Scientists at Rice University report their findings in PNAS
The question of whether amino acids in sandwich-like proteins are there to stabilize the structure or to speed up the protein-folding process is best answered by "all of the above," according to researchers at Rice University in Houston. This discovery, reported in todays issue of the Proceedings of the National Academy of Sciences, could benefit future research on treatments for diseases related to misfolded proteins, such as Alzheimers and Huntingtons.
The Rice scientists studied azurin – a copper-containing protein essential to electron transfer. Azurin is part of a group of proteins that fold into a sandwich-like structure consisting of two sheets of amino acids meshed together. Nearly 70 superfamilies of proteins of varying makeup have this sandwich-like structure, but they all have eight particular amino acids in common. Previous studies had shown that these eight amino acids were important to define the sandwich-like structure, but the exact role was unknown.
B.J. Almond | EurekAlert!
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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