Bob Schiffrin
YOU?
Author Swipe
View article: Buffer-dependent conformational dynamics of α-synuclein revealed by nanopipette electrospray ionisation ion mobility mass spectrometry
Buffer-dependent conformational dynamics of α-synuclein revealed by nanopipette electrospray ionisation ion mobility mass spectrometry Open
Electrolyte conditions in vivo and in vitro are known to influence protein structure and function. Intrinsically disordered proteins (IDPs) are particularly sensitive to their solution conditions such as ionic strength and molecular crowdi…
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: 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: <scp>PyXlinkViewer</scp> : A flexible tool for visualization of protein chemical crosslinking data within the <scp>PyMOL</scp> molecular graphics system
<span>PyXlinkViewer</span> : A flexible tool for visualization of protein chemical crosslinking data within the <span>PyMOL</span> molecular graphics system Open
Chemical crosslinking‐mass spectrometry (XL‐MS) is a valuable technique for gaining insights into protein structure and the organization of macromolecular complexes. XL‐MS data yield inter‐residue restraints that can be compared with high‐…
View article: PyXlinkViewer: a flexible tool for visualisation of protein chemical crosslinking data within the PyMOL molecular graphics system
PyXlinkViewer: a flexible tool for visualisation of protein chemical crosslinking data within the PyMOL molecular graphics system Open
Chemical crosslinking-mass spectrometry (XL-MS) is a valuable technique for gaining insights into protein structure and the organization of macromolecular complexes. XL-MS data yields inter-residue restraints that can be compared with high…
View article: Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients - dataset
Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients - dataset Open
SurA is the conserved major chaperone of outer membrane protein (OMP) biogenesis in the periplasm of Gram-negative bacteria, and plays a key role in cell envelope homeostasis and virulence. In E. coli, SurA comprises three domains: a core …
View article: Inter-domain dynamics in the chaperone SurA and multi-site binding to its unfolded outer membrane protein clients
Inter-domain dynamics in the chaperone SurA and multi-site binding to its unfolded outer membrane protein clients Open
The periplasmic chaperone SurA plays a key role in outer membrane protein (OMP) biogenesis. E. coli SurA comprises a core domain and two peptidylprolyl isomerase domains (P1 and P2), but how it binds its OMP clients and the mechanism(s) of…
View article: Data associated with 'An in vivo platform to select and evolve aggregation-resistant proteins'
Data associated with 'An in vivo platform to select and evolve aggregation-resistant proteins' Open
Protein biopharmaceuticals are highly successful, but their utility is compromised by their propensity to aggregate during manufacture and storage. As aggregation can be triggered by non-native states, whose population is not necessarily r…
View article: Effects of Periplasmic Chaperones and Membrane Thickness on BamA-Catalyzed Outer-Membrane Protein Folding
Effects of Periplasmic Chaperones and Membrane Thickness on BamA-Catalyzed Outer-Membrane Protein Folding Open
The biogenesis of outer-membrane proteins (OMPs) in gram-negative bacteria involves delivery by periplasmic chaperones to the β-barrel assembly machinery (BAM), which catalyzes OMP insertion into the outer membrane. Here, we examine the ef…