Journal of Molecular Biology
Crystals of modified fibrinogen: Size, shape and packing of molecules☆
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Cited by (33)
Chorography of blood proteins
2023, Journal of Thrombosis and HaemostasisMechanisms of fibrin polymerization and clinical implications
2013, BloodCitation Excerpt :This molecular packing leads to a regular 22.5-nm repeat corresponding to one-half the length of the fibrin monomer, visualized by transmission electron microscopy and by atomic force microscopy as cross-striations in fibrin fibers.15,16 In addition to knob-hole interactions, the D-D interface comprising γ275-300 residues is an important feature of most of the known crystal forms6,17 and is likely to be similar to that at the end-to-end junction between monomers in fibrin. The D-D interactions are weak and yield first upon forced stretching of fibrin(ogen) oligomers.18
Fibrinogen and fibrin
2005, Advances in Protein ChemistryCitation Excerpt :Bovine fibrinogen was first crystallized after proteolytic removal of C-terminal portions of the Aα chains with a bacterial enzyme possessing unique specificity (Tooney and Cohen, 1972, 1974). Both crystals and microcrystals of this modified fibrinogen were examined by electron microscopy and analyzed to provide information about fibrinogen structure and the molecular packing in fibrin (Cohen et al., 1983; Weisel et al., 1978, 1981). These crystal forms are unusual in that they are made up of end-to-end bonded molecules that form flexible filaments.
Tertiary structure of the hepatic cell protein fibrinogen in fluid revealed by atomic force microscopy
1997, Cell Biology International2D crystallization: from art to science
1992, Ultramicroscopy
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This research was supported by National Institutes of Health grant AM17346 to one of us (C. C.).
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Present address: National Center for Atmospheric Research, Boulder, Col. 80307, U.S.A.