메뉴 건너뛰기




Volumn 63, Issue 1, 2006, Pages 219-226

Predicting the redox state and secondary structure of cysteine residues in proteins using NMR chemical shifts

Author keywords

Chemical shifts; Disulfide bonded proteins; NMR; Prediction; Redox state; Secondary structure

Indexed keywords

CARBON 13; CYSTEINE; NITROGEN 15;

EID: 33645037915     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.20875     Document Type: Article
Times cited : (11)

References (29)
  • 1
    • 0008167648 scopus 로고    scopus 로고
    • Thiol-disulfide exchange of divalent sulfur
    • Sinnott M, editor. San Diego, CA: Academic Press
    • Gilbert HF. Thiol-disulfide exchange of divalent sulfur. In: Comprehensive Biological Catalysis, vol. 1, Sinnott M, editor. San Diego, CA: Academic Press; 1998. p 609-625.
    • (1998) Comprehensive Biological Catalysis , vol.1 , pp. 609-625
    • Gilbert, H.F.1
  • 2
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB. Principles that govern the folding of protein chains. Science 1973;181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 4
    • 19544393195 scopus 로고    scopus 로고
    • Disulfide connectivity prediction using secondary structure information and diresidue frequencies
    • Ferre F, Clote P. Disulfide connectivity prediction using secondary structure information and diresidue frequencies. Bioinformatics 2005;21:2336-2346.
    • (2005) Bioinformatics , vol.21 , pp. 2336-2346
    • Ferre, F.1    Clote, P.2
  • 5
    • 3242886780 scopus 로고    scopus 로고
    • GDAP: A web tool for genome-wide protein disulfide bond prediction
    • O'Connor BD, Yeates TO. GDAP: a web tool for genome-wide protein disulfide bond prediction. Nucleic Acids Res 2004;32 (Web Server issue):W360-W364.
    • (2004) Nucleic Acids Res , vol.32 , Issue.WEB SERVER ISSUE
    • O'Connor, B.D.1    Yeates, T.O.2
  • 6
    • 0032454094 scopus 로고    scopus 로고
    • Protein chemical shift analysis: A practical guide
    • Wishart DS, Nip AM. Protein chemical shift analysis: a practical guide. Biochem Cell Biol 1998;76:1-10.
    • (1998) Biochem Cell Biol , vol.76 , pp. 1-10
    • Wishart, D.S.1    Nip, A.M.2
  • 7
    • 0034501067 scopus 로고    scopus 로고
    • De novo protein structure determination using sparse NMR data
    • Bowers PM, Strauss CE, Baker D. De novo protein structure determination using sparse NMR data. J Biomol NMR 2000;18:311-318.
    • (2000) J Biomol NMR , vol.18 , pp. 311-318
    • Bowers, P.M.1    Strauss, C.E.2    Baker, D.3
  • 8
    • 0042622449 scopus 로고    scopus 로고
    • PROTINFO: Secondary and tertiary protein structure prediction
    • Hung LH, Samudrala R. PROTINFO: secondary and tertiary protein structure prediction. Nucleic Acids Res 2003;31:3296-3299.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3296-3299
    • Hung, L.H.1    Samudrala, R.2
  • 9
    • 0028434564 scopus 로고
    • 15N NMR chemical shifts in proteins and secondary structure
    • 15N NMR chemical shifts in proteins and secondary structure. J Biomol NMR 1994;4:341-348.
    • (1994) J Biomol NMR , vol.4 , pp. 341-348
    • Le, H.1    Oldfield, E.2
  • 10
    • 0014259794 scopus 로고
    • Systematic analysis of chemical shifts in the nuclear magnetic resonance spectra of peptide chains. II. Oligoglycines
    • Nakamura A, Jardetzky O. Systematic analysis of chemical shifts in the nuclear magnetic resonance spectra of peptide chains. II. Oligoglycines. Biochemistry 1968;7:1226-1230.
    • (1968) Biochemistry , vol.7 , pp. 1226-1230
    • Nakamura, A.1    Jardetzky, O.2
  • 11
    • 0001202015 scopus 로고
    • The relationship between chemical shifts and secondary structure in proteins
    • Pastore A, Saudek V. The relationship between chemical shifts and secondary structure in proteins. J Magn Reson 1990;90:165-176.
    • (1990) J Magn Reson , vol.90 , pp. 165-176
    • Pastore, A.1    Saudek, V.2
  • 12
    • 0033794319 scopus 로고    scopus 로고
    • Random coil chemical shifts in acidic 8 M urea: Implementation of random coil shift data in NMRView
    • Schwarzinger S, Kroon GJA, Foss TR, Wright PE, Dyson HJ. Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView. J Biomol NMR 2000;18:43-48.
    • (2000) J Biomol NMR , vol.18 , pp. 43-48
    • Schwarzinger, S.1    Kroon, G.J.A.2    Foss, T.R.3    Wright, P.E.4    Dyson, H.J.5
  • 13
    • 0347610773 scopus 로고
    • 13C nuclear magnetic resonance chemical shifts
    • 13C nuclear magnetic resonance chemical shifts. J Am Chem Soc 1991;113:5490-5492.
    • (1991) J Am Chem Soc , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 14
    • 0000701932 scopus 로고
    • α-proton chemical-shifts and secondary structure in proteins
    • Szilagyi L, Jardetzky O. α-Proton chemical-shifts and secondary structure in proteins. J Magn Reson 1989;83:441-449.
    • (1989) J Magn Reson , vol.83 , pp. 441-449
    • Szilagyi, L.1    Jardetzky, O.2
  • 17
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart DS, Sykes BD, Richards FM. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J Mol Biol 1991;222:311-333.
    • (1991) J Mol Biol , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 18
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart DS, Sykes BD, Richards FM. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 1992;31:1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 19
    • 0036129107 scopus 로고    scopus 로고
    • Probability-based protein secondary structure identification using combined NMR chemical-shift data
    • Wang Y, Jardetzky O. Probability-based protein secondary structure identification using combined NMR chemical-shift data. Protein Sci 2002;11:852-861.
    • (2002) Protein Sci , vol.11 , pp. 852-861
    • Wang, Y.1    Jardetzky, O.2
  • 20
    • 0033626528 scopus 로고    scopus 로고
    • 13C NMR chemical shifts can predict disulfide bond formation
    • 13C NMR chemical shifts can predict disulfide bond formation. J Biomol NMR 2000;18:165-171.
    • (2000) J Biomol NMR , vol.18 , pp. 165-171
    • Sharma, D.1    Rajarathnam, K.2
  • 21
    • 0037354231 scopus 로고    scopus 로고
    • RefDB: A database of uniformly referenced protein chemical shifts
    • Zhang H, Neal S, Wishart DS. RefDB: a database of uniformly referenced protein chemical shifts. J Biomol NMR 2003;25:173-195.
    • (2003) J Biomol NMR , vol.25 , pp. 173-195
    • Zhang, H.1    Neal, S.2    Wishart, D.S.3
  • 22
    • 15844395840 scopus 로고    scopus 로고
    • 15N chemical shift assignments of proteins
    • 15N chemical shift assignments of proteins. J Biomol NMR 2005;31:143-148.
    • (2005) J Biomol NMR , vol.31 , pp. 143-148
    • Wang, Y.1    Wishart, D.S.2
  • 23
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure
    • Kabsch W, Sander CA. dictionary of protein secondary structure. Biopolymers 1983;22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.A.2
  • 24
    • 11144240469 scopus 로고    scopus 로고
    • Solution structure and dynamics of a prototypical chordin-like cysteine-rich repeat (von Willebrand Factor type C module) from collagen IIA
    • O'Leary JM, Hamilton JM, Deane CM, Valeyev NV, Sandell LJ, Downing AK. Solution structure and dynamics of a prototypical chordin-like cysteine-rich repeat (von Willebrand Factor type C module) from collagen IIA. J Biol Chem 2004;279:53857-53866.
    • (2004) J Biol Chem , vol.279 , pp. 53857-53866
    • O'Leary, J.M.1    Hamilton, J.M.2    Deane, C.M.3    Valeyev, N.V.4    Sandell, L.J.5    Downing, A.K.6
  • 26
    • 8544271634 scopus 로고    scopus 로고
    • Solution structure of the dimeric SAM domain of MAPKKK Stell and its interactions with the adaptor protein Ste50 from the budding yeast: Implications for Stell activation and signal transmission through the Ste50-Ste11 complex
    • Bhattacharjya S, Xu P, Gingras R, Shaykhutdinov R, Wu C, Whiteway M, Ni F. Solution structure of the dimeric SAM domain of MAPKKK Stell and its interactions with the adaptor protein Ste50 from the budding yeast: implications for Stell activation and signal transmission through the Ste50-Ste11 complex. J Mol Biol 2004;344:1071-1087.
    • (2004) J Mol Biol , vol.344 , pp. 1071-1087
    • Bhattacharjya, S.1    Xu, P.2    Gingras, R.3    Shaykhutdinov, R.4    Wu, C.5    Whiteway, M.6    Ni, F.7
  • 27
    • 0028907436 scopus 로고
    • Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disulphide connectivities
    • Nilges M. Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disulphide connectivities. J Mol Biol 1995;245:645-660.
    • (1995) J Mol Biol , vol.245 , pp. 645-660
    • Nilges, M.1
  • 29
    • 0037986814 scopus 로고    scopus 로고
    • BioMagResBank database with sets of experimental NMR constraints corresponding to the structures of over 1400 biomolecules deposited in the Protein Data Bank
    • Doreleijers JF, Mading S, Maziuk D, Sojourner K, Yin L, Zhu J, Markley JL, Ulrich EL. BioMagResBank database with sets of experimental NMR constraints corresponding to the structures of over 1400 biomolecules deposited in the Protein Data Bank. J Biomol NMR 2003;26:139-146.
    • (2003) J Biomol NMR , vol.26 , pp. 139-146
    • Doreleijers, J.F.1    Mading, S.2    Maziuk, D.3    Sojourner, K.4    Yin, L.5    Zhu, J.6    Markley, J.L.7    Ulrich, E.L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.