Gunnar von HEIJNE

This study shows that buried ion-pairs in artificial proteins reshape folding pathways by introducing kinetic barriers that are overcome by hydrophobic collapse and core packing.

This study uses Force Profile Analysis to examine the cotranslational folding of Firefly luciferase, revealing a complex, quasi-continuous folding process with multiple intermediate steps.

The paper shows that human signal peptides are inefficiently cleaved by yeast SPCs due to differences in SPC-lipid interactions and membrane thinning profiles.

This study investigates the biogenesis of the SARS-CoV-2 M protein, revealing key steps in its insertion, folding, and oligomerization.

The paper studies cotranslational folding and autoproteolytic processing of HIV-1 protease during viral particle assembly.

The paper investigates the cotranslational membrane insertion of the KvAP voltage-sensitive ion channel using Force Profile Analysis, revealing three distinct insertion steps and the role of charged residues and helical structures.

The paper develops a method to determine sequence-dependent propensities for membrane protein insertion states using glycosylation patterns and UMAP analysis.

This study shows calmodulin acts as a chaperone during co-translational folding of the Kv7.2 channel's calcium responsive domain by stabilizing metastable hairpins.

The paper uses FPA and MD simulations to study how individual residues in an AP-stalled NC interact with the ribosome exit tunnel, showing residue-specific effects on translational arrest.

This study investigates the cotranslational folding of human growth hormone in vitro and in E. coli, showing that folding begins before complete ribosomal release and involves chaperone interactions.

SignalP 6.0 predicts all five types of signal peptides with improved accuracy and applies to metagenomic data.

This study uses molecular dynamics simulations to investigate XBP1u AP-ribosome interactions and their variants, revealing insights into the mechanism of translational arrest.

The paper uses Force Profile Analysis to study cotranslational folding of a periplasmic protein domain in E. coli, finding that folding occurs post-translationally.

The paper analyzes the residue-specific forces during cotranslational membrane protein integration in E. coli using force profile analysis.

This study uses Force Profile Analysis to examine cotranslational folding of alkaline phosphatase in E. coli periplasm, revealing folding forces transmitted from periplasm to ribosome and identifying disulfide-stabilized intermediates.

The paper introduces TargetP 2.0, a deep learning method to identify N-terminal sorting signals in proteins, revealing insights into the importance of the second residue in targeting peptides.

The paper compares FPA with other techniques to study cotranslational folding of two protein domains, finding they identify similar folding transitions.

This study maps the membrane topology and maturation mechanism of murine Astn1 and Astn2, showing they mature via endoproteolytic cleavage by signal peptidase.

The paper studies cotranslational folding of a β-helix pentarepeat protein using a force sensor assay and finds that folding of a segment produces enough force to release ribosome stalling.

The paper identifies critical residues in the Xbp1 translational arrest peptide and constructs variants with enhanced arrest potency.