NMR study of parallel-stranded tetraplex formation by the hexadeoxynulceotide d(TG4T)

Article Abstract:

The structure of chromosome telomeres and the process of immunoglobulin class switching may depend upon guanine-associated multi-stranded DNA structures. Using nuclear magnetic resonance spectroscopy the structure of the d(TG4T) hexadeoxynucleotide was observed to form a parallel-stranded quadruplex structure in the presence of sodium ions. This quadruplex contains hydrogen-bonded guanine tetrads. The fold-back form which has been previously described differs significantly from the parallel-stranded form.

Nucleotides, Deoxyribonucleotides, Deoxynucleotides

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Applying a genetic cantilever

Article Abstract:

Understanding the solution structure of a DNA and DNA-binding domain of SRY complex is essential for the molecular interpretation of mutations which are responsible for the clinical effects. SRY is a DNA-binding protein determining the male gender in mammals and affiliated with abnormal sexual development. A mutation that incorporates an isoleucine residue lowers the specificity of the DNA target and causes DNA deformation.

Mutation (Biology), Mutation, Structure-activity relationships (Biochemistry), DNA binding proteins, DNA-ligand interactions, DNA binding

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HMG has DNA wrapped up

Article Abstract:

The high-mobility group protein (HMG) domain has been found to have a major effect on the bending and looping of DNA that is essential to genetic transcription. K. Giese and colleagues have determined that HMG1, as a part of the transcription factor LEF-1 or lymphoid enhancer factor, can turn a strand of DNA back on itself. Further research is needed to determine the extent of HMG1's control over DNA structure.

DNA, Proteins, Genetic transcription, Transcription (Genetics)

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