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Volumn 17, Issue 8, 2008, Pages 1319-1325

NMR insights into a megadalton-size protein self-assembly

Author keywords

Gdn HCl; NMR; Protein folding; Relaxation measurement; Self assembly

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 4; DYNAMIN;

EID: 48249102645     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.035840.108     Document Type: Article
Times cited : (16)

References (30)
  • 1
    • 0031160103 scopus 로고    scopus 로고
    • Temperature dependence of 1H chemical shifts in proteins
    • Baxter, N.J. and Williamson, M.P. 1997. Temperature dependence of 1H chemical shifts in proteins. J. Biomol. NMR 9: 359-369.
    • (1997) J. Biomol. NMR , vol.9 , pp. 359-369
    • Baxter, N.J.1    Williamson, M.P.2
  • 2
    • 0035846574 scopus 로고    scopus 로고
    • An efficient high-throughput resonance assignment procedure for structural genomics and protein folding research by NMR
    • Bhavesh, N.S., Panchal, S.C., and Hosur, R.V. 2001. An efficient high-throughput resonance assignment procedure for structural genomics and protein folding research by NMR. Biochemistry 40: 14727-14735.
    • (2001) Biochemistry , vol.40 , pp. 14727-14735
    • Bhavesh, N.S.1    Panchal, S.C.2    Hosur, R.V.3
  • 3
    • 0038504067 scopus 로고    scopus 로고
    • NMR elucidation of early folding hierarchy in HIV-1 protease
    • Bhavesh, N.S., Sinha, R., Mohan, P.M., and Hosur, R.V. 2003. NMR elucidation of early folding hierarchy in HIV-1 protease. J. Biol. Chem. 278: 19980-19985.
    • (2003) J. Biol. Chem , vol.278 , pp. 19980-19985
    • Bhavesh, N.S.1    Sinha, R.2    Mohan, P.M.3    Hosur, R.V.4
  • 5
  • 6
    • 33645034619 scopus 로고    scopus 로고
    • Structural characterization of the large soluble oligomers of the GTPase effector domain of dynamin
    • Chugh, J., Chatterjee, A., Kumar, A., Mishra, R.K., Mittal, R., and Hosur, R.V. 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    Kumar, A.3    Mishra, R.K.4    Mittal, R.5    Hosur, R.V.6
  • 7
    • 35448958168 scopus 로고    scopus 로고
    • Pockets of short-range transient order and restricted topological heterogeneity in the guanidine-denatured state ensemble of GED of dynamin
    • Chugh, J., Sharma, S., and Hosur, R.V. 2007. Pockets of short-range transient order and restricted topological heterogeneity in the guanidine-denatured state ensemble of GED of dynamin. Biochemistry 46: 11819-11832.
    • (2007) Biochemistry , vol.46 , pp. 11819-11832
    • Chugh, J.1    Sharma, S.2    Hosur, R.V.3
  • 8
    • 38349049191 scopus 로고    scopus 로고
    • Tuning the HNN experiment: Generation of serine-threonine check points
    • Chugh, J., Kumar, D., and Hosur, R.V. 2008. Tuning the HNN experiment: Generation of serine-threonine check points. J. Biomol. NMR 40: 145-152.
    • (2008) J. Biomol. NMR , vol.40 , pp. 145-152
    • Chugh, J.1    Kumar, D.2    Hosur, R.V.3
  • 9
    • 0344247997 scopus 로고
    • An on-line dynamic light scattering instrument for macromolecular instrumentation
    • eds. S.E. Harding, D.B. Sattelle, and V.A. Bloomfield, pp, Royal Society of Chemistry, Cambridge, UK
    • Claes, P., Dunford, M., Kenney, A., and Vardy, P. 1992. An on-line dynamic light scattering instrument for macromolecular instrumentation. In Laser light scattering in biochemistry (eds. S.E. Harding, D.B. Sattelle, and V.A. Bloomfield), pp. 66-76. Royal Society of Chemistry, Cambridge, UK.
    • (1992) Laser light scattering in biochemistry , pp. 66-76
    • Claes, P.1    Dunford, M.2    Kenney, A.3    Vardy, P.4
  • 10
    • 0033794003 scopus 로고    scopus 로고
    • NMR spectroscopy: A multifaceted approach to macromolecular structure
    • Ferentz, A.E. and Wagner, G. 2000. NMR spectroscopy: A multifaceted approach to macromolecular structure. Q. Rev. Biophys. 33: 29-65.
    • (2000) Q. Rev. Biophys , vol.33 , pp. 29-65
    • Ferentz, A.E.1    Wagner, G.2
  • 11
    • 0025361336 scopus 로고
    • Heteronuclear three-dimensional NMR spectroscopy of isotopically labelled biological macromolecules
    • Fesik, S.W. and Zuiderweg, E.R. 1990. Heteronuclear three-dimensional NMR spectroscopy of isotopically labelled biological macromolecules. Q. Rev. Biophys. 23: 97-131.
    • (1990) Q. Rev. Biophys , vol.23 , pp. 97-131
    • Fesik, S.W.1    Zuiderweg, E.R.2
  • 12
  • 13
    • 33846285730 scopus 로고    scopus 로고
    • Solution NMR of large molecules and assemblies
    • Foster, M.P., McElroy, C.A., and Amero, C.D. 2007. Solution NMR of large molecules and assemblies. Biochemistry 46: 331-340.
    • (2007) Biochemistry , vol.46 , pp. 331-340
    • Foster, M.P.1    McElroy, C.A.2    Amero, C.D.3
  • 15
    • 0034526495 scopus 로고    scopus 로고
    • Dynamin and its role in membrane fission
    • Hinshaw, J.E. 2000. Dynamin and its role in membrane fission. Annu. Rev. Cell Dev. Biol. 16: 483-519.
    • (2000) Annu. Rev. Cell Dev. Biol , vol.16 , pp. 483-519
    • Hinshaw, J.E.1
  • 16
    • 0030067634 scopus 로고    scopus 로고
    • The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
    • Hunt, J.F., Weaver, A.J., Landry, S.J., Gierasch, L., and Deisenhofer, J. 1996. The crystal structure of the GroES co-chaperonin at 2.8 Å resolution. Nature 379: 37-45.
    • (1996) Nature , vol.379 , pp. 37-45
    • Hunt, J.F.1    Weaver, A.J.2    Landry, S.J.3    Gierasch, L.4    Deisenhofer, J.5
  • 18
    • 33745915837 scopus 로고    scopus 로고
    • Residue-level NMR view of the urea-driven equilibrium folding transition of SUMO-1 (1-97): Native preferences do not increase monotonously
    • Kumar, A., Srivastava, S., Kumar, M.R., Mittal, R., and Hosur, R.V. 2006. Residue-level NMR view of the urea-driven equilibrium folding transition of SUMO-1 (1-97): Native preferences do not increase monotonously. J. Mol. Biol. 361: 180-194.
    • (2006) J. Mol. Biol , vol.361 , pp. 180-194
    • Kumar, A.1    Srivastava, S.2    Kumar, M.R.3    Mittal, R.4    Hosur, R.V.5
  • 19
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution
    • Lowe, J., Stock, D., Jap, B., Zwickl, P., Baumeister, W., and Huber, R. 1995. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science 268: 533-539.
    • (1995) Science , vol.268 , pp. 533-539
    • Lowe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 20
    • 0034919873 scopus 로고    scopus 로고
    • Improved 3D triple resonance experiments, HNN and HN(C)N, for HN and 15N sequential correlations in (13C, 15N) labeled proteins: Application to unfolded proteins
    • Panchal, S.C., Bhavesh, N.S., and Hosur, R.V. 2001. Improved 3D triple resonance experiments, HNN and HN(C)N, for HN and 15N sequential correlations in (13C, 15N) labeled proteins: Application to unfolded proteins. J. Biomol. NMR 20: 135-147.
    • (2001) J. Biomol. NMR , vol.20 , pp. 135-147
    • Panchal, S.C.1    Bhavesh, N.S.2    Hosur, R.V.3
  • 21
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: Universal membrane tubulation and fission molecules?
    • Praefcke, G.J. and McMahon, H.T. 2004. The dynamin superfamily: Universal membrane tubulation and fission molecules? Nat. Rev. Mol. Cell Biol. 5: 133-147.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 133-147
    • Praefcke, G.J.1    McMahon, H.T.2
  • 22
    • 0034306122 scopus 로고    scopus 로고
    • TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution
    • Riek, R., Pervushin, K., and Wuthrich, K. 2000. TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution. Trends Biochem. Sci. 25: 462-468.
    • (2000) Trends Biochem. Sci , vol.25 , pp. 462-468
    • Riek, R.1    Pervushin, K.2    Wuthrich, K.3
  • 23
    • 0037120882 scopus 로고    scopus 로고
    • Solution NMR techniques for large molecular and supramolecular structures
    • Riek, R., Fiaux, J., Bertelsen, E.B., Horwich, A.L., and Wuthrich, K. 2002. Solution NMR techniques for large molecular and supramolecular structures. J. Am. Chem. Soc. 124: 12144-12153.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 12144-12153
    • Riek, R.1    Fiaux, J.2    Bertelsen, E.B.3    Horwich, A.L.4    Wuthrich, K.5
  • 24
    • 0032506009 scopus 로고    scopus 로고
    • TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins
    • Salzmann, M., Pervushin, K., Wider, G., Senn, H., and Wuthrich, K. 1998. TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins. Proc. Natl. Acad. Sci. 95: 13585-13590.
    • (1998) Proc. Natl. Acad. Sci , vol.95 , pp. 13585-13590
    • Salzmann, M.1    Pervushin, K.2    Wider, G.3    Senn, H.4    Wuthrich, K.5
  • 25
    • 30844456535 scopus 로고    scopus 로고
    • SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds
    • Schanda, P., Kupce, E., and Brutscher, B. 2005. SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds. J. Biomol. NMR 33: 199-211.
    • (2005) J. Biomol. NMR , vol.33 , pp. 199-211
    • Schanda, P.1    Kupce, E.2    Brutscher, B.3
  • 26
    • 0030768045 scopus 로고    scopus 로고
    • A residue-specific NMR view of the non-cooperative unfolding of a molten globule
    • Schulman, B.A., Kim, P.S., Dobson, C.M., and Redfield, C. 1997. A residue-specific NMR view of the non-cooperative unfolding of a molten globule. Nat. Struct. Biol. 4: 630-634.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 630-634
    • Schulman, B.A.1    Kim, P.S.2    Dobson, C.M.3    Redfield, C.4
  • 27
    • 33846928691 scopus 로고    scopus 로고
    • Quantitative dynamics and binding studies of the 20S proteasome by NMR
    • Sprangers, R. and Kay, L.E. 2007. Quantitative dynamics and binding studies of the 20S proteasome by NMR. Nature 445: 618-622.
    • (2007) Nature , vol.445 , pp. 618-622
    • Sprangers, R.1    Kay, L.E.2
  • 29
    • 0035823118 scopus 로고    scopus 로고
    • Comparison of the denaturant-induced unfolding of the bovine and human α-lactalbumin molten globules
    • Wijesinha-Bettoni, R., Dobson, C.M., and Redfield, C. 2001. Comparison of the denaturant-induced unfolding of the bovine and human α-lactalbumin molten globules. J. Mol. Biol. 312: 261-273.
    • (2001) J. Mol. Biol , vol.312 , pp. 261-273
    • Wijesinha-Bettoni, R.1    Dobson, C.M.2    Redfield, C.3
  • 30
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • Xu, Z., Horwich, A.L., and Sigler, P.B. 1997. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388: 741-750.
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.