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Volumn 60, Issue 3, 2005, Pages 552-557

NMR structure determination of the conserved hypothetical protein TM1816 from Thermotoga maritima

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PROTEIN TM1816; PROTEOME; UNCLASSIFIED DRUG;

EID: 23044507033     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20465     Document Type: Article
Times cited : (7)

References (21)
  • 5
  • 6
    • 0003063776 scopus 로고    scopus 로고
    • NMR structure determination and structure-based functional characterization of conserved hypothetical protein MTH1175 from Methanobacterium thermoautotrophicum
    • Cort JR, Yee A, Edwards AM, Arrowsmith CH, Kennedy MA. NMR structure determination and structure-based functional characterization of conserved hypothetical protein MTH1175 from Methanobacterium thermoautotrophicum. Struct Funct Genomics 2000;1:15-25.
    • (2000) Struct Funct Genomics , vol.1 , pp. 15-25
    • Cort, J.R.1    Yee, A.2    Edwards, A.M.3    Arrowsmith, C.H.4    Kennedy, M.A.5
  • 7
    • 0037328545 scopus 로고    scopus 로고
    • NMR assignment of the conserved hypothetical protein TM1290 of Thermotoga maritima
    • Etezady-Esfarjani T, Peti W, Wüthrich K. NMR assignment of the conserved hypothetical protein TM1290 of Thermotoga maritima. J Biomol NMR 2003;25:167-168.
    • (2003) J Biomol NMR , vol.25 , pp. 167-168
    • Etezady-Esfarjani, T.1    Peti, W.2    Wüthrich, K.3
  • 8
    • 3042796495 scopus 로고    scopus 로고
    • Letter to the Editor: NMR structure determination of the hypothetical protein TM1290 from Thermotoga maritima using automated NOESY analysis
    • Etezady-Esfarjani T, Herrmann T, Peti W, Klock HE, Lesley SA, Wüthrich K. Letter to the Editor: NMR structure determination of the hypothetical protein TM1290 from Thermotoga maritima using automated NOESY analysis. J Biomol NMR 2004;29:403-406.
    • (2004) J Biomol NMR , vol.29 , pp. 403-406
    • Etezady-Esfarjani, T.1    Herrmann, T.2    Peti, W.3    Klock, H.E.4    Lesley, S.A.5    Wüthrich, K.6
  • 9
    • 0041856106 scopus 로고    scopus 로고
    • The three-dimensional structure of the core domain of NafY from Azotobacter vinelandii determined at 1.8-Å resolution
    • Dyer DH, Rubio LM, Thoden JB Holden HM, Ludden PW. The three-dimensional structure of the core domain of NafY from Azotobacter vinelandii determined at 1.8-Å resolution. J Biol Chem 2003;278:32150-32156.
    • (2003) J Biol Chem , vol.278 , pp. 32150-32156
    • Dyer, D.H.1    Rubio, L.M.2    Thoden, J.B.3    Holden, H.M.4    Ludden, P.W.5
  • 10
    • 2442425301 scopus 로고    scopus 로고
    • Purification and characterization of NafY (apodinitrogenase γ subunit) from Azotobacter vinelandii
    • Rubio LM, Singer SW, Ludden PW. Purification and characterization of NafY (apodinitrogenase γ subunit) from Azotobacter vinelandii. J Biol Chem 2004;279:19739-19746.
    • (2004) J Biol Chem , vol.279 , pp. 19739-19746
    • Rubio, L.M.1    Singer, S.W.2    Ludden, P.W.3
  • 11
    • 12044252858 scopus 로고
    • Methodological advances in protein NMR
    • Bax A, Grzesiek S. Methodological advances in protein NMR. Acc Chem Res 1993;26:131-138.
    • (1993) Acc Chem Res , vol.26 , pp. 131-138
    • Bax, A.1    Grzesiek, S.2
  • 12
    • 0033635869 scopus 로고    scopus 로고
    • Adiabatic TOCSY for C,C and H,H J-transfer
    • Peti W, Griesinger C, Bermel W. Adiabatic TOCSY for C,C and H,H J-transfer. J Biomol NMR 2000;18:199-205.
    • (2000) J Biomol NMR , vol.18 , pp. 199-205
    • Peti, W.1    Griesinger, C.2    Bermel, W.3
  • 14
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral-analysis of biological macromolecules
    • Bartels C, Xia TH, Billeter M, Güntert P, Wüthrich K. The program XEASY for computer-supported NMR spectral-analysis of biological macromolecules. J Biomol NMR 1995;6:1-10.
    • (1995) J Biomol NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 15
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann T, Güntert P, Wüthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol 2002;319:209-227.
    • (2002) J Mol Biol , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 16
    • 0036873589 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS
    • Herrmann T, Güntert P, Wüthrich K. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS. J Biomol NMR 2002;24: 171-189.
    • (2002) J Biomol NMR , vol.24 , pp. 171-189
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 17
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert P, Mumenthaler C, Wüthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol 1997;273:283-298.
    • (1997) J Mol Biol , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 19
    • 0030236215 scopus 로고    scopus 로고
    • The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules
    • Luginbühl P, Güntert P, Billeter M, Wüthrich K. The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules. J Biomol NMR 1996;8: 136-146.
    • (1996) J Biomol NMR , vol.8 , pp. 136-146
    • Luginbühl, P.1    Güntert, P.2    Billeter, M.3    Wüthrich, K.4
  • 20
    • 0034140558 scopus 로고    scopus 로고
    • Point-centered domain decomposition for parallel molecular dynamic simulation
    • Koradi R, Billeter M, Güntert P. Point-centered domain decomposition for parallel molecular dynamic simulation. Comput Phys Commun 2000;124:139-147.
    • (2000) Comput Phys Commun , vol.124 , pp. 139-147
    • Koradi, R.1    Billeter, M.2    Güntert, P.3
  • 21
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 1996;14:51-55.
    • (1996) J Mol Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.