Domain structure and interactions of the type I and type II modules in the gelatin-binding region of fibronectin. All six modules are independently folded.

@article{Litvinovich1991DomainSA,
  title={Domain structure and interactions of the type I and type II modules in the gelatin-binding region of fibronectin. All six modules are independently folded.},
  author={S V Litvinovich and Dudley K Strickland and Leonid Medved and Kenneth C Ingham},
  journal={Journal of molecular biology},
  year={1991},
  volume={217 3},
  pages={563-75}
}
The gelatin-binding region of fibronectin is isolated easily as a stable and functional 42 kDa fragment containing four type I "finger" modules and two type II "kringle-like" modules arranged in the order I6-II1-II2-I7-I8-I9. This fragment exhibits a single reversible melting transition near 64 degrees C in TBS buffer (0.02 M-Tris buffer containing 0.15 M-NaCl, pH 7.4). The transition is characterized by a calorimetric to van't Hoff enthalpy ratio of 1.6, suggesting a complex domain structure… CONTINUE READING
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