activity
20142022
most citedForce-dependent switch in protein unfolding pathways and transition state movements

68 citations · 147 across the 8 of their papers we have counts for

collaborators

8 papers

cs.CR2022★ 10 cited

Bayesian and Frequentist Semantics for Common Variations of Differential Privacy: Applications to the 2020 Census

Daniel Kifer, John M. Abowd, Robert Ashmead +5

The purpose of this paper is to guide interpretation of the semantic privacy guarantees for some of the major variations of differential privacy, which include pure, approximate, R…

cs.CR2022★ 4 cited

Geographic Spines in the 2020 Census Disclosure Avoidance System

Ryan Cumings-Menon, John M. Abowd, Robert Ashmead +5

The 2020 Census Disclosure Avoidance System (DAS) is a formally private mechanism that first adds independent noise to cross tabulations for a set of pre-specified hierarchical geo…

cs.CR2021★ 4 cited

An Uncertainty Principle is a Price of Privacy-Preserving Microdata

John Abowd, Robert Ashmead, Ryan Cumings-Menon +7

Privacy-protected microdata are often the desired output of a differentially private algorithm since microdata is familiar and convenient for downstream users. However, there is a…

cond-mat.soft2020

Low force unfolding of a single-domain protein by parallel pathways

Pavel I. Zhuravlev, Michael Hinczewski, D. Thirumalai

Deviations from linearity in the dependence of the logarithm of protein unfolding rates, , as a function of mechanical force, , measurable in single molecule experi…

cond-mat.soft2018

Symmetry, Rigidity, and Allosteric Signaling: From Monomeric Proteins to Molecular Machines

D. Thirumalai, Changbong Hyeon, Pavel I. Zhuravlev +1

Allosteric signaling in biological molecules, which may be viewed as specific action at a distance due to localized perturbation upon binding of ligands or changes in environmental…

q-bio.BM2016

Protein Collapse is Encoded in the Folded State Architecture

Himadri S. Samanta, Pavel I. Zhuravlev, Michael Hinczewski +3

Natural protein sequences that self-assemble to form globular structures are compact with high packing densities in the folded states. It is known that proteins unfold upon additio…

cond-mat.soft2015★ 68 cited

Force-dependent switch in protein unfolding pathways and transition state movements

Pavel I. Zhuravlev, Michael Hinczewski, Shaon Chakrabarti +2

Although known that single domain proteins fold and unfold by parallel pathways, demonstration of this expectation has been difficult to establish in experiments. Unfolding rate, $…

cond-mat.soft2014★ 61 cited

Propensity to form amyloid fibrils is encoded as excitations in the free energy landscape of monomeric proteins

Pavel I. Zhuravlev, Govardhan Reddy, John E. Straub +1

Protein aggregation, linked to many of diseases, is initiated when monomers access rogue conformations that are poised to form amyloid fibrils. We show, using simulations of src SH…