activity
20062023
most citedHigh-precision gigahertz-to-terahertz spectroscopy of aqueous salt solutions as a probe of the femtosecond-to-picosecond dynamics of liquid water

118 citations · 123 across the 5 of their papers we have counts for

collaborators

5 papers

physics.bio-ph2023★ 1 cited

Modular DNA origami-based electrochemical detection of DNA and proteins

Byoung-jin Jeon, Matteo M. Guareschi, Jaimie M. Stewart +7

The diversity and heterogeneity of biomarkers has made the development of general methods for single-step quantification of analytes difficult. For individual biomarkers, electroch…

q-bio.QM2018★ 3 cited

A topological study of protein folding kinetics

E. Panagiotou, K. W. Plaxco

Focusing on a small set of proteins that i) fold in a concerted, all-or-none fashion and ii) do not contain knots or slipknots, we show that the Gauss linking integral, the torsion…

physics.chem-ph2015★ 118 cited

High-precision gigahertz-to-terahertz spectroscopy of aqueous salt solutions as a probe of the femtosecond-to-picosecond dynamics of liquid water

N. Q. Vinh, Mark S. Sherwin, S. James Allen +3

Because it is sensitive to fluctuations occurring over femtoseconds to picoseconds, gigahertz-to-terahertz dielectric relaxation spectroscopy can provide a valuable window into wat…

physics.bio-ph2009★ 1 cited

Influence of Local and Residual Structures on the Scaling Behavior and Dimensions of Unfolded Proteins

Zhisong Wang, Kevin W. Plaxco, Dmitrii E. Makarov

Although recent spectroscopic studies of chemically denatured proteins hint at significant nonrandom residual structure, the results of extensive small angle X-ray scattering studi…

q-bio.BM2006

Cooperativity and the origins of rapid, single-exponential kinetics in protein folding

P. F. N. Faisca, K. W. Plaxco

The folding of naturally occurring, single domain proteins is usually well-described as a simple, single exponential process lacking significant trapped states. Here we further exp…