SAN FRANCISCO Scarpe Nike Air Max Plus TN Ultra Bianche Italia , July 18 (Xinhua) -- As advances indeoxyribonucleic acid (DNA) synthesis technology merge withimprovements in computational design of new proteins, the stage isset for a new era of data-driven protein molecular engineering,according to the researchers in a new study.


Gabriel Rocklin, a postdoctoral fellow in biochemistry at theUniversity of Washington School of Medicine, is the lead author ofa paper published in the latest issue of the journal Science on thetesting of folding stability for computationally designed proteins,which was made possible by a new high-throughput approach.


Made of amino acid chains with specific sequences Scarpe Nike Air Max Plus TN Ultra Rosse Nere Italia , proteins arebiological workhorses. As natural protein sequences are encoded incellular DNA, these chains fold into three-dimensionalconformations. The sequence of the amino acids in the chain guideswhere it will bend and twist, and how parts will interact to holdthe structure together.


Researchers have studied these interactions for decades byexamining the structures of naturally occurring proteins. However,natural protein structures are typically large and complex, withthousands of interactions that collectively hold the protein in itsfolded shape. Measuring the contribution of each interactionbecomes very difficult.


The problem could be addressed by computationally designingsimpler proteins, which would make it easier for researchers toanalyze the different types of interactions that hold all proteinsin their folded structures.


In addition Nike Air Max 270 Donne Nere Bianche Italia , researchers want to build new molecules, not foundnaturally, that can perform tasks in preventing or treatingdisease, in industrial applications, in energy production, and inenvironmental cleanups. "However Nike Air Max 270 Donne Rosa Bianche Italia , computationally designed proteinsoften fail to form the folded structures that they were designed tohave when they are actually tested in the lab," Rocklin noted.


"Still, even simple proteins are so complicated that it wasimportant to study thousands of them to learn why they fold,"Rocklin said. "This had been impossible until recently, due to thecost of DNA. Each designed protein requires its own customizedpiece of DNA so that it can be made inside a cell. This has limitedprevious studies to testing only tens of designs."


In the new study, the researchers tested more than 15 Nike Air Max 270 Uomo Nere Bianche Italia ,000 newlydesigned mini-proteins that do not exist in nature to see whetherthey form folded structures. And their testing led to the design of2,788 stable protein structures and could have many bioengineeringand synthetic biology applications. Their small size may beadvantageous for treating diseases when the drug needs to reach theinside of a cell.


In comparison, major protein design studies in the past fewyears have generally examined only 50 to 100 designs.


To encode their designs of short proteins in this project, theresearchers used what is called DNA oligo library synthesistechnology, which was originally developed for other laboratoryprotocols, such as large gene assembly. By repeating the cycle ofcomputation and experimental testing over several iterations Nike Air Max 270 Uomo Nere Oro Italia , theylearned from their design failures and progressively improved theirmodeling. Their design success rate rose from 6 percent to 47percent. They also produced stable proteins in shape where all oftheir first designs failed.


The most stable natural protein the researchers identified was amuch-studied protein from the bacteria Bacillus stearothermophilus.It basks in high temperatures, like those in hot springs and oceanthermal vents. Most proteins lose their folded structures undersuch high temperature conditions. Organisms thriving there haveevolved into highly stable proteins that stay folded even whenhot.


"A total of 774 designed proteins had higher stability scoresthan this most protease-resistant monomeric protein," theresearchers noted in their paper. Proteases are enzymes that breakdown proteins, and are essential tools the researchers used tomeasure stability for their thousands of proteins.


The authors predict that, as DNA synthesis technology continuesto improve, high-throughput protein design will become possible forlarger Nike Air Max 270 KPU TPU Uomo Grigie Nere Italia , more complex protein structures. "Protein designers werelike master craftsmen who used their experience to hand-sculpt eachpiece in their workshop. Sometimes things worked, but when theyfailed it was hard to say why," Rocklin was quoted as saying in anews release. "Our new approach lets us collect an enormous amountof data on what makes proteins stable. This data can now drive thedesign process."


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