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Protein folding is the process by which proteins achieve their mature functional (native) tertiary structure, and often begins co-translationally. Protein folding requires chaperones and often involves stepwise establishment of regular secondary and supersecondary structures, namely α-helices and β-sheets, that fold rapidly, stabilized by hydrogen bonding and disulphide bridges, and then tertiary structure.
The quality control of muscle myosin relies on the chaperone UNC-45. The chaperone binds folded and misfolded myosin and channel them into folding and degradation pathways. Interaction with UNC-45 is mediated by a conserved FX3HY motif, carrying myopathy mutations that can cause myosin to aggregate.
Cryo-electron microscopy, in vitro reconstitution and molecular dynamics simulations provide insight into the architecture of a plasma membrane microdomain in yeast, the organization and dynamics of the membrane lipids within this microdomain and how it responds to mechanical stress.
Heat-lability and fibrillation of insulin pose significant challenges for insulin storage. Here, the authors report chemically modified analogs of insulin by functionalizing the ε-amine group of B29 Lys with phenylalanine, to improve insulin thermostability and resist fibrillation while maintaining robust in vivo activity.
The central dogma of molecular biology requires many proteins, but how these proteins arose during evolution remains unclear. Here, authors reveal that a subset of RNA polymerases and ribosomal proteins featuring four distinct β-barrel folds diversified from a common ancestor.
Sensing stress within the endoplasmic reticulum (ER), the ER transmembrane protein IRE1α initiates a signal transduction pathway to restore homeostasis. A study finds that this process requires an ER membrane-bound phase separation event that leads to the local assembly of stress granules (SGs) and delivery of signalling components.
Claire Durrant reminds us of the importance of studying the physiological roles of proteins and their aggregates to understand their roles in disease and inform therapies, discussing a 2008 paper on amyloid-β from the Arancio lab.
Natural protein folding takes place in aqueous cell environments. Now, it has been found that proteins in a water-free environment undergo faster and more efficient folding.