Biomolecular NMR Assignments

, Volume 1, Issue 1, pp 85–87

Backbone NMR assignment of the internal interaction site of ALP

  • Nanna Alho
  • Tuula Klaavuniemi
  • Jari Ylänne
  • Perttu Permi
  • Sampo Mattila
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

Authors and Affiliations

  • Nanna Alho
    • 1
  • Tuula Klaavuniemi
    • 2
  • Jari Ylänne
    • 2
    • 3
  • Perttu Permi
    • 4
  • Sampo Mattila
    • 1
  1. 1.Department of ChemistryUniversity of OuluOuluFinland
  2. 2.Department of BiochemistryUniversity of OuluOuluFinland
  3. 3.Department of Biological and Environmental SciencesUniversity of JyväskyläJyvaskylaFinland
  4. 4.Institute of Biotechnology, National Biological NMR centreUniversity of HelsinkiHelsinkiFinland