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Related Experiment Videos

Models of fibronectin.

M Rocco1, E Infusini, M G Daga

  • 1Servizio di Biologia Cellulare, Istituto Nazionale per la Ricerca sul Cancro (IST), Genova, Italy.

The EMBO Journal
|August 1, 1987
PubMed
Summary
This summary is machine-generated.

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Human plasma fibronectin

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Human plasma fibronectin is a large glycoprotein crucial for cell adhesion and tissue repair.
  • Understanding fibronectin's conformation is key to elucidating its biological functions.

Purpose of the Study:

  • To determine the radius of gyration of human plasma fibronectin in extended and compact conformations.
  • To model the molecular structure of fibronectin based on experimental data.

Main Methods:

  • Light scattering measurements were used to determine the radius of gyration.
  • Molecular modeling was employed to construct and analyze potential fibronectin conformations.

Main Results:

  • The radius of gyration was 17.5 nm (extended) and 10.7 nm (compact) at a constant molecular weight of 533,000 Da.

Related Experiment Videos

  • Models suggest a compact, tangled conformation for circulating fibronectin, with exposed domains.

    • Conclusions:

    • Fibronectin adopts a compact conformation in circulation, with most domains accessible for ligand binding.
    • The proposed models provide insights into fibronectin's structural dynamics and functional implications.