Welcome to Daedalus Innovations

Daedalus Innovations is the leading provider in the state for high pressure and reverse micelle NMR apparatus and supplies.

Our Mission

We offer leading edge tools to utilize high pressure in NMR based studies. High active volume coupled with high pressure tolerance opens a host of applications in areas as diverse as petroleum chemistry, structural biology and quantum computing.

Daedalus Innovations is the only provider of seamlessly integrated pressure generation and robust large active volume high resolution NMR cells rated to operation at pressures as high as 3 kbar.

We are also the world leaders in the development of the apparatus necessary to implement the “reverse micelle encapsulation strategy” for solution NMR studies of biological macromolecules.

Our Designs

Daedalus Innovations has entered a new arena of high pressure NMR/MRI applications with the development of a biaxial overburden cell that is critical to analysis of rock cores derived from petroleum exploration. The Daedalus cell offers the highest pressure and temperature performance, and works for NMR and MRI applications.

We have just introduced a revolutionary new rock core cell that offers superior pressure and temperature capabilities in a remarkably easy to use patent pending design.

Our patented designs and proprietary manufacturing techniques place us in a truly unique position. We can now enable your work with high pressure NMR.

The Daedalus Innovations’ high pressure NMR cells are truly a class by themselves.

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News & Announcements

We have expanded!

Daedalus Innovations has added a new site in ASTON, PENNSYLVANIA. This is our new home for development and manufacturing.

Daedalus Innovations Introduces a Revolutionary Rock Core Cell

Our new ceramic overburden cells promise to greatly extend the pressure and temperature ranges accessible for wide-line NMR analysis of the properties of rock cores.

Don’t think you can make a solution of encapsulated proteins?

Try our new REVERSE MICELLE DEMONSTRATION KIT. You will be amazed how easy it really is!

Daedalus Innovations in the Journals!

Wand and coworkers have used high-pressure NMR relaxation techniques to expose cooperative motion in proteins. Check it out: Fu et al. (2012) Journal of the American Chemical Society 134:8543−8550. PMID: 22452540

Valente and coworkers use high-pressure NMR to assist in understanding the structural and energetic basis for epitope definition in a fish protein that is connected to a major human allergen. Check it out: Moraes et al. (2014) Proteins 82:3032–3042.

Roumestand and coworkers and Fu and Wand demonstrate the ability to carry out partial alignment of proteins to obtain residual dipolar couplings (RDC) under high pressure. Check it out: Sibelle et al. (2014) J Biomol NMR 58:9–16 and Fu & Wand. (2013) J Biomol NMR 56:353–357.

Royer and coworkers have used high-pressure NMR to investigate the role of internal voids in the stability of proteins to applied hydrostatic pressure, helping to resolve a long-standing paradox noted by Kauzmann. Check it out: Roche et al. (2012) Proceedings of the National Academy of Sciences USA 111:13846-13851.

Kalbitzer and coworkers use high-pressure NMR to explore the free energy landscape of the Alzheimers' Abeta peptide. Check it out: Munti et al. (2013) Angewandte Chemie International Edition 52:8943 –8947.

Schwalbe and coworkers use high-pressure NMR to explore structural plasticity of the important human kinase p38alpha. Check it out: Nielsen et al. (2013) ChemBioChem 14:1799 – 1806.

Wand and coworkers use high-pressure NMR to explore the hydration of internal hydrophobic cavities in proteins. Check it out: Nucci et al. (2014) Proceedings of the National Academy of Sciences USA 82:3032–3042.

Jaszunski and coworkers have used high-pressure NMR to examine the effect of weak intermolecular forces on NMR shielding. Check it out: Garbacz et al. (2011) Journal of Chemical Physics 135, 084310

Kalbitzer and coworkers have calibrated the response of backbone 1 bond J-couplings in amino acids to high-pressure and thereby provide an important reference standard. Check it out: Koehler et al. (2014) J. Biomol. NMR 60:45–50.

Kitahara and coworkers find they are able to populate a minor structural species of ubiquitin at high presssure that coresponds to the structure adopted in a protein complex. Check it out: Kitazawa et al. (2014) Biochemistry 53:447−449.

Kalbitzer and coworkers have calibrated the response of backbone chemical shifts in amino acids to high-pressure and thereby provide an important reference standard for local structural changes. Check it out: Erlach et al. (2014) J. Physical Chemistry B 118:5681−5690.

Wand and coworkers have shown how reverse micelle encapsulation can be used to study protein hydration. Check it out: Nucci et al. (2011) Nature Structural & Molecular Biology 18, 245-249. PMID: 2119693

Nisius and Grzesiek have used high-pressure NMR examine the energetics of hydrogen bonding in proteins. Check it out: Nisius and Grzesiek (2012) Nature Chemistry 4:711–717.