Physical and conformational properties of staphylokinase in solution |
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| Institution: | 1. Department of Mechanical Engineering, Boston University, Boston, Massachusetts;2. Department of Laboratory Medicine, Boston Children''s Hospital, Harvard Medical School, Boston, Massachusetts;3. Department of Biomedical Engineering, Tulane University, New Orleans, Louisiana;2. Department of Systems Biology, Boston Biomedical Research Institute and Harvard Medical School, Boston, Massachusetts, USA;1. AZTI, Food Research Division, Astondo Bidea, Edificio 609, Parque Tecnológico de Bizkaia, 48160 Derio, Bizkaia, Spain;2. Sorbonne Universités, Université de Technologie de Compiègne, Département Génie des Procédés Industriels, Laboratoire Transformations Intégrées de la Matière Renouvelable (UTC/ESCOM, EA 4297 TIMR), Centre de Recherche de Royallieu, B.P. 20529, 60205 Compiègne Cedex, France;3. Nutrition and Food Science Area, Universitat de València, Avda. Vicent Andrés Estellés, s/n 46100 Burjassot, València, Spain;4. Department of Food Science, Faculty of Science, University of Copenhagen, Rolighedsvej 26, 1958 Frederiksberg C, Denmark;1. Department of Food Science, University of Otago, PO Box 56, Dunedin, New Zealand;2. Department of Biochemistry, University of Otago, PO Box 56, Dunedin, New Zealand;3. NSW Department of Primary Industries, Orange Agricultural Institute, Forest Road, Orange NSW 2800, Australia;4. NSW Department of Primary Industries, Centre for Red Meat and Sheep Development, PO Box 129, Cowra NSW 2794, Australia |
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| Abstract: | The structure of staphylokinase has been analyzed by solution X-ray scattering, dynamic light scattering, ultracentrifugation and ultraviolet circular dichroism spectroscopy. Staphylokinase has a radius of gyration of 2.3 nm, a Stokes radius of 2.12 nm and a maximum dimension of 10 nm. The sedimentation coefficient is 1.71 S. These physical parameters indicate that the shape of staphylokinase is very elongated. The protein molecule consists of two folded domains of similar size. The mean distance of the centres of gravity of the domains is 3.7 nm. The mutual positions of the two domains are variable in solution. Thus, the molecule is shaped like a flexible dumbbell. About 18% of the amino acids of staphylokinase are organized in helical structures, 30% are incorporated in β-sheets and 20% form turns. |
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