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The schematic diagram indicates the roles of insufficient DNA repair in aging and cancer, and the role of apoptosis in cancer prevention. An excess of naturally occurring DNA damage, due to inherited deficiencies in particular DNA repair enzymes, can cause premature aging or increased risk for cancer (see DNA repair-deficiency disorder).
The HD gene [8] is found in all human genomes. In the event that a slippage event occurs there can be a large expansion in the tandem repeats of the HD gene. [8] An individual who is not affected by Huntington's disease will have 6-35 tandem repeats at the HD locus. However, an affected individual will have 36- 121 repeats present. [7]
In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]
Structure of the base-excision repair enzyme uracil-DNA glycosylase excising a hydrolytically-produced uracil residue from DNA. The uracil residue is shown in yellow. When only one of the two strands of a double helix has a defect, the other strand can be used as a template to guide the correction of the damaged strand.
Many allergies are caused by the incorrect folding of some proteins because the immune system does not produce the antibodies for certain protein structures. [5] Denaturation of proteins is a process of transition from a folded to an unfolded state. It happens in cooking, burns, proteinopathies, and other contexts. Residual structure present ...
The phage gene 52 protein shares homology with the bacterial gyrase gyrA subunit [18] and the phage gene 39 protein shares homology with the gyrB subunit. [19] Since the host E. coli DNA gyrase can partially compensate for the loss of the phage gene products, mutants defective in either genes 39, 52 or 60 do not completely abolish phage DNA ...
The crystal structure of MutS reveals that it is exceptionally asymmetric, and, while its active conformation is a dimer, only one of the two halves interacts with the mismatch site. In eukaryotes, M ut S h omologs form two major heterodimers: Msh2 /Msh6 (MutSα) and Msh2 /Msh3 (MutSβ).
Neomorphic mutations are a part of the gain-of-function mutations and are characterized by the control of new protein product synthesis. The newly synthesized gene normally contains a novel gene expression or molecular function. The result of the neomorphic mutation is the gene where the mutation occurs has a complete change in function. [57]