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Volumn 88, Issue 2, 2013, Pages 196-200

Bacterial expression and purification of the amyloidogenic peptide PAPf39 for multidimensional NMR spectroscopy

Author keywords

Aggregation prone; Atomic force microscopy; Escherichia coli expression; HIV infection; Isotopic labeling; Nuclear magnetic resonance spectroscopy

Indexed keywords

AMYLOID; HYBRID PROTEIN; INTEIN; PEPTIDE FRAGMENT; PROSTATIC ACID PHOSPHATASE (248 286), HUMAN; PROSTATIC ACID PHOSPHATASE (248-286), HUMAN; PROTEIN TYROSINE PHOSPHATASE; UBIQUITIN;

EID: 84873682057     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2013.01.003     Document Type: Article
Times cited : (5)

References (15)
  • 2
    • 73149094532 scopus 로고    scopus 로고
    • Mechanism of fibril formation by a 39-residue peptide (PAPf39) from human prostatic acidic phosphatase
    • Z. Ye, K.C. French, L.A. Popova, I.K. Lednev, M.M. Lopez, and G.I. Makhatadze Mechanism of fibril formation by a 39-residue peptide (PAPf39) from human prostatic acidic phosphatase Biochemistry 48 2009 11582 11591
    • (2009) Biochemistry , vol.48 , pp. 11582-11591
    • Ye, Z.1    French, K.C.2    Popova, L.A.3    Lednev, I.K.4    Lopez, M.M.5    Makhatadze, G.I.6
  • 3
    • 84871554404 scopus 로고    scopus 로고
    • Core sequence of PAPf39 amyloid fibrils and mechanism of pH-dependent fibril formation: The role of monomer conformation
    • K.C. French, and G.I. Makhatadze Core sequence of PAPf39 amyloid fibrils and mechanism of pH-dependent fibril formation: the role of monomer conformation Biochemistry 51 2012 10127 10136
    • (2012) Biochemistry , vol.51 , pp. 10127-10136
    • French, K.C.1    Makhatadze, G.I.2
  • 5
    • 33744908076 scopus 로고    scopus 로고
    • Characterization of the dynamics of biomacromolecules using rotating-frame spin relaxation NMR spectroscopy
    • DOI 10.1021/cr0404287
    • A.G. Palmer 3rd, and F. Massi Characterization of the dynamics of biomacromolecules using rotating-frame spin relaxation NMR spectroscopy Chem. Rev. 106 2006 1700 1719 (Pubitemid 43840531)
    • (2006) Chemical Reviews , vol.106 , Issue.5 , pp. 1700-1719
    • Palmer III, A.G.1    Massi, F.2
  • 6
    • 17044446282 scopus 로고    scopus 로고
    • NMR studies of structure and function of biological macromolecules (Nobel Lecture)
    • DOI 10.1002/anie.200300595
    • K. Wuthrich, NMR studies of structure and function of biological macromolecules (Nobel lecture). Angewandte Chemie (International ed 42 (2003) 3340-3363. (Pubitemid 36975327)
    • (2003) Angewandte Chemie - International Edition , vol.42 , Issue.29 , pp. 3340-3363
    • Wuthrich, K.1
  • 7
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to- millisecond motions in biological macromolecules
    • DOI 10.1016/S0076-6879(01)39315-1
    • A.G. Palmer 3rd, C.D. Kroenke, and J.P. Loria Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules Methods Enzymol. 339 2001 204 238 (Pubitemid 32666562)
    • (2001) Methods in Enzymology , vol.339 , pp. 204-238
    • Palmer III, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 8
    • 34247234602 scopus 로고    scopus 로고
    • The Alzheimer's Peptides Aβ40 and 42 Adopt Distinct Conformations in Water: A Combined MD / NMR Study
    • DOI 10.1016/j.jmb.2007.02.093, PII S0022283607003105
    • N.G. Sgourakis, Y. Yan, S.A. McCallum, C. Wang, and A.E. Garcia The Alzheimer's peptides Abeta40 and 42 adopt distinct conformations in water: a combined MD/NMR study J. Mol. Biol. 368 2007 1448 1457 (Pubitemid 46617600)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.5 , pp. 1448-1457
    • Sgourakis, N.G.1    Yan, Y.2    McCallum, S.A.3    Wang, C.4    Garcia, A.E.5
  • 9
    • 77957283101 scopus 로고    scopus 로고
    • Experimental test of the thermodynamic model of protein cooperativity using temperature-induced unfolding of a Ubq-UIM fusion protein
    • M.M. Patel, N.G. Sgourakis, A.E. Garcia, and G.I. Makhatadze Experimental test of the thermodynamic model of protein cooperativity using temperature-induced unfolding of a Ubq-UIM fusion protein Biochemistry 49 2010 8455 8467
    • (2010) Biochemistry , vol.49 , pp. 8455-8467
    • Patel, M.M.1    Sgourakis, N.G.2    Garcia, A.E.3    Makhatadze, G.I.4
  • 10
    • 0347753737 scopus 로고    scopus 로고
    • Temperature Dependence of the Thermodynamics of Helix-Coil Transition
    • DOI 10.1016/j.jmb.2003.11.027
    • J.M. Richardson, and G.I. Makhatadze Temperature dependence of the thermodynamics of helix-coil transition J. Mol. Biol. 335 2004 1029 1037 (Pubitemid 38091608)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.4 , pp. 1029-1037
    • Richardson, J.M.1    Makhatadze, G.I.2
  • 11
    • 77649272589 scopus 로고    scopus 로고
    • Conformational dynamics and structural plasticity play critical roles in the ubiquitin recognition of a UIM domain
    • N.G. Sgourakis, M.M. Patel, A.E. Garcia, G.I. Makhatadze, and S.A. McCallum Conformational dynamics and structural plasticity play critical roles in the ubiquitin recognition of a UIM domain J. Mol. Biol. 396 2010 1128 1144
    • (2010) J. Mol. Biol. , vol.396 , pp. 1128-1144
    • Sgourakis, N.G.1    Patel, M.M.2    Garcia, A.E.3    Makhatadze, G.I.4    McCallum, S.A.5
  • 12
    • 0344351815 scopus 로고    scopus 로고
    • Semisynthesis of cytotoxic proteins using a modified protein splicing element
    • T.C. Evans Jr., J. Benner, and M.Q. Xu Semisynthesis of cytotoxic proteins using a modified protein splicing element Protein Sci. 7 1998 2256 2264 (Pubitemid 28506942)
    • (1998) Protein Science , vol.7 , Issue.11 , pp. 2256-2264
    • Evans Jr., T.C.1    Benner, J.2    Xu, M.-Q.3
  • 14
    • 0037266406 scopus 로고    scopus 로고
    • MONTE: An automated Monte Carlo based approach to nuclear magnetic resonance assignment of proteins
    • DOI 10.1023/A:1021975923026
    • T.K. Hitchens, J.A. Lukin, Y. Zhan, S.A. McCallum, and G.S. Rule MONTE: an automated Monte Carlo based approach to nuclear magnetic resonance assignment of proteins J. Biomol. NMR 25 2003 1 9 (Pubitemid 36181757)
    • (2003) Journal of Biomolecular NMR , vol.25 , Issue.1 , pp. 1-9
    • Hitchens, T.K.1    Lukin, J.A.2    Zhan, Y.3    McCallum, S.A.4    Rule, G.S.5
  • 15
    • 0004040543 scopus 로고    scopus 로고
    • University of California, San Francisco, (Ed.)
    • T.D. Goddard, D.G. Kneller, SPARKY 3, University of California, San Francisco, in: http://www.cgl.ucsf.edu/home/sparky/ (Ed.), 2012.
    • (2012) SPARKY 3
    • Goddard, T.D.1    Kneller, D.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.