A new look at the human Rad51 protein

Cox, Michael M.

doi:10.1073/pnas.0906816106

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Structural Analysis Of Proteins Measured By Linear Dichroism1

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2016

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Cited by 2 publications

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“…Rad51 is a protein involved in repair of double-strand breaks in DNA in eukaryotic cells (Baumann and West 1998 ). Rad51 and RecA form extended filaments on DNA and promote the DNA strand exchange in recombinant DNA repair (Cox 2009 ). Combining molecular modeling with LD of the human Rad51-dsDNA-ATP complex in solution (HsRad51-dsDNA-ATP), Nordén et al (Reymer et al 2009 ) proposed a model corresponding to the final product of the recombination reaction.…”

Section: Structural Analysis Of Proteins Measured By Linear Dichroismmentioning

confidence: 99%

UV–Vis spectroscopy of tyrosine side-groups in studies of protein structure. Part 2: selected applications

2016

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In Part 2 we discuss application of several different types of UV–Vis spectroscopy, such as normal, difference, and second-derivative UV absorption spectroscopy, fluorescence spectroscopy, linear and circular dichroism spectroscopy, and Raman spectroscopy, of the side-chain of tyrosine residues in different molecular environments. We review the ways these spectroscopies can be used to probe complex protein structures.

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Section: Structural Analysis Of Proteins Measured By Linear Dichroismmentioning

confidence: 99%