Gray, Geoffrey M. published the artcileSecondary structure of peptides mimicking the Gly-rich regions of major ampullate spidroin protein 1 and 2, Synthetic Route of 111-87-5, the main research area is spider silk dope secondary structure helix simulation; 3(1)-helices; Dope; Secondary structure; Simulation; Spider silk.
Spider dragline silk has highly desirable material properties, possessing high extensibility, strength, and biocompatibility. Before it is spun, the constituent proteins are stored in a concentrated dope that is void of fibrils. To investigate the structural properties of the amorphous fiber regions in the dope, computer simulations were performed on model peptides representing the N. clavipes Gly-rich regions. Anal. of the secondary structure found predominantly turns, bends and coils; a small 31-helical population decreased with increasing concentration Interestingly, the population of 31-helixes saw a large increase in octanol. These results indicate that the unusual 31-helical secondary structure of the Gly-rich region of the fiber is a consequence of the spinning process, and that the low dielec. environment of the fiber may assist in favoring this structure.
Biophysical Chemistry published new progress about Biocompatibility. 111-87-5 belongs to class alcohols-buliding-blocks, name is n-Octanol, and the molecular formula is C8H18O, Synthetic Route of 111-87-5.
Referemce:
Alcohol – Wikipedia,
Alcohols – Chemistry LibreTexts