Structural analysis of proteinaceous components in Byssal threads of the mussel Mytilus galloprovincialis.
The mussel byssus is a unique holdfast structure employed by marine mussels to colonize diverse substrates. The byssus consists of extracellular threads with mainly proteinaceous components. Individual threads reveal high tensile strength at their distal end and high elasticity in their proximal portion. Our studies show that proteins of the distal part are oriented along the thread axis and are well-ordered with a high beta-structural content. In contrast, proteins of the proximal part are less ordered and are not as well-oriented with primarily alpha-helical structure. The detected differences in the structural features of the proteins along a byssus thread are likely an important basis for its gradual mechanical properties.
Collagen dynamics in articular cartilage under osmotic pressure
Cartilage is a complex biological tissue consisting of collagen, proteoglycans and water. The structure and molecular mobility of the collagen component of cartilage were studied by 13C solid‐state NMR spectroscopy as a function of hydration. The hydration level of cartilage was adjusted between fully hydrated (∼80 wt% H2O) and highly dehydrated (∼30 wt% H2O) using the osmotic stress technique. Thus, the conditions of mechanical load could be simulated and the response of the tissue macromolecules to mechanical stress is reported. From the NMR measurements, the following results were obtained. (i) Measurements of motionally averaged dipolar 1H–13C couplings were carried out to study the segmental mobility in cartilage collagen at full hydration. Backbone segments undergo fast motions with amplitudes of ∼35° whereas the collagen side‐chains are somewhat more mobile with amplitudes between 40 and 50°. In spite of the high water content of cartilage, collagen remains essentially rigid. (ii) No chemical shift changes were observed in 13C cross‐polarization magic angle spinning spectra of cartilage tissue at varying hydration indicating that the collagen structure was not altered by application of high osmotic stress. (iii) The 1H–13C dipolar coupling values detected for collagen signals respond to dehydration. The dipolar coupling values gradually increase upon cartilage dehydration, reaching rigid limit values at ∼30 wt% H2O. This indicates that collagen is essentially dehydrated in cartilage tissue under very high mechanical load, which provides insights into the elastic properties of cartilage collagen, although the mechanical pressures applied here exceed the physiological limit. Copyright © 2006 John Wiley & Sons, Ltd.
Evaluation of Impact of Yarn Count and Stitch Length on Pilling, Abrasion, Shrinkage and Tightness Factor of 1 ? 1 Rib Cotton Knitted Fabrics
This study investigates the impact of yarn count and stitch length of 100% cotton knitted fabrics. 1 × 1 ribs structured fabrics were used in this research work. The stitch length 2.50 mm, 2.52 mm, 2.60 mm, 2.70 mm, 2.80 mm and 2.96 mm were used of the yarn count of 26Ne, 28Ne and 36Ne. The areal densities of the grey fabrics were in various amounts. The impacts of yarn count and stitch length were measured concerning pilling resistance, abrasion resistance, and shrinkage and tightness factor. The result showed that the fabric pilling grade decreased while number of cycle increased. Abrasion resistance decreased but length wise shrinkage increased despite the fact that the stitch length increased. The results also exposed that the tightness factor of the fabric increased with the increase of the stitch length in both dyeing and washing state and finished state compared to grey state for the yarn count 26Ne and homogeneous result not found for yarn count 28Ne and 36 Ne. Evaluation of Impact of Yarn Count and Stitch Length on Pilling, Abrasion, Shrinkage and Tightness Factor of 1 × 1 Rib Cotton Knitted Fabrics