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#chaperone protein

2 public questions tagged with this topic.

Which protein prevents premature protein folding in the ER?

During insertion into endoplasmic reticulum, nascent polypeptide must remain in extended unfolded conformation to pass through narrow Sec61 channel approximately two nanometers wide and to allow domain-wise folding only after full entry into oxidizing, calcium-rich lumen favorable for disulfide formation and N-glycosylation. Premature formation of stable secondary structure, hydrophobic collapse or helical hairpins inside ribosome exit tunnel or within translocon would block progress and cause jamming requiring ribosome-associated quality control rescue. Lumenal chaperone BiP contributes to ho

Ref: Alberts et al., Molecular Biology of the Cell, 6th ed., Chapter 12: BiP Preventing Premature Folding.

Which protein facilitates ER protein folding by recognizing exposed hydrophobic regions?

Early folding intermediates expose hydrophobic clusters that normally bury within native core and are highly aggregation-prone in crowded ER environment at high protein concentration. Recognition of such patches is specialized function of Hsp70 family member BiP, also called GRP78 encoded by HSPA5 gene, abundant in ER lumen. Its C-terminal substrate binding domain forms beta-sandwich hydrophobic cleft with lid that binds extended stretches five to seven residues enriched in leucine, isoleucine, valine, phenylalanine and tryptophan via van der Waals contacts. ATP-bound open conformation has low

Ref: Mayer & Bukau, Cell Mol Life Sci 62: 2005, BiP Binding Hydrophobic Patches.