperature
    • Van Geet, A. L. 1970. Calibration of methanol nuclear magnetic resonance thermometer at low temperature. Anal. Chem. 42:679-680.
    • (1970) Anal. Chem. , vol.42 , pp. 679-680
    • Van Geet, A.L.1
  • 41
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., S. Grzesiek, A. Bax. 1995. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR. 6:277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Bax, A.3
  • 42
    • 34249765651 scopus 로고
    • NMRView-a computer program for the visualization and analysis of NMR data
    • Johnson, B. A., and R. A. Blevins. 1994. NMRView-a computer program for the visualization and analysis of NMR data. J. Biomol. NMR. 4:603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 43
    • 0000451529 scopus 로고    scopus 로고
    • Improved HSQC experiments for the observation of exchange broadened signals
    • Mulder, F. A. A., C. Spronk, R. Boelens. 1996. Improved HSQC experiments for the observation of exchange broadened signals. J. Biomol. NMR. 8:223-228.
    • (1996) J. Biomol. NMR , vol.8 , pp. 223-228
    • Mulder, F.A.A.1    Spronk, C.2    Boelens, R.3
  • 44
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin, K., R. Riek, K. Wüthrich. 1997. Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc. Natl. Acad. Sci. USA. 94:12366-12371.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wüthrich, K.3
  • 46
    • 0344994534 scopus 로고    scopus 로고
    • NMR spectroscopy of large molecules and multimolecular assemblies in solution
    • DOI 10.1016/S0959-440X(99)00011-1
    • Wider, G., and K. Wüthrich. 1999. NMR spectroscopy of large molecules and multimolecular assemblies in solution. Curr. Opin. Struct. Biol. 9:594-601. (Pubitemid 29460586)
    • (1999) Current Opinion in Structural Biology , vol.9 , Issue.5 , pp. 594-601
    • Wider, G.1    Wuthrich, K.2
  • 48
    • 0141928674 scopus 로고    scopus 로고
    • TROSY in NMR studies of the structure and function of large biological macromolecules
    • Fernández, C., and G. Wider. 2003. TROSY in NMR studies of the structure and function of large biological macromolecules. Curr. Opin. Struct. Biol. 13:570-580.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 570-580
    • Fernández, C.1    Wider, G.2
  • 49
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J. Biomol. NMR. 5:67-81.
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Sykes, B.D.3
  • 55
    • 0000660936 scopus 로고
    • Mapping of spectral density functions using heteronuclear NMR relaxation measurements
    • Peng, J. W., and G. Wagner. 1992. Mapping of spectral density functions using heteronuclear NMR relaxation measurements. J. Magn. Reson. 98:308-332.
    • (1992) J. Magn. Reson , vol.98 , pp. 308-332
    • Peng, J.W.1    Wagner, G.2
  • 56
    • 0028674384 scopus 로고
    • Investigation of protein motions via relaxation measurements
    • Peng, J. W., and G. Wagner. 1994. Investigation of protein motions via relaxation measurements. Methods Enzymol. 239:563-596.
    • (1994) Methods Enzymol. , vol.239 , pp. 563-596
    • Peng, J.W.1    Wagner, G.2
  • 57
    • 27844563112 scopus 로고    scopus 로고
    • The burial of solvent-accessible surface area is a predictor of polypeptide folding and misfolding as a function of chain elongation
    • Kurt, N., and S. Cavagnero. 2005. The burial of solvent-accessible surface area is a predictor of polypeptide folding and misfolding as a function of chain elongation. J. Am. Chem. Soc. 127:15690-15691.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 15690-15691
    • Kurt, N.1    Cavagnero, S.2
  • 60
    • 0347610773 scopus 로고
    • Empirical correlation between protein backbone conformation and C-α and C-β C-13 nuclear-magnetic-resonance chemical-shifts
    • Spera, S., and A. Bax. 1991. Empirical correlation between protein backbone conformation and C-α and C-β C-13 nuclear-magnetic-resonance chemical-shifts. J. Am. Chem. Soc. 113:5490-5492.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 61
    • 0030575785 scopus 로고    scopus 로고
    • Is apomyoglobin a molten globule? Structural characterization by NMR
    • Eliezer, D., and P. E. Wright. 1996. Is apomyoglobin a molten globule? Structural characterization by NMR. J. Mol. Biol. 263:531-538.
    • (1996) J. Mol. Biol. , vol.263 , pp. 531-538
    • Eliezer, D.1    Wright, P.E.2
  • 62
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L. E., P. Keifer, and T. Saarinen. 1992. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114:10663-10665.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 63
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari, G., and A. Szabo. 1982. Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104:4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 64
    • 0025046144 scopus 로고
    • Deviations from the simple 2-parameter model-free approach to the interpretation of N-15 nuclear magnetic-relaxation of proteins
    • Clore, G. M., A. Szabo, A. M. Gronenborn. 1990. Deviations from the simple 2-parameter model-free approach to the interpretation of N-15 nuclear magnetic-relaxation of proteins. J. Am. Chem. Soc. 112:4989-4991.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 4989-4991
    • Clore, G.M.1    Szabo, A.2    Gronenborn, A.M.3
  • 65
    • 55649093500 scopus 로고    scopus 로고
    • Model-independent interpretation of NMR relaxation data for unfolded proteins: The acid-denatured state of ACBP
    • Modig, K., and F. M. Poulsen. 2008. Model-independent interpretation of NMR relaxation data for unfolded proteins: the acid-denatured state of ACBP. J. Biomol. NMR. 42:163-177.
    • (2008) J. Biomol. NMR , vol.42 , pp. 163-177
    • Modig, K.1    Poulsen, F.M.2
  • 66
    • 0033595571 scopus 로고    scopus 로고
    • Dynamics of unfolded proteins: Incorporation of distributions of correlation times in the model free analysis of NMR relaxation data
    • Buevich, A. V., and J. Baum. 1999. Dynamics of unfolded proteins: Incorporation of distributions of correlation times in the model free analysis of NMR relaxation data. J. Am. Chem. Soc. 121:8671-8672.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 8671-8672
    • Buevich, A.V.1    Baum, J.2
  • 67
    • 0029872895 scopus 로고    scopus 로고
    • Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions
    • Lefevre, J. F., K. T. Dayie, G. Wagner. 1996. Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions. Biochemistry. 35:2674-2686.
    • (1996) Biochemistry , vol.35 , pp. 2674-2686
    • Lefevre, J.F.1    Dayie, K.T.2    Wagner, G.3
  • 68
    • 0030976048 scopus 로고    scopus 로고
    • Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
    • Rüdiger, S., L. Germeroth, B. Bukau. 1997. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 16:1501-1507.
    • (1997) EMBO J. , vol.16 , pp. 1501-1507
    • Rüdiger, S.1    Germeroth, L.2    Bukau, B.3
  • 69
    • 33749512433 scopus 로고    scopus 로고
    • Secondary structure mapping of DnaK-bound protein fragments: Chain helicity and local helix unwinding at the binding site
    • Chen, Z., N. Kurt, S. Cavagnero. 2006. Secondary structure mapping of DnaK-bound protein fragments: chain helicity and local helix unwinding at the binding site. Biochemistry. 45:12325-12333.
    • (2006) Biochemistry , vol.45 , pp. 12325-12333
    • Chen, Z.1    Kurt, N.2    Cavagnero, S.3
  • 70
    • 0023042853 scopus 로고
    • X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 Å resolution
    • Kuriyan, J., S. Wilz, G. A. Petsko. 1986. X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 Å resolution. J. Mol. Biol. 192:133-154.
    • (1986) J. Mol. Biol. , vol.192 , pp. 133-154
    • Kuriyan, J.1    Wilz, S.2    Petsko, G.A.3
  • 71
    • 0022412192 scopus 로고
    • Hydrophobicity of amino acid residues in globular proteins
    • Rose, G. D., A. R. Geselowitz, M. H. Zehfus. 1985. Hydrophobicity of amino acid residues in globular proteins. Science. 229:834-838.
    • (1985) Science , vol.229 , pp. 834-838
    • Rose, G.D.1    Geselowitz, A.R.2    Zehfus, M.H.3
  • 72
    • 33751212795 scopus 로고    scopus 로고
    • Binding specificity of an α-helical protein sequence to a full-length Hsp70 chaperone and its minimal substrate-binding domain
    • Vega, C. A., N. Kurt, S. Cavagnero. 2006. Binding specificity of an α-helical protein sequence to a full-length Hsp70 chaperone and its minimal substrate-binding domain. Biochemistry. 45:13835-13846.
    • (2006) Biochemistry , vol.45 , pp. 13835-13846
    • Vega, C.A.1    Kurt, N.2    Cavagnero, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.