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Analysis of the thermal stress behaviour of functionally graded hollow circular cylinders

This paper presents an analysis of the thermomechanical behavior of hollow circular cylinders of functionally graded material (FGM). The solutions are obtained by a novel limiting process that employs the solutions of homogeneous hollow circular cylinders, with no recourse to the basic theory or the equations of non-homogeneous thermoclasticity. Several numerical cases are studied, and conclusions are drawn regarding the general properties of thermal stresses in the FGM cylinder. We conclude that thermal stresses necessarily occur in the FGM cylinder, except in the trivial case of zero temperature. While heat resistance may be improved by sagaciously designing the material composition, careful attention must be paid to the fact that thermal stresses in the FGM cylinder are governed by more factors than are its homogeneous counterparts. The results that are presented here will serve as benchmarks for future related work. (C) 2003 Elsevier Science Ltd. All rights reserved.

Disulfide folding pathways of cystine knot proteins: Tying the knot within the circular backbone of the cyclotides

The plant cyclotides are a fascinating family of circular proteins that contain a cyclic cystine knot motif. The knotted topology and cyclic nature of the cyclotides pose interesting questions about folding mechanisms and how the knotted arrangement of disulfide bonds is formed. In the current study we have examined the oxidative refolding and reductive unfolding of the prototypic cyclotide, kalata B1. A stable two-disulfide intermediate accumulated during oxidative refolding but not in reductive unfolding. Mass spectrometry and NMR spectroscopy were used to show that the intermediate contained a native-like structure with two native disulfide bonds topologically similar to the intermediate isolated for the related cystine knot protein EETI-II (LeNguyen, D., Heitz, A., Chiche, L., El Hajji, M., and Castro B. (1993) Protein Sci. 2, 165-174). However, the folding intermediate observed for kalata B1 is not the immediate precursor of the three-disulfide native peptide and does not accumulate in the reductive unfolding process, in contrast to the intermediate observed for EETI-II. These alternative pathways of linear and cyclic cystine knot proteins appear to be related to the constraints imposed by the cyclic backbone of kalata B1 and the different ring size of the cystine knot. The three-dimensional structure of a synthetic version of the two-disulfide intermediate of kalata B1 in which Ala residues replace the reduced Cys residues provides a structural insight into why the two-disulfide intermediate is a kinetic trap on the folding pathway.