2008
DOI: 10.1016/j.jinorgbio.2008.02.007
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Characteristic differences in the X-ray photoelectron spectrum between B-DNA and M-DNA monolayers on gold

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Cited by 18 publications
(18 citation statements)
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“…The principal N 1s core-level peak consists of two-component structure for DNA with BE of 400.8 and 399.3 eV, respectively, consistent with published results [55]. The higher energy peak is attributed to amino N sites connected with single bonds, and the peak at the lower BE is assigned to imino species that include a double N=C bond.…”
Section: Resultssupporting
confidence: 87%
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“…The principal N 1s core-level peak consists of two-component structure for DNA with BE of 400.8 and 399.3 eV, respectively, consistent with published results [55]. The higher energy peak is attributed to amino N sites connected with single bonds, and the peak at the lower BE is assigned to imino species that include a double N=C bond.…”
Section: Resultssupporting
confidence: 87%
“…Thus, the C 1s spectra exhibit features uniquely due to the different contributions of carbon species in the bulk sample. The XPS C 1s spectrum of oligo shows faithful agreement with the previously reported single-strand DNA [55]. From the convoluted peak areas of the different carbon species, the percentage of corresponding 1–4 carbon components is found to change from 7.13%, 17.73%, 38.19%, and 36.95%, to 3.18%, 15.24%, 29.77%, and 51.18%, respectively, with the ratio of cisplatin to oligo increasing from 0 to 10.…”
Section: Resultssupporting
confidence: 87%
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“…666 X-ray photoelectron spectroscopy has been used to study the effect of charging the imino nitrogen atoms of thymine and guanine with metal ions in basic pH. 844 A variety of structures have been examined using EM. These include the formation of Holliday junctions in the RecA homologues Rhp51 and hRad51, 845 C. Elegans telomeric DNA bound to the single-stranded DNA binding proteins CeOB1 and CeOB2, 846 DNA binding to the bacteriophage P22 Terminase small subunit, 847 binding of the bacterial actin-like proteins ParR and parC, 848 the structure of the U4/U6 small ribonucleoprotein (snRNP) complex 849 and the origin recognition complex (ORC) from S. cerevisiae.…”
Section: Other Structural Methodsmentioning
confidence: 99%