Jonathan Machin
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View article: Protein-induced membrane asymmetry modulates OMP folding kinetics and stability
Protein-induced membrane asymmetry modulates OMP folding kinetics and stability Open
Complementary charge matching between a protein-induced membrane dipole and a folding OMP leads to optimal folding kinetics and protein stability.
View article: Residues 2 to 7 of α-synuclein regulate amyloid formation via lipid-dependent and lipid-independent pathways
Residues 2 to 7 of α-synuclein regulate amyloid formation via lipid-dependent and lipid-independent pathways Open
Amyloid formation by α-synuclein (αSyn) occurs in Parkinson’s disease, multiple system atrophy, and dementia with Lewy bodies. Deciphering the residues that regulate αSyn amyloid fibril formation will not only provide mechanistic insight b…
View article: Residues 2-7 of α-synuclein regulate amyloid formation via lipid-dependent and -independent pathways
Residues 2-7 of α-synuclein regulate amyloid formation via lipid-dependent and -independent pathways Open
Amyloid formation by α-synuclein (αSyn) occurs in Parkinson’s disease, multiple system atrophy, and dementia with Lewy bodies. Deciphering the residues that regulate αSyn amyloid fibril formation will not only provide mechanistic insight, …
View article: Inside Cover: Darobactin B Stabilises a Lateral‐Closed Conformation of the BAM Complex in <i>E. coli</i> Cells (Angew. Chem. Int. Ed. 34/2023)
Inside Cover: Darobactin B Stabilises a Lateral‐Closed Conformation of the BAM Complex in <i>E. coli</i> Cells (Angew. Chem. Int. Ed. 34/2023) Open
The β-barrel assembly machine (BAM) is essential for folding outer membrane proteins (OMPs) into the outer membrane (OM) of Gram-negative bacteria. Structures of BAM have been solved using X-ray crystallography and cryoEM, but the conforma…
View article: Darobactin B Stabilises a Lateral‐Closed Conformation of the BAM Complex in <i>E. coli</i> Cells
Darobactin B Stabilises a Lateral‐Closed Conformation of the BAM Complex in <i>E. coli</i> Cells Open
The β‐barrel assembly machinery (BAM complex) is essential for outer membrane protein (OMP) folding in Gram‐negative bacteria, and represents a promising antimicrobial target. Several conformational states of BAM have been reported, but al…
View article: Darobactin B Stabilises a Lateral‐Closed Conformation of the BAM Complex in <i>E. coli</i> Cells
Darobactin B Stabilises a Lateral‐Closed Conformation of the BAM Complex in <i>E. coli</i> Cells Open
The β‐barrel assembly machinery (BAM complex) is essential for outer membrane protein (OMP) folding in Gram‐negative bacteria, and represents a promising antimicrobial target. Several conformational states of BAM have been reported, but al…
View article: Protein-lipid charge interactions control the folding of OMPs into asymmetric membranes
Protein-lipid charge interactions control the folding of OMPs into asymmetric membranes Open
Biological membranes consist of two leaflets of phospholipid molecules that form a bilayer, and typically the composition of lipids in each leaflet is distinct. This asymmetry is created and maintained in vivo by dedicated biochemical path…
View article: Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding
Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding Open
Correct folding of outer membrane proteins (OMPs) into the outer membrane of Gram-negative bacteria depends on delivery of unfolded OMPs to the β-barrel assembly machinery (BAM). How unfolded substrates are presented to BAM remains elusive…
View article: Detergent-Free Functionalization of Hybrid Vesicles with Membrane Proteins Using SMALPs
Detergent-Free Functionalization of Hybrid Vesicles with Membrane Proteins Using SMALPs Open
Hybrid vesicles (HVs) that consist of mixtures of block copolymers and lipids are robust biomimetics of liposomes, providing a valuable building block in bionanotechnology, catalysis, and synthetic biology. However, functionalization of HV…
View article: Detergent-free functionalisation of hybrid vesicles with membrane proteins using SMALPs
Detergent-free functionalisation of hybrid vesicles with membrane proteins using SMALPs Open
Hybrid vesicles (HVs) that consist of mixtures of block copolymers and lipids are robust biomimetics of liposomes, providing a valuable building block in bionanotechnology, catalysis and synthetic biology. However, functionalisation of HVs…
View article: Detergent-free functionalisation of hybrid vesicles with membrane proteins using SMALPs
Detergent-free functionalisation of hybrid vesicles with membrane proteins using SMALPs Open
Hybrid vesicles (HVs) that consist of mixtures of block copolymers and lipids are robust biomimetics of liposomes, providing a valuable building block in bionanotechnology, catalysis and synthetic biology. However, functionalisation of HVs…
View article: The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding
The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding Open
The folding of β-barrel outer membrane proteins (OMPs) in Gram-negative bacteria is catalysed by the β-barrel assembly machinery (BAM). How lateral opening in the β-barrel of the major subunit BamA assists in OMP folding, and the contribut…
View article: The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding.
The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding. Open
The folding of β-barrel outer membrane proteins (OMPs) in Gram-negative bacteria is catalysed by the β-barrel assembly machinery (BAM). How lateral opening in the β-barrel of the major subunit BamA assists in OMP folding, and the contribut…
View article: Supporting data for “The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding”
Supporting data for “The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding” Open
The folding of β-barrel outer membrane proteins (OMPs) in Gram-negative bacteria is catalysed by the β-barrel assembly machinery (BAM). How lateral opening in the BamA β-barrel, the core component of BAM, catalyses OMP folding remains uncl…