Greetings from Daedalus Innovations, the leading provider of state-of-the-art high pressure and reverse micelle NMR apparatus and supplies.
Our mission is to provide you with the leading edge tools to utilize high pressure in your NMR based studies. We are 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. High active volume coupled to high pressure tolerance opens a host of applications in areas as diverse as petroleum chemistry, structural biology and quantum computing. Our patented designs and proprietary manufacturing techniques place us in a truly unique position to enable your work with high-pressure NMR.
Leveraging our expertise in high pressure NMR, 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. With applications in soluble and membrane protein NMR and protein and nucleic acid biophysics, reverse micelle NMR is seeing a growing cadre of users and enthusiasts. Daedalus Innovations is the sole source of a complete line of instruments used in this uniquely powerful methodology.
More recently, Daedalus Innovations has entered a new arena of high pressure NMR applications - the so-called overburdened cell that is critical to analysis of rock cores derived from petroleum exploration. 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.
Announcements & News
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