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Full-Text Articles in Physical Sciences and Mathematics

Multi-Frequency Ferromagnetic Resonance Investigation Of Nickel Nanocubes Encapsulated In Diamagnetic Magnesium Oxide Matrix, Saritha Nellutla, Sudhakar Nori, Srinivasa R. Singamaneni, John T. Prater, Jagdish Narayan, Alix I. Smirnov Jan 2016

Multi-Frequency Ferromagnetic Resonance Investigation Of Nickel Nanocubes Encapsulated In Diamagnetic Magnesium Oxide Matrix, Saritha Nellutla, Sudhakar Nori, Srinivasa R. Singamaneni, John T. Prater, Jagdish Narayan, Alix I. Smirnov

Chemical Sciences Faculty Publications

Partially aligned nickel nanocubes were grown epitaxially in a diamagnetic magnesium oxide (MgO:Ni) host and studied by a continuous wave ferromagnetic resonance (FMR) spectroscopy at the X-band (9.5 GHz) from ca. 117 to 458 K and then at room temperature for multiple external magnetic fields/resonant frequencies from 9.5 to 330 GHz. In contrast to conventional magnetic susceptibility studies that provided data on the bulk magnetization, the FMR spectra revealed the presence of three different types of magnetic Ni nanocubes in the sample. Specifically, three different ferromagnetic resonances were observed in the X-band spectra: a line 1 assigned to large nickel …


Polymerase Manager Protein Umud Directly Regulates Escherichia Coli Dna Polymerase Iii Α Binding To Ssdna, Kathy R. Chaurasiya, Clarissa Ruslie, Michelle C. Silva, Lukas Voortman, Philip Nevin, Samer Lone, Penny J. Buening, Mark C. Williams Jan 2013

Polymerase Manager Protein Umud Directly Regulates Escherichia Coli Dna Polymerase Iii Α Binding To Ssdna, Kathy R. Chaurasiya, Clarissa Ruslie, Michelle C. Silva, Lukas Voortman, Philip Nevin, Samer Lone, Penny J. Buening, Mark C. Williams

Chemical Sciences Faculty Publications

Replication by Escherichia coli DNA polymerase III is disrupted on encountering DNA damage. Consequently, specialized Y-family DNA polymerases are used to bypass DNA damage. The protein UmuD is extensively involved in modulating cellular responses to DNA damage and may play a role in DNA polymerase exchange for damage tolerance. In the absence of DNA, UmuD interacts with the α subunit of DNA polymerase III at two distinct binding sites, one of which is adjacent to the single-stranded DNA-binding site of α. Here, we use single molecule DNA stretching experiments to demonstrate that UmuD specifically inhibits binding of α to ssDNA. …


Structure Of Human Dna Polymerase Κ Inserting Datp Opposite An 8-Oxog Dna Lesion, Rodrigo Vasquez-Del Carpio, Timothy D. Silverstein, Samer Lone, Michael K. Swan, Jayati R. Choudhury, Robert E. Johnson, Satya Prakash, Louise Prakash, Aneel K. Aggarwal Jan 2009

Structure Of Human Dna Polymerase Κ Inserting Datp Opposite An 8-Oxog Dna Lesion, Rodrigo Vasquez-Del Carpio, Timothy D. Silverstein, Samer Lone, Michael K. Swan, Jayati R. Choudhury, Robert E. Johnson, Satya Prakash, Louise Prakash, Aneel K. Aggarwal

Chemical Sciences Faculty Publications

Background: Oxygen-free radicals formed during normal aerobic cellular metabolism attack bases in DNA and 7,8-dihydro-8-oxoguanine (8-oxoG) is one of the major lesions formed. It is amongst the most mutagenic lesions in cells because of its dual coding potential, wherein 8-oxoG(syn) can pair with an A in addition to normal base pairing of 8-oxoG(anti) with a C. Human DNA polymerase κ (Polκ) is a member of the newly discovered Y-family of DNA polymerases that possess the ability to replicate through DNA lesions. To understand the basis of Polκ's preference for insertion of an A opposite 8-oxoG lesion, …