Direct observation of steps in rotation of the bacterial flagellar motor

Nature 437 (2005) 916-919

Authors:

RM Berry, Leake MC, Rowe AD, Sowa Y

Rapid chiral assembly of rigid DNA building blocks for molecular nanofabrication.

Science 310:5754 (2005) 1661-1665

Authors:

RP Goodman, IAT Schaap, CF Tardin, CM Erben, RM Berry, CF Schmidt, AJ Turberfield

Abstract:

Practical components for three-dimensional molecular nanofabrication must be simple to produce, stereopure, rigid, and adaptable. We report a family of DNA tetrahedra, less than 10 nanometers on a side, that can self-assemble in seconds with near-quantitative yield of one diastereomer. They can be connected by programmable DNA linkers. Their triangulated architecture confers structural stability; by compressing a DNA tetrahedron with an atomic force microscope, we have measured the axial compressibility of DNA and observed the buckling of the double helix under high loads.

Torque-generating units of the flagellar motor of Escherichia coli have a high duty ratio.

Nature 403:6768 (2000) 444-447

Authors:

WS Ryu, RM Berry, HC Berg

Abstract:

Rotation of the bacterial flagellar motor is driven by an ensemble of torque-generating units containing the proteins MotA and MotB. Here, by inducing expression of MotA in motA- cells under conditions of low viscous load, we show that the limiting speed of the motor is independent of the number of units: at vanishing load, one unit turns the motor as rapidly as many. This result indicates that each unit may remain attached to the rotor for most of its mechanochemical cycle, that is, that it has a high duty ratio. Thus, torque generators behave more like kinesin, the protein that moves vesicles along microtubules, than myosin, the protein that powers muscle. However, their translation rates, stepping frequencies and power outputs are much higher, being greater than 30 microm s(-1), 12 kHz and 1.5 x 10(5) pN nm s(-1), respectively.

Towards a perfusion system for functional study of membrane proteins with independent control of the electrical and chemical transmembrane potential

Biophysical Reviews Springer Nature (2025) 1-9

Authors:

Zuzana Coculova, Richard M Berry

Abstract:

The main motivation of this work was to address the challenge of single-molecule functional study of membrane proteins under stable and independently controlled electrical and chemical membrane potentials. Although transmembrane potential is often essential for the function of membrane proteins, current in vitro systems provide only limited options for studying them under biologically relevant conditions. Our experimental assay is based on the droplet-on-hydrogel bilayer technique (Leptihn et al. Nat Protoc 8:1048–1057, 2013), where a lipid bilayer forms between a sub-millimetre water droplet and a thin hydrogel layer on a glass cover slip, enabling high-resolution microscopy in total internal reflection mode. To extend the application of this assay beyond channels to other membrane proteins, we introduce a custom-built, electronically controlled perfusion system that is designed to directly connect to the droplet above the lipid bilayer. This system can supply a stable voltage to the bilayer and is suitable for delivery of fragile membrane proteins embedded in proteoliposomes via charged fusion (Ishmukhametov et al. Nat Commun 7:13025, 2016), introducing changes of chemical potentials, and timed introduction of labels or substrate into the droplet. This work represents one of the steps towards single-molecule functional study of F1Fo ATP synthase under variable transmembrane potentials. High-resolution single-molecule observation of its rotation steps on the microsecond timescale could provide valuable insights into the mechanisms of energy transport across the molecule.

Redshift tomography of the kinematic matter dipole

Physical Review D American Physical Society (APS) 111:12 (2025) 123547

Authors:

Sebastian von Hausegger, Charles Dalang

Abstract:

The dipole anisotropy induced by our peculiar motion in the sky distribution of cosmologically distant sources is an important consistency test of the standard Friedmann-Lemaître-Robertson-Walker cosmology. In this work, we formalize how to compute the kinematic matter dipole in redshift bins. Apart from the usual terms arising from angular aberration and flux boosting, there is a contribution from the boosting of the redshifts that becomes important when considering a sample selected on observed redshift, leading to nonvanishing correction terms. We discuss examples and provide expressions to incorporate arbitrary redshift selection functions. We also discuss the effect of redshift measurement uncertainties in this context, in particular in upcoming surveys for which we provide estimates of the correction terms. Depending on the shape of a sample’s redshift distribution and on the applied redshift cuts, the correction terms can become substantial, even to the degree that the direction of the dipole is reversed. Lastly, we discuss how cuts on variables correlated with observed redshift, such as color, can induce additional correction terms. Published by the American Physical Society 2025