Streptokinase is a flexible multi-domain protein

• Published in: European biophysics journal Vol. 20; no. 6; pp. 355 - 361
• Main Authors: DAMASCHUN, G, DAMASCHUN, H, GAST, K, GERLACH, D, MISSELWITZ, R, WELFLE, H, ZIRWER, D
• Format: Journal Article
• Language: English
• Published: Berlin Springer 1992
• Subjects: Animals; Biological and medical sciences; Circular Dichroism; Cytochrome c Group - chemistry; Fundamental and applied biological sciences. Psychology; Horses; Molecular biophysics; Molecular Structure; Phosphoglycerate Kinase - chemistry; Protein Conformation; Scattering, Radiation; Streptokinase - chemistry; Structure in molecular biology; Tridimensional structure; X-Ray Diffraction; Streptococcaceae; Streptococcus; Streptokinase; Small angle light scattering; Molecular structure; Light scattering; Circular dichroism spectrometry; Bacteria; Micrococcales; Secondary structure; Intramolecular interaction

The structure of streptokinase in solution has been studied by dynamic light scattering, small-angle X-ray scattering and circular dichroism spectroscopy. The Stokes' radius and radius of gyration of the protein monomer are 3.58 nm and 4.03 nm, respectively. The maximum intraparticle distance o...