Matthew Batchelor
University of Leeds
19 Papers
58 Citations
Matthew Batchelor is an academic researcher from University of Leeds. The author has contributed to research in topics: Force spectroscopy & Chemistry. The author has an hindex of 9, co-authored 18 publications. Previous affiliations of Matthew Batchelor include University of Nottingham & University of Cambridge.
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Papers
Nanomechanical detection of antibiotic-mucopeptide binding in a model for superbug drug resistance.
Joseph W. Ndieyira,Moyu Watari,Alejandra Donoso Barrera,Dejian Zhou,Dejian Zhou,Manuel Vögtli,Matthew Batchelor,Mark E. Cooper,Torsten Strunz,Michael A. Horton,Chris Abell,Trevor Rayment,Gabriel Aeppli,Rachel A. McKendry +13 more
TL;DR: The label-free detection of vancomycin binding to bacterial cell wall precursor analogues (mucopeptides) on cantilever arrays is reported, with 10 nM sensitivity and at clinically relevant concentrations in blood serum, placing BioMEMS devices in a new class of percolative systems.
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Stable Single α-Helices Are Constant Force Springs in Proteins
TL;DR: Modeling and experiments show that SAH domains unfold non-cooperatively at low forces and maintain an approximately constant force as they unfold, which enables the SAH domain to act as a constant force spring in the mechanically dynamic environment of the cell.
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Nonexponential Kinetics of Loop Formation in Proteins and Peptides: A Signature of Rugged Free Energy Landscapes?
TL;DR: This work presents simulations, with different atomistic models, of short peptides with varied structural propensity, and of a structured protein, showing exponential contact formation kinetics at long times, and a power law relaxation at very short times.
Differential Effects of Hydrophobic Core Packing Residues for Thermodynamic and Mechanical Stability of a Hyperthermophilic Protein
Katarzyna M. Tych,Matthew Batchelor,Toni Hoffmann,Michael C. Wilson,Megan L. Hughes,Emanuele Paci,David J. Brockwell,Lorna Dougan +7 more
TL;DR: While the impact on the mechanical stability is subtle, the results demonstrate the power of tuning noncovalent interactions to modulate both the thermodynamic and mechanical stability of a protein.
Influence of the foundation layer on the layer-by-layer assembly of poly-L-lysine and poly(styrenesulfonate) and its usage in the fabrication of 3D microscale features.
TL;DR: LBL assembly of PLL and PSS on patterned TSG surfaces produced by micro contact printing leads to structurally distinct microscale features, including pillars, ridges and wells, whose height can be controlled with nanometer precision.
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