title: Backbone NMR assignment of the internal interaction site of ALP.
abstract: Earlier reports have shown that ALP has an internal interaction site. We were able to stabilize 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.
authors.affiliation: Department of Chemistry, University of Oulu, P.O. Box 3000, 90014 Oulu, Finland.
authors.forename: Nanna
authors.initials: N
authors.lastname: Alho
authors.forename: Tuula
authors.initials: T
authors.lastname: Klaavuniemi
authors.forename: Jari
authors.initials: J
authors.lastname: Ylänne
authors.forename: Perttu
authors.initials: P
authors.lastname: Permi
authors.forename: Sampo
authors.initials: S
authors.lastname: Mattila
mesh_terms: D000185:Actinin / Q000737:chemistry; D000818:Animals; D001224:Aspartic Acid / Q000737:chemistry; D001665:Binding Sites; D060588:LIM Domain Proteins; D051379:Mice; D008840:Microfilament Proteins / Q000737:chemistry* / Q000235:genetics; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics
chemical_list: D060588:LIM Domain Proteins; D008840:Microfilament Proteins; C484642:Pdlim3 protein, mouse; D011994:Recombinant Proteins; D000185:Actinin; D001224:Aspartic Acid