
Ramin has been working to evaluate the viscoelastic properties of bovine cornea and sclera. This was done with an Enduratech ELF 3100 Dynamic Mechanical Analyzer. This instrument is able to create 22 N of linear force with 20 g acceleration with a frequency response to 100 Hz with 50 mg and 50 nm resolution. The mechanical properties of sclera and corneal are measured in a uniaxial tension according to specific conditions. Straight samples are stretched at different stages with the mechanical properties of corneal and sclera tested at each stage. The results enable us to obtain the position and formation of fibrils during tension test.

For Ramins' Masters thesis, he is looking more closely at how collagen responds as an individual molecule. To identify how the body controls the assembly and degradation of collagen at extracellular matrix level is of critical importance to understanding the formation and degradation of tissue.
Collagen molecules are 300 nm long and 1.5 nm in diameter. They are the fibrous structural proteins of the body. In the human body, they are degraded by specific enzymes called Matrixmetalloproteinases (MMP's).
The purpose of his project is to investigate the influence of mechanical loads on the cleavage rate of type I collagen by MMP's on the molecular scale. The experiments involve trapping and stretching collagen monomers between a fixed glass surface and supper-paramagnetic beads (average bead diameter 1 micrometer).
These magnetic particles have magnetic properties for the duration of present magnetic field. The time to cleavage collagen monomers as a function of mechanical load and concentration of MMP are observed and evaluated by a Nikon microscope (TE 2000-U) with DIC capabilities using a 60X objective. By this method, we can investigate the influence of mechanical load during the process of degrading monomers.
B.S. (2001) Mechanical Engineering, Sharif University of Technology, Iran.