![]() They’re then shared with senior executives and customer-facing teams, before eventually making it to production. These designs are modified in real time in Dropbox. “Our attention to detail is our competitive advantage,” Vlad Grodzinskiy, Senior Manager of Product Development, says. The headphone team is continually improving upon their patented oval ear tips to make sure their options fit comfortably into any ear canal. ![]() Designers mock up sketches and renderings incorporating the newest premium materials-like titanium tweeters and cerametallic woofers-while also making sure fans are getting what they love and expect from the brand. The product development process at Klipsch is thorough. Now headquartered in Indianapolis, the company uses the latest acoustic and technological advancements in their products and the way they market them around the world. It all started in a tin shed in Hope, Arkansas, where Paul Klipsch designed and hand-built his revolutionary speakers. And Dropbox is key to ensuring Klipsch’s teams stay in rhythm. Using patented horn loaded technology, Klipsch delivers high-clarity, low-distortion audio for their customers’ favorite music and entertainment. Klipsch founded the company in 1946, and his legacy lives on among audiophiles and people who aren’t satisfied with standard TV speakers or headphones that come with your phone. To see this figure in color, go online.Klipsch® makes speakers and headphones that deliver the latter. The image in ( B) was reprinted with permission from Dunkin et al. The scheme in ( A) was reprinted with permission from Yandek et al. The salt bridges between the lysine residues of the peptide and the phosphate headgroups of the lipids stabilize the high-energy inserted intermediate. Shown is the final state of an MD simulation of TP10W placed in a lipid bilayer. The Gibbs energies in each step are Δ G bind, binding to the bilayer interface Δ G oct, insertion into the bilayer core, approximated by transfer to octanol Δ G ins = Δ G oct − Δ G bind, insertion into the bilayer interior and Δ G f, folding in water. The peptide is shown in water ( left) and on the membrane interface ( bottom right) or inserted into the bilayer ( top right)-no orientation is implied. Shown is the thermodynamic cycle for the interactions of a membrane-active peptide with a membrane. We conclude that large effects on translocation are probably determined by hydrophobicity, but the fine tuning appears to arise from the distribution of cationic residues along the peptide sequence.Ĭopyright © 2016 Biophysical Society. We found that with regard to the changes introduced in the sequences, five out of six peptide variants translocated in agreement with the charge-distribution hypothesis, whereas none showed agreement with the hydrophobicity hypothesis. The peptides in those two series had small sequence changes relative to TP10W and DL1a: either single-residue substitutions or two-residue switches, which were designed to increase or decrease translocation differently according to the two hypotheses. The first series was based on TP10W, a peptide derived from the amphipathic CPP transportan 10 the second was based on DL1a, a synthetic peptide derived from staphylococcal δ-lysin. To test these hypotheses, we measured translocation of two series of peptide variants. The second, which we call the charge-distribution hypothesis, is that translocation is determined by whether the distribution of cationic residues in the peptide can transiently stabilize a high-energy inserted intermediate by forming salt bridges to the phosphates of lipid headgroups. ![]() The first, which we now call the hydrophobicity hypothesis, is that peptide translocation is determined by the Gibbs energy of insertion into the bilayer from the membrane interface. Here, we test two hypotheses for the differences in the ability of these peptides to translocate across membranes. ![]() Hundreds of cationic antimicrobial and cell-penetrating peptides (CPPs) form amphipathic α-helices when bound to lipid membranes.
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