G. Von Heijne

This study demonstrates that the E. coli inner membrane protein EmrE begins to fold and dimerize cotranslationally during membrane insertion.

The paper shows that charged and hydrophobic residues outside transmembrane helices delay their membrane insertion during cotranslational translocation.

The paper investigates how the ribosomal exit tunnel affects the folding of a small zinc-finger domain, finding that electrostatic interactions, not just confinement, contribute to folding acceleration and stabilization.

The paper investigates how adjacent domains of α-spectrin influence each other's cotranslational folding and estimates the mechanical force exerted during this process.

The paper investigates the membrane topology of RIFIN and STEVOR proteins in Plasmodium falciparum using N-linked glycosylation to determine their ER membrane insertion patterns.

This study shows that monomeric SMR proteins exhibit topological dynamics, with the N-terminal transmembrane helix switching between inserted and non-inserted states, and this dynamics is lost upon dimerization.

The paper uses experimental and computational methods to study forces on nascent polypeptides during membrane insertion and translocation via the Sec translocon.

The study shows that the geometry of the E. coli ribosome exit tunnel influences where proteins fold during translation, with larger domains folding deeper when tunnel space is available.

This study investigates how protein size, thermodynamic stability, and net charge influence cotranslational folding on the ribosome using arrest peptides and proteolysis analysis.

The paper shows that the folding pathway of the titin I27 domain is conserved whether folding occurs on or off the ribosome.

This study investigates whether monomers of anti-parallel homo- or hetero-dimeric Small Multidrug Resistance proteins can undergo reversible topological inversion in the membrane, finding that dimerization does not affect their final topology.