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Raman spectroscopy has proved to be a useful tool in the study of protein conformation in aqueous solution. Structural changes have been observed by this technique during the enzymatic conversion of fibrinogen into fibrin (J. Marx and col. (1979) Biochim. Biophys. Acta., 578, 107-115), particularly by the study of the Amide I and Amide III regions an important increase in the β-sheet form has been shown to occur. This variation is investigated under various conditions of ionic strength (μ) and protein concentration (c), two parameters which are known to change the fibre diameter (low values of μ and c favor an increase in the fibre diameter). The amount of β-sheet structure in fibrinogen is approximately 10 % and is unaffected by μ or c. In fibrin, the amount of β-sheet increases progressively from 20 % in fine clots (low diameter fibres) to more than 30 % in coarse clots (high diameter fibres). This correlation between the percentage of β-sheet structure and fibre diameter in fibrin indicates that numerous intermonomer hydrogen bonds are formed in the equatorial direction of the fibre. These bonds would greatly consolidate the association between monomers which is probably initiated at a few highly specific sites.

Laser Raman Spectroscopic Study Of The β-Sheet Structure Of Fibrinx