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Backbone NMR assignment of the internal interaction site of ALP

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Abstract

Earlier reports have shown that ALP has an internal interaction site. We were able to stablize the structure of this unfolded part to a great extent by aspartic acid, which allowed the backbone assignment. No secondary structure of the polypeptide was observed.

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References

  • Bondos SE, Bricknell A (2003) Detection and prevention of protein aggregation before, during, and after purification. Anal Biochem 316:223–231

    Article  Google Scholar 

  • Goddard TD, Kneller DG (2003) SPARKY 3. University of California, San Francisco

  • Golovanov AP, Hauptbergue GM, Wilson SA, Lian L (2004) A simple method for improving protein solubility and long-term stability. J Am Chem Soc 126:8933–8939

    Article  Google Scholar 

  • Ikura M, Kay LE, Bax A (1990) A novel approach for sequential assignment of proton, carbon-13, and nitrogen-15 spectra of larger proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin. Biochemistry 29:4659–4667

    Article  Google Scholar 

  • Kay LE, Ikura M, Tschudin R, Bax A (1990) Three-dimensional triple-resonance spectroscopy of isotopically enriched proteins. J Magn Reson 89:496–514

    Google Scholar 

  • Klaavuniemi T, Kelloniemi A, Ylänne J (2004) The ZASP-like motif in actinin-associated LIM protein is required for interaction with the α-actinin rod and for targeting the muscle Z-line. J Biol Chem 279:26402–26410

    Article  Google Scholar 

  • Lorenzen-Schmidt I, McCulloch AD, Omens JH (2005) Deficiency of actinin-associated LIM protein alters regional rigth ventricular function and hypertrophic remodelling. Ann Biomed Eng 33:888–896

    Article  Google Scholar 

  • Permi P (2002) Intraresidual HNCA: An experiment for correlating only intraresidual backbone resonances. J Biol NMR 23:201–209

    Article  Google Scholar 

  • Spera S, Bax A (1991) Empirical correlation between protein backbone conformation and Cα and Cβ 13C nuclear magnetic resonance chemical shifts. J Am Chem Soc 113:5490–5492

    Article  Google Scholar 

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Acknowledgments

This work was financially supported by the Academy of Finland, Biocenter Oulu and Finnish Heart Foundation.

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Authors and Affiliations

  1. Department of Chemistry, University of Oulu, P.O. Box 3000, 90014, Oulu, Finland

    Nanna Alho & Sampo Mattila

  2. Department of Biochemistry, University of Oulu, Oulu, Finland

    Tuula Klaavuniemi & Jari Ylänne

  3. Department of Biological and Environmental Sciences, University of Jyväskylä, Jyvaskyla, Finland

    Jari Ylänne

  4. Institute of Biotechnology, National Biological NMR centre, University of Helsinki, Helsinki, Finland

    Perttu Permi

Authors
  1. Nanna Alho
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  2. Tuula Klaavuniemi
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  3. Jari Ylänne
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  4. Perttu Permi
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  5. Sampo Mattila
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Correspondence to Sampo Mattila.

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Alho, N., Klaavuniemi, T., Ylänne, J. et al. Backbone NMR assignment of the internal interaction site of ALP. Biomol NMR Assign 1, 85–87 (2007). https://doi.org/10.1007/s12104-007-9024-1

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  • DOI: https://doi.org/10.1007/s12104-007-9024-1

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