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|Title:||Molecular recognition in G-quadruplexes : from G-tetrad formation to protein binding||Authors:||Cheong, Vee Vee||Keywords:||DRNTU::Science::Chemistry::Biochemistry::Spectroscopy||Issue Date:||2014||Source:||Cheong, V. V. (2014). Molecular recognition in G-quadruplexes : from G-tetrad formation to protein binding. Doctoral thesis, Nanyang Technological University, Singapore.||Abstract:||Under physiological conditions, guanine-rich oligonucleotides may assemble into a four-stranded structure, the G-quadruplex. G-quadruplexes may cause genomic instability in cells, requiring modulation by proteins. As guanine-rich DNA is susceptible to DNA damage, a G-quadruplex with complementary 8-oxoguanine-xanthine mutation was characterized. Its structure resolved in K+ highly resembles the wild-type G-quadruplex. In contrast, the non-complementary arrangement of 8-oxoguanine and xanthine within a G-tetrad inverts the polarity of the modified tetrad. We demonstrated Rhau53-105 to preferentially bind parallel G-quadruplexes, and identified residues 53–70 (Rhau18) as the determinant G-quadruplex binding region. We present the solution structure of a G-quadruplex bound with peptide, and identified hydrophobic, stacking and electrostatic interactions between the two biomolecules. BLM is a RecQ helicase that selectively resolves G-quadruplexes. The RQC domain (BLMRQC) is highly soluble and the solution structure of BLMRQC adopts a winged-helix motif. BLMRQC binds DNA weakly and requires the zinc-binding domain for tight G-quadruplex binding.||URI:||https://hdl.handle.net/10356/65412||DOI:||10.32657/10356/65412||Fulltext Permission:||open||Fulltext Availability:||With Fulltext|
|Appears in Collections:||SPMS Theses|
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|[2014.Cheong, Vee Vee]Molecular recognition in G-quadruplexes From G-tetrad formation to protein binding.pdf||PhD thesis||10.48 MB||Adobe PDF|
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