J-815 is a Circular Dichroism (CD) spectropolarimeter from JASCO. The J-815 is designed to measure CD in the UV/Vis region, and the instrument has two additional measurement modes.

Features:

• Light source: 150 W Xe arc lamp.
• Wavelength range: 163-900 nm.
• Standard modes: circular dichroism & UV/VIS absorbance.
• Optional modes: linear dichroism & fluorescence.
• Four-channel simultaneous data acquisition: 2 internal and and 2 external channels.
• Six-position Peltier cuvette holder for temperature-controlled measurements (thermal denaturation and cold effects).

JASCO recommends to use CDPro package for data analysis. It is available for download here. Unzip it to C:\CDPro directory and run index.html file.

Applications:

Overall secondary structure determination and melting curves of proteins and peptides. Below are selected publications:

• Fealey, ME, B Horn, C Coffman, R Miller, AY Lin, AR Thompson, J Schramel, E Groth, A Hinderliter, A Cembran, and DD Thomas. 2018. Dynamics of dystrophin’s actin-binding domain. Biophys J 115:1-10.
• Fealey, ME, BP Binder, VN Uversky, A Hinderliter, and DD Thomas. 2018. Structural impact of phosphorylation and dielectric constant variation on synaptotagmin’s IDR. Biophys J 114:550-561.
• Her, C, JE McCaffrey, DD Thomas*, and CB Karim*. 2016. Calcium-dependent structural dynamics of a spin-labeled ryanodine receptor peptide bound to calmodulin. Biophys J 111:2387-2394.
• Lin, AY, E Prochniewicz, ZM James, B Svensson, and DD Thomas. 2011. Large-scale opening of utrophin’s tandem calponin homology (CH) domains upon actin binding by an induced-fit mechanism. Proc Natl Acad Sci U S A 108:12729–12733. 
• Balog, EM, EL Lockamy, DD Thomas, and DA Ferrington. 2009. Site-specific methionine oxidation initiates calmodulin degradation by the 20S proteasome. Biochemistry 48:3005-3016.
• Balog, EM, LE Norton, RA Bloomquist, RL Cornea, DJ Black, CF Louis, DD Thomas, and BR Fruen. 2003. Calmodulin oxidation and methionine to glutamine substitutions reveal methionine residues critical for functional interaction with ryanodine receptor-1. J Biol Chem 278:15615-15621.
• Zhang, Z, HA Remmer, DD Thomas, and CB Karim. 2007. Backbone dynamics determined by electron paramagnetic resonance to optimize solid-phase peptide synthesis of TOAC-labeled phospholamban. Biopolymers 88:29-35.
• Zhang, J, BJ Wallar, CV Popescu, DB Renner, DD Thomas, and JD Lipscomb. 2006. Methane monooxygenase hydroxylase and B component interactions. Biochemistry 45:2913-2926.
• Paterlini, MG, and DD Thomas. 2005. The alpha-helical propensity of the cytoplasmic domain of phospholamban: a molecular dynamics simulation of the effect of phosphorylation and mutation. Biophys J 88:3243-3251.

Acknowledgements

The BTC should be acknowledged in any publications arising from the data analyzed in the BTC with the following text:

Experiments reported in this paper were performed at the Biophysical Technology Center, University of Minnesota Department of Biochemistry, Molecular Biology, and Biophysics.

Once published, please let us know via an email to umn-btc@umn.edu.

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