The IRE1 protein's interaction with unfolded peptides can be better understood through molecular dynamics simulations.

The Structural Dynamics of IRE1 and its Interaction with Unfolded Peptides hypothes.is/a/L60OrD5GEfGb4uvyC0sTag **eLife Assessment** In this important study, the authors conducted atomistic molecular dynamics simulations to probe the interactions between IRE and unfolded peptides. The results help reconcile contradicting experimental findings in the literature…

The Structural Dynamics of IRE1 and its Interaction with Unfolded Peptides hypothes.is/a/L0Gq_j5GEfG0IN9myv3UfA **Reviewer #2 (Public review):** Summary: In this manuscript, the authors investigated the interactions between IRE and unfolded peptides using all-atom molecular dynamics simulations. The interactions between a couple of unfolded peptides and…

The Structural Dynamics of IRE1 and its Interaction with Unfolded Peptides hypothes.is/a/Lw-9Rj5GEfGQYo_0pgMrEg **Reviewer #3 (Public review):** Summary: In this important work, the authors use extensive MD simulations to study how the IRE1 protein can detect unfolded peptides. Their study consolidates contradictory experimental results and offers a unique…

The Structural Dynamics of IRE1 and its Interaction with Unfolded Peptides hypothes.is/a/LsOK6D5GEfGeFltgPYdyhQ **Author response:** The following is the authors’ response to the original reviews > **Public Reviews:** > > **Reviewer 1 (Public review):** > > (1) "The timescales of the peptide recognition and unbinding process are much longer than what can be…

The Structural Dynamics of IRE1 and its Interaction with Unfolded Peptides hypothes.is/a/L2-YLj5GEfGhPAcJ3ZfXDw **Reviewer #1 (Public review):** Summary: This work provides structural and mechanistic insights into the disordered protein recognition process inside the endoplasmic reticulum by the inositol-requiring enzyme 1. Using state-of-the-art molecular…