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Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins (2017)

  • Authors:
  • USP affiliated authors: MARCO, RICARDO DE - IFSC ; LOPES, JOSÉ LUIZ DE SOUZA - IF
  • USP Schools: IFSC; IF
  • DOI: 10.1007/s00249-017-1202-1
  • Subjects: PROTEÍNAS; CRISTALOGRAFIA; MEMBRANAS CELULARES
  • Keywords: Secondary structure; Intrinsically disordered protein; Protein conformation; Synchrotron radiation circular dichroism spectroscopy
  • Language: Inglês
  • Imprenta:
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    Informações sobre o DOI: 10.1007/s00249-017-1202-1 (Fonte: oaDOI API)
    • Este periódico é de assinatura
    • Este artigo NÃO é de acesso aberto
    Versões disponíveis em Acesso Aberto do: 10.1007/s00249-017-1202-1 (Fonte: Unpaywall API)

    Título do periódico: European Biophysics Journal

    ISSN: 0175-7571,1432-1017



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    Informações sobre o Citescore
  • Título: European Biophysics Journal

    ISSN: 0175-7571

    Citescore - 2017: 1.59

    SJR - 2017: 0.604

    SNIP - 2017: 0.613


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    • ABNT

      KUMAGAI, Patricia S.; DE MARCO, Ricardo; LOPES, José luiz de Souza. Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins. European Biophysics Journal, Heidelberg, Springer, v. 46, n. 7, p. 599-606, 2017. Disponível em: < http://dx.doi.org/10.1007/s00249-017-1202-1 > DOI: 10.1007/s00249-017-1202-1.
    • APA

      Kumagai, P. S., De Marco, R., & Lopes, J. luiz de S. (2017). Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins. European Biophysics Journal, 46( 7), 599-606. doi:10.1007/s00249-017-1202-1
    • NLM

      Kumagai PS, De Marco R, Lopes J luiz de S. Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins [Internet]. European Biophysics Journal. 2017 ; 46( 7): 599-606.Available from: http://dx.doi.org/10.1007/s00249-017-1202-1
    • Vancouver

      Kumagai PS, De Marco R, Lopes J luiz de S. Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins [Internet]. European Biophysics Journal. 2017 ; 46( 7): 599-606.Available from: http://dx.doi.org/10.1007/s00249-017-1202-1

    Referências citadas na obra
    Bürgi J, Xue B, Uversky VN, van der Goot FG (2016) Intrinsic disorder in transmembrane proteins: roles in signaling and topology prediction. PLoS One 11(7):e0158594
    Cammers-Goodwin A, Allen TJ, Oslick SL, Mcclure KF, Lee JH, Kemp DS (1996) Mechanism of stabilization of helical conformations of polypeptides by water containing trifluoroethanol. J Am Chem Soc 118:3082–3090
    Chemes LB, Alonso LG, Noval MG, de Prat-Gay G (2012) Circular dichroism techniques for the analysis of intrinsically disordered proteins and domains. Methods Mol Biol 895:387–404
    Dunker AK, Lawson JD, Brown CJ, Williams RM, Romero P, Oh JS, Oldfield CJ, Campen AM, Ratliff CM, Hipps KW, Ausio J, Nissen MS, Reeves R, Kang C, Kissinger CR, Bailey RW, Griswold MD, Chiu W, Garner EC, Obradovic Z (2001) Intrinsically disordered protein. J Mol Graph Model 19(1):26–59
    Dunker AK, Oldfield CJ, Meng J, Romero P, Yang JY, Chen JW, Vacic V, Obradovic Z, Uversky VN (2008) The unfoldomics decade: an update on intrinsically disordered proteins. BMC Genom 9(2):S1
    Galea CA, Wang Y, Sivakolundu SG, Kriwacki RW (2008) Regulation of cell division by intrinsically unstructured proteins: intrinsic flexibility, modularity, and signaling conduits. Biochem 47(29):7598–7609
    Greenfield NJ (2006) Using circular dichroism spectra to estimate protein secondary structure. Nat Protoc 1(6):2876–2890
    Hider RC, Kupryszewski G, Rekowski P, Lammek B (1988) Origin of the positive 225–230 nm circular dichroism band in proteins. Its application to conformational analysis. Biophys Chem 31(1–2):45–51
    Jasanoff A, Fersht AR (1997) Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. Biochem 36:8413
    Kelly SM, Jess TJ, Price NC (2005) How to study proteins by circular dichroism. BBA 1751:119–139
    Korsak M, Kozyreva T (2015) Beta amyloid hallmarks: from intrinsically disordered proteins to Alzheimer’s disease. In: Felli IC, Pierattelli R (eds) Intrinsically disordered proteins studies by NMR spectroscopy, 1st edn, Springer, Switzerland, pp 401–421. Adv Exp Med Biol 870:401–21
    Kragelund BB, Schenstrøm SM, Rebula CA, Panse VG, Hartmann-Petersen R (2016) DSS1/Sem1, a multifunctional and intrinsically disordered protein. Trends Biochem Sci 41(5):446–459
    Lees JG, Smith BR, Wien F, Miles AJ, Wallace BA (2004) CDtool—an integrated software package for circular dichroism spectroscopic data processing, analysis and archiving. Anal Biochem 332(2):285–289
    Lopes JLS, Orcia D, Araujo APU, DeMarco R, Wallace BA (2013) Folding factors and partners for the intrinsically disordered protein micro-exon gene 14 (MEG-14). Biophys J 104(11):2512–2520
    Miles AJ, Wallace BA (2006) Synchrotron radiation circular dichroism spectroscopy of proteins and applications in structural and functional genomics. Chem Soc Rev 35(1):39–51
    Money VA, McPhee HK, Mosely JA, Sanderson JM, Yeo RP (2009) Surface features of a Mononegavirales matrix protein indicate sites of membrane interaction. Proc Natl Acad Sci USA 106(11):4441–4446
    Moritsugu K, Terada T, Kidera A (2012) Disorder-to-order transition of an intrinsically disordered region of sortase revealed by multiscale enhanced sampling. J Am Chem Soc 134(16):7094–7101
    Powl AM, O’Reilly AO, Miles AJ, Wallace BA (2009) Synchrotron radiation circular dichroism spectroscopy-defined structure of the C-terminal domain of NaChBac and its role in channel assembly. PNAS 107(32):14064–14069
    Ranjbar B, Gill P (2009) Circular dichroism techniques: biomolecular and nanostructural analyses- a review. Chem Biol Drug Des 74(2):101–120
    Sreerama N, Woody RW (2003) Structural composition of I and II-proteins. Protein Sci 12:384–388
    Sutherland JC, Emrick A, France LL, Monteleone DC, Trunk J (1992) Circular dichroism user facility at the national synchrotron light source: estimation of protein secondary structure. Biotechniques 13(4):588–590
    Tetenbaum J, Miller LM (2001) A new spectroscopic approach to examining the role of disulfide bonds in the structure and unfolding of soybean trypsin inhibitor. Biochem 40(40):12215–12219
    Tompa P (2012) Intrinsically disordered proteins: a 10-year recap. Trends Biochem Sci 37(12):509–516
    Uversky VN (2003) A protein-chameleon: conformational plasticity of α-synuclein, a disordered protein involved in neurodegenerative disorders. J Biomol Struct Dyn 21:211–234
    Uversky VN (2009) Intrinsically disordered proteins and their environment: effects of strong denaturants, temperature, pH, counter ions, membranes, binding partners, osmolytes, and macromolecular crowding. Protein J 28(7):305–325
    Uversky VN (2013) Intrinsic disorder-based protein interactions and their modulators. Curr Pharm Des 19(23):4191–4213
    Uversky VN (2014) Introduction to intrinsically disordered proteins (IDPs). Chem Rev 114(13):6557–6560
    Uversky VN, Oldfield CJ, Dunker K (2008) Intrinsically disordered proteins in human diseases: introducing the D2 concept. Annu Rev Biophys 37:215–246
    Vavouri T, Semple JI, Garcia-Verdugo R, Lehner B (2009) Intrinsic proteins disorder and interaction promiscuity are widely associated with dosage sensitivity. Cell 138(1):198–208
    Wallace BA (2000) Conformational changes by synchrotron radiation circular dichroism spectroscopy. Nat Struct Biol 7(9):708–709
    Wallace BA, Janes RW (2001) Synchrotron radiation circular dichroism spectroscopy of proteins: secondary structure, fold recognition and structural genomics. Curr Opin Chem Biol 5(5):567–571
    Wallace BA, Janes RW (2009) Modern techniques for circular dichroism and synchrotron radiation circular dichroism spectroscopy. IOS Press, London
    Wallace BA, Janes RW (2010) Synchrotron radiation circular dichroism (SRCD) spectroscopy: an enhanced method for examining protein conformations and protein interactions. Biochem Soc Trans 38(4):861–873
    Wallace BA, Miles AJ (2016) Circular dichroism spectroscopy of membrane proteins. Chem Soc Rev 45:4859–4872
    Woody RW (1994) Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins. Eur Biophys J 23(4):253–262
    Wright PE, Dyson HJ (2015) Intrinsically disordered proteins in cellular signalling and regulation. Nature Rev Mol Cell Biol 16:18–29