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Backbone NMR assignment of the internal interaction site of ALP
Authors:Nanna Alho  Tuula Klaavuniemi  Jari Ylänne  Perttu Permi  Sampo Mattila
Affiliation:1. Department of Chemistry, University of Oulu, P.O. Box 3000, 90014, Oulu, Finland
2. Department of Biochemistry, University of Oulu, Oulu, Finland
3. Department of Biological and Environmental Sciences, University of Jyv?skyl?, Jyvaskyla, Finland
4. Institute of Biotechnology, National Biological NMR centre, University of Helsinki, Helsinki, Finland
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:NMR  ALP  Aspartic acid  iHNCA
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