J. E. Straub

Synergistic computational and experimental studies of a phosphoglycosyltransferase membrane/ligand ensemble

This study combines computational and experimental approaches to investigate the interaction of undecaprenol phosphate with the phosphoglycosyltransferase PglC from Campylobacter, revealing insights into substrate recognition and binding mechanisms.

Sizes, conformational fluctuations, and SAXS profiles for Intrinsically Disordered Proteins

This paper develops a transferable model to predict biophysical properties of IDPs, showing agreement with experimental data on size, conformation, and SAXS profiles.

Energy landscapes of Aβ monomers are sculpted in accordance with Ostwald's rule of stages

The paper shows that N* states in Aβ40 and Aβ42 monomers follow Ostwald's rule of stages, influencing aggregation and dimer formation.

Sequence Determines the Switch in the Fibril Forming Regions in the Low-Complexity FUS Protein and Its Variants

The paper shows that sequence determines the fibril-forming structure in FUS-LC and its variants, with core-1 forming more readily than core-2.

Differences in the free energies between the excited states of Aβ40 and Aβ42 monomers encode their distinct aggregation propensities

This paper explains the faster aggregation rate of Aβ42 compared to Aβ40 by showing that their distinct populations of high free energy excited states encode their aggregation propensities.

Sequence effects on size, shape, and structural heterogeneity in Intrinsically Disordered Proteins

This study uses simulations to analyze how sequence and length affect the structural properties of intrinsically disordered proteins, showing sequence-dependent conformational heterogeneity despite polymer-like scaling behavior.

Regimes of Complex Lipid Bilayer Phases Induced by Cholesterol Concentration in MD Simulation.

This study uses MD simulations to show cholesterol induces three distinct phase behaviors in ternary lipid mixtures.

Structure of APP-C991-99 and Implications for Role of Extra-Membrane Domains in Function and Oligomerization

This study investigates the structure of APP-C99 in model membranes, revealing how extra-membrane domains influence Aβ oligomerization and γ-secretase processing.