This is a P41 renewal proposal to continue the National Biomedical Center for Advance ESR Technology (ACERT). Four principal areas of Technology Research and Development (TR&D) will be emphasized. They consist of 1) High-Sensitivity Pulse Dipolar ESR Spectroscopy and 2D-FT ESR from X to Ka Band; 2) Electron Spin Resonance with Ultra-High Sensitivity for Very Small Biological Samples; 3) Developments in High Frequency ESR, and 4) Improved Computational Methods for ESR Analysis and Spectral Processing. Extensive Driven Biomedical Projects and other collaborations with biomedical researchers will greatly benefit from these TR&Ds, which in turn are driven by the DBP needs for the new and improved ESR technologies. Thus, there is an important synergism amongst the TR&Ds and the DBPs. The technologies being developed at ACERT are in many respects unique in the world. The extensive DBP's and collaborative/service projects at ACERT will continue to bring these modern ESR methods to the forefront of biomedical research, especially as the additional challenges are addressed in the TR&D's. This includes our plans to increase spectral sensitivity in our ACERT spectrometers, for which the demands continue to grow. The plans for dissemination and training address the need to bring these new technologies to other laboratories in the USA and elsewhere in addition to making the facilities available to outside scientists, publishing and advertising the results of the Center and running workshops on the new methodologies.
This BTRR supports several NIH sponsored projects aimed at understanding and combating diseases and ailments (e.g., AIDS, allergies and inflammations, ALS, Alzheimer's, bacterial infection, cancer, cardiac disease, depressive disorders and schizophrenia, Ebola viral infections, eye disorders, infertility, neurological disorders, Parkinson's, SARS, and Wernicke Encephalopathy) by studying their key proteins' structure and functional mechanisms.
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|Meirovitch, Eva; Liang, Zhichun; Freed, Jack H (2018) Protein dynamics in the solid-state from 2H NMR lineshape analysis. III. MOMD in the presence of Magic Angle Spinning. Solid State Nucl Magn Reson 89:35-44|
|Lengyel, Zsófia; Rufo, Caroline M; Moroz, Yurii S et al. (2018) Copper-Containing Catalytic Amyloids Promote Phosphoester Hydrolysis and Tandem Reactions. ACS Catal 8:59-62|
|Usery, Rebecca D; Enoki, Thais A; Wickramasinghe, Sanjula P et al. (2018) Membrane Bending Moduli of Coexisting Liquid Phases Containing Transmembrane Peptide. Biophys J 114:2152-2164|
|Zhang, Yiren; Park, Albert; Cintora, Alicia et al. (2018) Impact of the Synthesis Method on the Solid-State Charge Transport of Radical Polymers. J Mater Chem C Mater 6:111-118|
|Srivastava, Madhur; Freed, Jack H (2018) Singular Value Decomposition Method to Determine Distance Distributions in Pulse Dipolar Electron Spin Resonance: II. Estimating Uncertainty. J Phys Chem A :|
|Selmke, Benjamin; Borbat, Peter P; Nickolaus, Chen et al. (2018) Open and Closed Form of Maltose Binding Protein in Its Native and Molten Globule State As Studied by Electron Paramagnetic Resonance Spectroscopy. Biochemistry 57:5507-5512|
|Riederer, Erika A; Focke, Paul J; Georgieva, Elka R et al. (2018) A facile approach for the in vitro assembly of multimeric membrane transport proteins. Elife 7:|
|Vilbert, Avery C; Caranto, Jonathan D; Lancaster, Kyle M (2018) Influences of the heme-lysine crosslink in cytochrome P460 over redox catalysis and nitric oxide sensitivity. Chem Sci 9:368-379|
|Merz, Gregory E; Borbat, Peter P; Muok, Alise R et al. (2018) Site-Specific Incorporation of a Cu2+ Spin Label into Proteins for Measuring Distances by Pulsed Dipolar Electron Spin Resonance Spectroscopy. J Phys Chem B 122:9443-9451|
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