Quan Wang

University of Strathclyde

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W. E. Moerner

Stanford University

Hugh D. Wilson

NOAA National Marine Fisheries Service

Samuel Bockenhauer

Stanford University

Zhenya Zang

University of Strathclyde

David Li

University of Strathclyde

Gabriela S. Schlau‐Cohen

Massachusetts Institute of Technology

Dong Xiao

Hubei Water Resources Research Institute

Yu Chen

University of Strathclyde

Fan Xia

Nanjing Agricultural University

Xiaoding Lou

China University of Geosciences

Cooperative Institutions

Chinese Academy of Sciences

University of Chinese Academy of Sciences

Stanford University

Xi'an Institute of Optics and Precision Mechanics

University of Strathclyde

University of California, Berkeley

Huazhong University of Science and Technology

Shandong Academy of Agricultural Sciences

Chinese Academy of Agricultural Sciences

Harvard University

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Single-molecule diffusometry reveals the nucleotide-dependent oligomerization pathways ofNicotiana tabacumRubisco activase

bioRxiv (Cold Spring Harbor Laboratory) (2017)

Quan Wang Andrew J. Serban Rebekka M. Wachter W. E. Moerner

ABSTRACT Oligomerization plays an important role in the function of many proteins, but a quantitative picture of the oligomer distribution has been difficult to obtain using existing techniques. Here we describe a method that combines sub-stoichiometric labeling and recently-developed single-molecule diffusometry to measure the size distribution of oligomers under equilibrium conditions in solution, one molecule at a time. We use this technique to characterize the oligomerization behavior of Nicotiana tabacum (Nt) rubisco activase (Nt-Rca), a chaperone-like, AAA-plus ATPase essential in regulating carbon fixation during photosynthesis. We directly observed monomers, dimers and a tetramer/hexamer mixture, and extracted their fractional abundance as a function of protein concentration. We show that the oligomerization pathway of Nt-Rca is nucleotide dependent: ATPγS binding strongly promotes tetramer/hexamer formation from dimers and results in a preferred tetramer/hexamer population for concentrations in the 1-10μM range. Furthermore, we directly observed dynamic assembly and disassembly processes of single complexes in real time, and from there estimated the rate of subunit exchange to be ~0.1s -1 with ATPγS. On the other hand, ADP binding destabilizes Rca complexes by enhancing the rate of subunit exchange by >2 fold. These observations provide a quantitative starting point to elucidate the structure-function relations of Nt-Rca complexes. We envision the method to fill a critical gap in defining and quantifying protein assembly pathways in the small-oligomer regime.

Random hexamer

Tetramer

Oligomer

10.1101/191742

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Citations (1)

Optimal strategy for trapping single fluorescent molecules in solution using the ABEL trap

Applied Physics B (2009)

Quan Wang W. E. Moerner

Trap (plumbing)

Position (finance)

10.1007/s00340-009-3843-y

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Citations (77)

Dual-signal electrochemical sensor based on Cu-MOF and MnCO₃ for ultra-sensitive detection of mercury ions in water

Electrochimica Acta (2025)

Xue Bai Liyin Bu Yongqiang Du Quan Wang

Mercury

Electrochemical gas sensor

10.1016/j.electacta.2024.145636

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An FPGA-based Anti-Brownian Electrokinetic trap for studying single molecules in solution

Quan Wang Alexandre Fuerstenberg Samuel Bockenhauer W. E. Moerner

We have designed and implemented an Anti-Brownian ELectrokinetic (ABEL) trap on an FPGA platform, with programmable feedback algorithms and online tunable trapping parameters. Trapping of sub-10nm biomolecules for seconds in buffer is achieved.

Trap (plumbing)

Biomolecule

10.1364/ls.2009.lstuf3

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Towards High-performance Deep Learning Architecture and Hardware Accelerator Design for Robust Parameters Analysis in Diffuse Correlation Spectroscopy

Computer Methods and Programs in Biomedicine (2024)

Zhenya Zang Quan Wang Mingliang Pan Yuanzhe Zhang Xi Chen

10.1016/j.cmpb.2024.108471

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Tetherless, Precise and Extended Observation of Single-Molecule FRET in an Anti-Brownian Trap

Biophysical Journal (2019)

Hugh D. Wilson Quan Wang

Single-molecule FRET

Millisecond

Biomolecule

Photon Counting

10.1016/j.bpj.2018.11.254

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An Adaptive Anti-Brownian Electrokinetic Trap with Real-Time Information on Single-Molecule Diffusivity and Mobility

ACS Nano (2011)

Quan Wang W. E. Moerner

We present the design and implementation of an adaptive Anti-Brownian ELectrokinetic (ABEL) trap capable of extracting estimates of the diffusion coefficient and mobility of single trapped fluorescent nanoscale objects such as biomolecules in solution. The system features rapid acousto-optic scanning of a confocal excitation spot on a 2D square lattice to encode position information on the arrival time of each detected photon, and Kalman filter-based signal processing unit for refined position estimation. We demonstrate stable trapping of multisubunit proteins (D ≈ 22 μm(2)/s) with a count rate of 6 kHz for as long as 15 s and small single-stranded DNA molecules (D ≈ 118 μm(2)/s) at a 15 kHz count rate for seconds. Moreover, we demonstrate real-time measurement of diffusion coefficient and electrokinetic mobility of trapped objects, using adaptive tuning of the Kalman filter parameters.

Biomolecule

Position (finance)

10.1021/nn2014968

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Citations (90)

ABEL-FRET: tether-free single-molecule FRET with hydrodynamic profiling

Nature Methods (2021)

Hugh D. Wilson Quan Wang

Single-molecule FRET

Biomolecule

Single-molecule experiment

Molecular biophysics

10.1038/s41592-021-01173-9

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Citations (42)

ZmFdC2 Encoding a Ferredoxin Protein With C-Terminus Extension Is Indispensable for Maize Growth

Frontiers in Plant Science (2021)

Yue Chen Deyi Zhong Xiu Yang Yonghui Zhao Liping Dai

As important electron carriers, ferredoxin (Fd) proteins play important roles in photosynthesis, and the assimilation of CO 2 , nitrate, sulfate, and other metabolites. In addition to the well-studied Fds, plant genome encodes two Fd-like protein members named FdC1 and FdC2, which have extension regions at the C-terminus of the 2Fe-2S cluster. Mutation or overexpression of FdC genes caused alterations in photosynthetic electron transfer rate in rice and Arabidopsis. Maize genome contains one copy of each FdC gene. However, the functions of these genes have not been reported. In this study, we identified the ZmFdC2 gene by forward genetics approach. Mutation of this gene causes impaired photosynthetic electron transport and collapsed chloroplasts. The mutant plant is seedling-lethal, indicating the indispensable function of ZmFdC2 gene in maize development. The ZmFdC2 gene is specifically expressed in photosynthetic tissues and induced by light treatment, and the encoded protein is localized on chloroplast, implying its specialized function in photosynthesis. Furthermore, ZmFdC2 expression was detected in both mesophyll cells and bundle sheath cells, the two cell types specialized for C4 and C3 photosynthesis pathways in maize. Epigenomic analyses showed that ZmFdC2 locus was enriched for active histone modifications. Our results demonstrate that ZmFdC2 is a key component of the photosynthesis pathway and is crucial for the development of maize.

10.3389/fpls.2021.646359

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Citations (7)

Dissecting pigment architecture of individual photosynthetic antenna complexes in solution

Proceedings of the National Academy of Sciences (2015)

Quan Wang W. E. Moerner

Significance Energy from the sun is captured by the biosphere through photosynthetic antenna proteins, which function by integration of a set of pigments into a protein scaffold. Nature uses relatively similar pigment building blocks to achieve diverse functions, and the organizing principles behind this process are not fully understood. Using a single-molecule microfluidic trap and multiparameter fluorescence spectroscopy, we explore how the photophysical properties of individual pigment sites are modulated by the protein’s oligomerization states, using single proteins of a model antenna from cyanobacteria. Our measurements achieve a bottom-up dissection of the structural-function relation of the model pigment−protein complex with important implications for photosynthetic antenna biophysics.

Photosynthetic pigment

10.1073/pnas.1514027112

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Citations (46)