4.0 Article

Shape Determination of Bovine Fibrinogen in Solution Using Small-Angle Scattering Data

Journal

CRYSTALLOGRAPHY REPORTS
Volume 63, Issue 6, Pages 871-873

Publisher

PLEIADES PUBLISHING INC
DOI: 10.1134/S1063774518060202

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Funding

  1. Federal Agency for Scientific Organizations [007-Gamma3/3363/26]
  2. Russian Science Foundation [18-15-00407]
  3. Program 5-100

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A 3D model of the shape of bovine fibrinogen, one of the proteins responsible for blood coagulation, is constructed based on small-angle X-ray scattering (SAXS) data on bovine fibrinogen in solution, and the oligomeric composition of fibrinogen in solution is estimated. It is shown that fibrinogen molecules form elongated vermicular structures with a length on the order of 50 nm and an effective cross section of about 10nm. The volume of these particles correlates well with the volume of two fibrinogen dimers. The results obtained may be helpful when applying fibrinogen and its modifications in tissue engineering.

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