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Julien Roche

Researcher at Iowa State University

Publications -  55
Citations -  1621

Julien Roche is an academic researcher from Iowa State University. The author has contributed to research in topics: Protein folding & Hydrostatic pressure. The author has an hindex of 19, co-authored 45 publications receiving 1325 citations. Previous affiliations of Julien Roche include Rensselaer Polytechnic Institute & Centre national de la recherche scientifique.

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Journal ArticleDOI

Cavities determine the pressure unfolding of proteins

Julien Roche, +8 more
- 01 May 2012 - 
TL;DR: The promise of pressure perturbation is illustrated as a unique tool for examining the roles of packing, conformational fluctuations, and water penetration as determinants of solution properties of proteins, and for detecting folding intermediates and other structural details of protein-folding landscapes that are invisible to standard experimental approaches.
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Monomeric Aβ1–40 and Aβ1–42 Peptides in Solution Adopt Very Similar Ramachandran Map Distributions That Closely Resemble Random Coil

Julien Roche, +4 more
- 27 Jan 2016 - 
TL;DR: The results suggest that the self-association of Aβ peptides into toxic oligomers is not driven by elevated propensities of the monomeric species to adopt β-strand-like conformations, and suggests that intermolecular interactions between the hydrophobic regions of the peptide dominate the aggregation process.
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Homonuclear decoupling for enhancing resolution and sensitivity in NOE and RDC measurements of peptides and proteins.

Jinfa Ying, +2 more
- 01 Apr 2014 - 
TL;DR: Application of band-selective homonuclear (BASH) decoupling pulses during acquisition of the (1)H free induction decay is shown to be an efficient procedure for removal of scalar and residual dipolar couplings between amide and aliphatic protons.
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Size and Sequence and the Volume Change of Protein Folding

Jean-Baptiste Rouget, +7 more
- 20 Apr 2011 - 
TL;DR: Examination of the effects of protein size and sequence on the value of ΔV(u) using as a model system a series of deletion variants of the ankyrin repeat domain of the Notch receptor provides strong evidence in support of the notion that the major contributing factor to pressure effects on proteins is their imperfect internal packing in the folded state.
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Local unfolding of the HSP27 monomer regulates chaperone activity.

T. Reid Alderson, +10 more
- 06 Mar 2019 - 
TL;DR: While HSP27 assembles into oligomers, it is shown that the monomers formed upon reduction are highly active chaperones in vitro, but are susceptible to self-aggregation.