Backbone NMR assignment of the internal interaction site of ALP.
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.
Alho
Nanna
N
Department of Chemistry, University of Oulu, P.O. Box 3000, 90014 Oulu, Finland.
Klaavuniemi
Tuula
T
Ylänne
Jari
J
Permi
Perttu
P
Mattila
Sampo
S
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
D060588:LIM Domain Proteins; D008840:Microfilament Proteins; C484642:Pdlim3 protein, mouse; D011994:Recombinant Proteins; D000185:Actinin; D001224:Aspartic Acid