SynopsisThe depolarized forward-scattered light from solutions of rat tail collagen has been studied by photon correlation spectroscopy. The measured autocorrelation function is seen to decay on two widely different time scales. The decay time for the fast component is consistent with the rotational diffusion of rodlike collagen monomers. The slowly decaying autocorrelation component is attributed to large nonspecific aggregates of collagen. A substantial fraction of the collagen is in this aggregated form. Extrapolation of the faster decay times to zero concentration yields a value of e$,w = 1082 f 30 sec-I for the rotational diffusion coefficient of the collagen monomer.
SynopsisSolutions of native collagen extracted from rat tail tendons in neutral salt solution have been studied by dynamic light scattering. The spectra obtained are consistent with the presence in solution of both single rod-shaped collagen molecules and aggregates of molecules. No contribution to the spectrum has been detected a t any scattering angle from rotational diffusion of single molecules, although a measurable broadening effect is expected at high angles. * 0.2 X lo-" m2/sec a t 0.064% collagen.
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