ArticleBiophysical journal1993
The Ca(2+)-induced conformational change of gelsolin is located in the carboxyl-terminal half of the molecule.
Article in Biophysical journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 49 citations in OpenAlex.
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- Distinguishing Between Monomeric scFv and Diabody in Solution Using Light and Small Angle X-ray Scattering.Antibodies (Basel, Switzerland) · 2019Article
- Activation of Recombinantly Expressed l-Amino Acid Oxidase from Rhizoctonia solani by Sodium Dodecyl Sulfate.Molecules (Basel, Switzerland) · 2017Article
- The DFPase from Loligo vulgaris in sugar surfactant-based bicontinuous microemulsions: structure, dynamics, and enzyme activity.European biophysics journal : EBJ · 2011Article
- Accelerators, Brakes, and Gears of Actin Dynamics in Dendritic Spines.The open neuroscience journal · 2009Article
- Topological assignment of the N-terminal extension of plasma gelsolin to the gelsolin surface.The Biochemical journal · 2005Article
- Visualizing the Ca2+-dependent activation of gelsolin by using synchrotron footprinting.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Purification of native myosin filaments from muscle.Biophysical journal · 2001Article
- Kettin, a major source of myofibrillar stiffness in Drosophila indirect flight muscle.The Journal of cell biology · 2001Article
- Destabilization of Ca2+-free gelsolin may not be responsible for proteolysis in Familial Amyloidosis of Finnish Type.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Calcium-dependent conformational stability of modules 1 and 2 of human gelsolin.The Biochemical journal · 2000Article
- Ca2+ regulation of gelsolin activity: binding and severing of F-actin.Biophysical journal · 1998Article
- Severing of F-actin by the amino-terminal half of gelsolin suggests internal cooperativity in gelsolin.Biophysical journal · 1998Article
- Determination of the gelsolin binding site on F-actin: implications for severing and capping.Biophysical journal · 1998Article
- Actin-titin interaction in cardiac myofibrils: probing a physiological role.Biophysical journal · 1997Article
- The size and shape of caldesmon and its fragments in solution studied by dynamic light scattering and hydrodynamic model calculations.Biophysical journal · 1997Article
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3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
We have purified the two functionally distinct domains of gelsolin, a Ca(2+)-dependent actin binding protein, by proteolytic cleavage and characterized their size and shape in solution by dynamic light scattering. In the absence of calcium we obtained the same translational diffusion coefficient for both fragments which are of approximately equal molecular mass. The frictional ratio fo/fexp (1.33-1.39) is similar to the value as obtained for intact gelsolin (1.37) in aqueous solution (Patkowski, A., J. Seils, H. Hinssen, and T. Dorfmüller. 1990. Biopolymers. 30:427-435), indicating a similar molecular shape for the native protein as well as for the two subdomains. Upon addition of Ca2+ the translational diffusion coefficient of the carboxyl-terminal half decreased by almost 10%, while there was no change observed for the amino terminus. This result indicates that the ligand-induced conformational change as seen for intact gelsolin is probably located on the carboxyl-terminal domain of the protein. Since gelsolin has binding sites in both domains, and the isolated amino terminus binds and severs actin in a calcium-independent manner, our results suggests that the structural transition in the carboxyl-terminal part of intact gelsolin also affects the actin binding properties of the amino-terminal half.
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