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Showing 1 to 4 of 4 for “"Co-translational Folding"”.

  1. Energetics of [alpha]-helix formation in peptides and proteins

    … [alpha]-helix is the most prevalent type of secondary structure found in proteins, and has arguably dominated our thinking about protein structure since its discovery, as it plays an important role in the early stages of protein folding. The intrinsic helical propensities of the natural amino …

    mit Repository record for Energetics of [alpha]-helix formation in peptides and proteins (opens in a new tab)

  2. Structure and Function of the ER-Membrane Complex

    The ER-Membrane Complex (EMC) is a highly conserved heterodecameric membrane protein complex, found in the Endoplasmic Reticulum (ER) membrane. The EMC has been implicated in a wide range of processes including viral reproduction, inter-organelle phospholipid transfer, cholesterol biosynthesis and …

    cambridge Repository record for Structure and Function of the ER-Membrane Complex (opens in a new tab)

  3. Translational Control by the Ribosome-Associated Complex in the Unfolded Protein Response

    … chaperones are ubiquitous and highly conserved. There are two classes of ribosome-associated chaperones in eukaryotes, the nascent polypeptide-associated complex (NAC) and the ribosome-associated complex (RAC). Mammalian RAC consists of Hsp70L1, an Hsp70 chaperone homologue, and Mpp11, …

    utswmed Repository record for Translational Control by the Ribosome-Associated Complex in the Unfolded Protein Response (opens in a new tab)

  4. From disorder to order: the importance of context in protein folding and binding mechanisms

    … its specific three-dimensional structure is encoded into its amino acid sequence. The protein structure was believed to determine its activity, meaning that a protein needs to fold in order to function. More recently, intrinsically disordered proteins (IDPs) have been shown to represent a …

    cambridge Repository record for From disorder to order: the importance of context in protein folding and binding mechanisms (opens in a new tab)