About

Professor Lori Goldner leads research in the Goldner Research Lab at the Department of Physics, UMass Amherst, specializing in single molecule biophysics. Her group focuses on the use of optical techniques for physical and spectroscopic measurements on single molecules in biophysical and polymeric systems. The lab's work emphasizes biophysical applications, including the study of protein folding, RNA interactions, and molecular dynamics, as well as polymer science topics such as transport, flow, and phase transitions. They employ a variety of single-molecule-sensitive measurement techniques, including fluorescence, nonlinear spectroscopies, electronic measurements, and force measurements using optical or magnetic tweezers or microcantilevers. The lab also utilizes superresolution microscopy facilities such as PALM/STORM for advanced imaging.

Research topics

• Materials science
• Chemistry
• Physics
• Optics
• Nanotechnology

Selected publications

• The Nanomechanics of Cellulose Synthesis

  Bulletin of the American Physical Society · 2019-03-04

  article1st authorCorresponding
  Publisher

• Evidence of a Transition from Diffusive to Super-Diffusive Motion of Cellulose Synthase Complexes in Living Plants

  Biophysical Journal · 2017-02-01

  articleOpen accessSenior author
  PublisherOA PDFDOI

• Imaging cellulose synthase motility during primary cell wall synthesis in the grass Brachypodium distachyon

  Scientific Reports · 2017-11-03 · 14 citations

  articleOpen access

  Abstract The mechanism of cellulose synthesis has been studied by characterizing the motility of cellulose synthase complexes tagged with a fluorescent protein; however, this approach has been used exclusively on the hypocotyl of Arabidopsis thaliana . Here we characterize cellulose synthase motility in the model grass, Brachypodium distachyon . We generated lines in which mEGFP is fused N-terminal to BdCESA3 or BdCESA6 and which grew indistinguishably from the wild type (Bd21-3) and had dense fluorescent puncta at or near the plasma membrane. Measured with a particle tracking algorithm, the average speed of GFP-BdCESA3 particles in the mesocotyl was 164 ± 78 nm min −1 (error gives standard deviation [SD], n = 1451 particles). Mean speed in the root appeared similar. For comparison, average speed in the A. thaliana hypocotyl expressing GFP-AtCESA6 was 184 ± 86 nm min −1 (n = 2755). For B. distachyon , we quantified root diameter and elongation rate in response to inhibitors of cellulose (dichlorobenylnitrile; DCB), microtubules (oryzalin), or actin (latrunculin B). Neither oryzalin nor latrunculin affected the speed of CESA complexes; whereas, DCB reduced average speed by about 50% in B. distachyon and by about 35% in A. thaliana . Evidently, between these species, CESA motility is well conserved.

  PublisherOA PDFDOI

• On the pH of Aqueous Attoliter-Volume Droplets

  Bulletin of the American Physical Society · 2016-03-16

  articleSenior author
  Publisher

• Mechanics of Cellulose Synthase Complexes in Living Plant Cells

  Bulletin of the American Physical Society · 2016-03-18

  article
  Publisher

• Observation of an angular change in the structure of an RNA complex using Fluorescence Resonance Energy Transfer

  Bulletin of the American Physical Society · 2016-03-18

  articleSenior author
  Publisher

• Observation of a Change in Twist of an RNA Kissing Complex Using the Angular Dependence of Fluorescence Resonance Energy Transfer

  Biophysical Journal · 2015-01-01

  articleOpen accessSenior author
  PublisherOA PDFDOI

• Single-Molecule-Sensitive FRET in Freely-Diffusing Attoliter Droplets

  Biophysical Journal · 2015-01-01 · 1 citations

  articleOpen accessSenior author
  PublisherOA PDFDOI

• Single-molecule-sensitive fluorescence resonance energy transfer in freely-diffusing attoliter droplets

  Applied Physics Letters · 2015-05-11 · 4 citations

  articleOpen accessSenior author

  Fluorescence resonance energy transfer (FRET) from individual, dye-labeled RNA molecules confined in freely-diffusing attoliter-volume aqueous droplets is carefully compared to FRET from unconfined RNA in solution. The use of freely-diffusing droplets is a remarkably simple and high-throughput technique that facilitates a substantial increase in signal-to-noise for single-molecular-pair FRET measurements. We show that there can be dramatic differences between FRET in solution and in droplets, which we attribute primarily to an altered pH in the confining environment. We also demonstrate that a sufficient concentration of a non-ionic surfactant mitigates this effect and restores FRET to its neutral-pH solution value. At low surfactant levels, even accounting for pH, we observe differences between the distribution of FRET values in solution and in droplets which remain unexplained. Our results will facilitate the use of nanoemulsion droplets as attoliter volume reactors for use in biophysical and biochemical assays, and also in applications such as protein crystallization or nanoparticle synthesis, where careful attention to the pH of the confined phase is required.

  PublisherOA PDFDOI

• Observation of Global Changes in Conformation of an RNA Kissing Complex using Single-Molecular-Pair FRET

  Biophysical Journal · 2014-01-01

  articleOpen accessSenior author
  PublisherOA PDFDOI

Recent grants

• The Nanomechanics of Cellulose and Cellulose Synthesis

  NSF · $485k · 2012–2017

• Capturing the Ephemeral: Transient and Irreversible RNA-protein Interactions Studied one-at-a-time

  NSF · $553k · 2009–2013

• IDBR: Nanodroplet reactor arrays and imaging system for biomolecular structure and kinetics

  NSF · $509k · 2012–2016

Frequent coauthors

• Kristian Helmerson

  Monash University

  18 shared

• Rani Kishore

  17 shared

• Jeeseong Hwang

  National Institute of Standards and Technology

  17 shared

• Jianyong Tang

  Xi'an Jiaotong University

  17 shared

• Ana Jofré

  National University of San Luis

  16 shared

• Peker Milas

  16 shared

• Mark E. Greene

  15 shared

• S. L. Rolston

  15 shared