Biophysical aspects and modelling of ciliary motility.

The dominance of viscous forces in the generation of propulsive thrust by cilia is emphasised. Fourier analysis indicates that ciliary bends consist of circular arcs joined by linear segments; this arc-line shape appears to be a property associated with the molecular mechanism responsible for bending the cilium and is unchanged by variations in the external viscous loading on the organelle. The flexibility of a computer-generated model of axonemal structure is demonstrated by the incorporation of recent data concerning the surface lattice of the microtubules. Computer simulations using the model show that predictions based on stochastic, rather than co-ordinated, dynein arm activity provide a qualitative match to experimental observations of microtubules gliding over fields of dynein molecules.

The effect of soft X-radiation on myofibrils.

Myofibrils, the contractile organelles from striated muscles, have been examined in the X-ray microscope to determine the effect of radiation on their function and structure. Using X-rays of energy 350-385 eV in the water window we find that after an exposure to 7.5 x 10(5) photons/micron2 (calculated to give an absorbed dose of 20,000 Gy) the myofibrils will no longer contract. The use of the free radical scavenging agent, DMSO, gives some protection to the fibrils. It has also been found that after this much irradiation the fibrils lose up to 20% of their mass. Further substantial mass loss occurs on subsequent irradiation. After 25 times the loss-of-function exposure only 30% of the mass remains. Analysis of a series of images of the same myofibril covering this range of exposures shows that the mass is preferentially lost in some areas of the structure and consequently significant structural changes occur.

X-Ray Microscopy at Suboptical Resolution: Direct Observation of the 65-nm Periodicity in Collagen Fibrils.

Using a Fresnel zone plate we demonstrate for the first time the direct visualization by x-ray microscopy of suboptical regularity in a biological specimen, namely the 65-nm axial periodicity of tendon collagen. This resolution test demonstrates a resolving power of about 20λ; a resolving power of <10λ is in prospect.