Biomolecular NMR Assignments

, Volume 1, Issue 1, pp 85–87

Backbone NMR assignment of the internal interaction site of ALP

Authors

  • Nanna Alho
    • Department of ChemistryUniversity of Oulu
  • Tuula Klaavuniemi
    • Department of BiochemistryUniversity of Oulu
  • Jari Ylänne
    • Department of BiochemistryUniversity of Oulu
    • Department of Biological and Environmental SciencesUniversity of Jyväskylä
  • Perttu Permi
    • Institute of Biotechnology, National Biological NMR centreUniversity of Helsinki
    • Department of ChemistryUniversity of Oulu
Article

DOI: 10.1007/s12104-007-9024-1

Cite this article as:
Alho, N., Klaavuniemi, T., Ylänne, J. et al. Biomol NMR Assign (2007) 1: 85. doi:10.1007/s12104-007-9024-1

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.

Keywords

NMRALPAspartic acidiHNCA

Copyright information

© Springer Science+Business Media B.V. 2007