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Biology subjects

Schiffrin, B.

Publications and source records attributed to Schiffrin, B..

5 recordsLinked to original sources

FENNEC: photon-level deep learning for classifying bursts in diffusion-based single-molecule FRET

Single-molecule Forster resonance energy transfer (smFRET) reports on biomolecular conformational dynamics by measuring distance changes between donor and acceptor fluorophores. In diffusion-based smFRET, however, the detection of genuine conformational exchange is routinely confounded by photophysical artefacts, notably acceptor photobleaching and blinking, which produce similar burst-level signatures. Many existing methods for resolving conformational dynamics and dye photophysics rely on fitting kinetic models with a fixed number of states, which is typically unknown. Here we present FENNEC (Fluorescence Event Neural Network for Evaluating and Classifying bursts), a dilated convolutional neural network for diffusion-based smFRET data that simultaneously detects conformational dynamics, acceptor photobleaching, and acceptor blinking within individual bursts, directly from raw photon arrival times. FENNEC is trained entirely on simulated data, and requires no experimental data with assigned labels for training. Crucially, the dynamics classification is independent of the number of underlying states, and therefore provides an analysis and filtering method that complements established methods that extract the number of states and their kinetics. FENNEC can identify a high-confidence subset of static and dynamic bursts, while ambiguous bursts can be excluded or set aside for further analysis. Applied to a dynamic DNA hairpin, FENNEC recovers the expected population distributions. Together, these results provide proof of principle that a classifier trained on simulated photon-level data can identify conformational dynamics and photophysical artefacts in experimental smFRET data, and we invite further evaluation on a range of instruments and systems. FENNEC is freely available at https://github.com/jacrossley/FENNEC.

biophysics↗

Selective miniprotein inhibitors of Aurora-A kinase designed using interaction-motif scaffolding

Targeting kinase ATP-binding sites has produced many successful therapeutics, but selectivity remains a major challenge. We hypothesised that substrate-recognition surfaces could provide an alternative route to selective kinase inhibition. Here, we designed and tested structure-guided miniprotein inhibitors of Aurora-A using N-Myc as a template, a natural weak binder of the P+1 pocket. The most potent designs bind Aurora-A with single-digit nanomolar affinity, more than a thousand fold higher than the starting template, and selectively inhibit Aurora-A over Aurora-B in kinase assays and mitotic cells. Despite diverse architectures, successful binders targeting the substrate-recognition surface converged on a common strategy, coupling extensive engagement of the G helix with activation loop stabilisation. Together these results show that selective kinase inhibition can be achieved by exploiting structurally well-defined active-state conformations rather than kinase-specific inactive states. Our work establishes a framework for converting weak substrate-recognition surface interactors into potent, selective kinase inhibitors through structure-guided protein design.

molecular biology↗

Buffer-dependent conformational dynamics of α-synuclein revealed by nanopipette electrospray ionisation ion mobility mass spectrometry

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 crowding, and their dynamic structural ensembles rapidly respond to the cellular environment. While structural mass spectrometry (MS) techniques are uniquely able to capture aspects of this structural diversity, technical limitations have largely precluded the use of native MS approaches to interrogate the conformational rearrangements of IDPs in response to high concentrations of non-volatile salts. Here, we overcome this challenge by employing sub 100-nm nanopipette electrospray emitters for more gentle and salt-tolerant analysis to study the conformational distribution of -Synuclein (S) using native MS and ion mobility-MS in varied solution conditions, including in phosphate buffered saline. We show using native MS that it is possible to capture salt and buffer induced changes in the S conformational ensemble when using traditional biochemical buffers, which reflect structural changes from in silico predictions and in-solution measurements. This work demonstrates the power of nanopipette emitters for the study of IDPs, and establishes native MS as a method that can be routinely used to determine how solution conditions tune the conformational landscape of IDPs. O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=110 SRC="FIGDIR/small/671163v2_ufig1.gif" ALT="Figure 1"> View larger version (28K): org.highwire.dtl.DTLVardef@35ff69org.highwire.dtl.DTLVardef@113821aorg.highwire.dtl.DTLVardef@1c27b90org.highwire.dtl.DTLVardef@13e4db1_HPS_FORMAT_FIGEXP M_FIG C_FIG

biophysics↗

PyXlinkViewer: a flexible tool for visualisation of protein chemical crosslinking data within the PyMOL molecular graphics system

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-resolution structural data. Distances greater than the crosslinker spacer-arm can reveal lowly-populated "excited" states of proteins/protein assemblies, or crosslinks can be used as restraints to generate structural models in the absence of structural data. Despite increasing uptake of XL-MS, there are few tools to enable rapid and facile mapping of XL-MS data onto high-resolution structures or structural models. PyXlinkViewer is a user-friendly plugin for PyMOL v2 that maps intra-protein, inter-protein and dead-end crosslinks onto protein structures/models and automates the calculation of inter-residue distances for the detected crosslinks. This enables rapid visualisation of XL-MS data, assessment of whether a set of detected crosslinks is congruent with structural data, and easy production of high-quality images for publication.

biochemistry↗

Inter-domain dynamics in the chaperone SurA and multi-site binding to its unfolded outer membrane protein clients

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 its chaperone action remain unclear. Here, we have used chemical cross-linking, hydrogen-deuterium exchange, single-molecule FRET and molecular dynamics simulations to map the client binding site(s) on SurA and to interrogate the role of conformational dynamics of the chaperones domains in OMP recognition. We demonstrate that SurA samples a broad array of conformations in solution in which P2 primarily lies closer to the core/P1 domains than suggested by its crystal structure. Multiple binding sites for OMPs are located primarily in the core domain, with binding of the unfolded OMP resulting in conformational changes between the core/P1 domains. Together, the results portray a model in which unfolded OMP substrates bind in a cradle formed between the SurA domains, with structural flexibility between its domains assisting OMP recognition, binding and release.

biochemistry↗