Fibrinogen (factor I) is a soluble plasma glycoprotein, synthesised by the liver, that is converted by thrombin into fibrin during blood coagulation. Fibrinogen is clotted by thrombin, composed of a dimer of three non-identical pairs of polypeptide chains (alpha, beta, gamma) held together by disulfide bonds.

Crystal structure of fibrinogen. The central nodule, formed by the N-terminal portions of all six chains, is connected to the distal β- and γ-nodules formed by the C-terminal portions of the Bβ and γ chains, respectively, by triple-helical coiled-coils, each formed by the middle portions of the Aα, Bβ and γ chains.

CETP (cholesteryl ester-transfer protein) is essential for neutral lipid transfer between HDL (high-density lipoprotein) and LDL (low-density lipoprotein) and plays a critical role in the reverse cholesterol transfer pathway.
In clinical trials, CETP inhibitors increase HDL levels and reduce LDL levels, and therefore may be used as a potential treatment for atherosclerosis.

The structure of CETP reveals a 60-A-log tunnel filled with two hydorphobic cholesteryl esters and plugged by an amphiphilic phosphatidylcholine at eatch end. The two tunnel openings are large enough to allow lipid access, which is aided by a flexible helix and possibly also by a mobile flap. The curvature of the concave surface of CETP matches the radius of curvature of HDL particles, and potential conformational changes may occur to accommodate larger lipoprotein particles. Point mutations blocking the middle of the tunnel abolish lipid-transfer activities, suggesting that neutral lipids pass through this continuous tunnel.

Influenza virus particle entering a cell in the respiratory tract.
Once the cell membrane and the virus have been closely juxtaposed by virus-receptor interaction, the complex is endocytosed.