Porcine pancreatic phospholipase A sub(2): Sequence-specific super(1)H and super(15)N NMR assignments and secondary structure

The solution structure of porcine pancreatic phospholipase A sub(2) (124 residues, 14 kDa) has been studied by two-dimensional homonuclear super(1)H and two- and three-dimensional heteronuclear super(15)N- super(1)H nuclear magnetic resonance spectroscopy. Backbone assignments were made for 117 of t...

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Bibliographic Details
Published in:Biochemistry (Easton) 1991-01, Vol.30 (M2), p.3135-3147
Main Authors: Dekker, N, Peters, A R, Slotboom, AJ, Boelens, R, Kaptein, R, de Haas, G
Format: Article
Language:English
Subjects:
cattle
N.M.R
pancreas
phospholipase A2
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Summary:The solution structure of porcine pancreatic phospholipase A sub(2) (124 residues, 14 kDa) has been studied by two-dimensional homonuclear super(1)H and two- and three-dimensional heteronuclear super(15)N- super(1)H nuclear magnetic resonance spectroscopy. Backbone assignments were made for 117 of the 124 amino acids. Short-range nuclear Overhauser effect (NOE) data show three alpha -helices from residues 1-13, 40-58, and 90-109, an antiparallel beta -sheet for residues 74-85, and a small antiparallel beta -sheet between residues 25-26 and 115-116. A super(15)N- super(1)H heteronuclear multiple-quantum correlation experiment was used to monitor amide proton exchange over a period of 22 h. In total, 61 amide protons showed slow or intermediate exchange, 46 of which are located in the three large helices.
ISSN:0006-2960