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Combining ns temperature-jump pump with X-ray pulse probe: study of structural dynamics in insulin

September 22, 2017

Biological functions frequently require protein–protein interactions that involve secondary and tertiary structural perturbation. Here we study protein–protein dissociation and reassociation dynamics in insulin, a model system for protein oligomerization. Insulin dimer dissociation into monomers was induced by a nanosecond temperature-jump (T-jump) of ∼8 °C in aqueous solution, and the resulting protein and solvent dynamics were tracked by time-resolved X-ray solution scattering (TRXSS) on time scales of 10 ns to 100 ms.

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New Technique Shocks Proteins Into Action

December 12, 2016

For a protein to carry out its job—whether it be replicating DNA, metabolizing fuel, transporting biomolecules, or sending cell signals—its amino acids have to move in certain ways. The patterns of these internal motions aren’t always well understood because the tools available to study them are limited.

A new technique, electric field-stimulated X-ray crystallography (EF-X), combines electric pulses with time-resolved X-ray crystallography to provide more comprehensive views of the ways proteins work. Electrical charges and dipoles are present in all proteins, and external electric fields can exert forces on them, causing atoms to move.

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In Situ Serial Laue Diffraction on a Microfluidic Crystallization Device

Journal of Applied Crystallography 47
November 18, 2014

Signal amplification and transduction in phytochrome photosensors

Takala et al, Nature 509, 245–248, 2014
May 8, 2014

Cell Death Versus Cell Survival Instructed by Supramolecular Cohesion of Nanostructures

Nature Communications 5, Article number: 3321
February 17, 2014