Arterioles were modeled as elastic cylindrical vessels with an

elastic matrix support and underwent axial and radial growth. Our results demonstrated that arteriole critical buckling pressure decreased with increasing axial growth ratio and radius growth ratio, but increased with increasing wall thickness. Arteriole buckling mode number increased (wavelength decreased) with increasing axial growth ratio, but decreased with increasing radius growth ratio and wall thickness. Our study suggests that axial growth in arterioles makes them prone to buckling and that buckling leads to tortuous collaterals. These results shed light on the mechanism of collateral arteriole tortuosity. (C) 2012 Elsevier Ltd. All rights reserved.”
“This review discusses the inherent challenge of linking “”reductionist”" approaches to decipher the information encoded in protein sequences with burgeoning efforts selleck chemicals to explore protein folding in native environments-”"postreductionist”" approaches. Because the invitation to write this article came as a result of my selection to receive the 2010 Dorothy Hodgkin Award of the Protein Society, I use examples

from my own work to illustrate the evolution from the reductionist to the postreductionist perspective. I am incredibly find more honored to receive the Hodgkin Award, but I want to emphasize that it is the combined effort, creativity, and talent of many students, postdoctoral fellows, and collaborators over several years that has led to any accomplishments on which this selection is based. Moreover, I do not claim to have unique insight into the topics discussed here; but this writing opportunity not allows me to illustrate some threads in the evolution of protein folding research with my own experiences and to point out to those embarking on careers how the twists and turns in anyone’s scientific path are influenced

and enriched by the scientific context of our research. The path my own career has taken thus far has been shaped by the timing of discoveries in the field of protein science; together with our contemporaries, we become part of a knowledge evolution. In my own case, this has been an epoch of great discovery in protein folding and I feel very fortunate to have participated in it.”
“Repetitive cycles of protein elongation by the ribosome involve dynamic changes in tRNA occupancy and the deacylated-tRNA dissociation plays an important role in the process. Here we present a detailed analysis of the dynamics for the complicated process. We study analytically the dynamic tRNA occupancy and, specifically, the mean time for occupancy of one tRNA molecule, two tRNA molecules and three tRNA molecules during one cycle of protein elongation. The deacylated-tRNA dissociation probability at each state of the elongation cycle is analytically studied.