Site-directed mutagenesis is a method used to construct amino acid changes in a protein in order to test the function of a specific amino acid. It is the way to study protein structure and function change the amino acid sequence of a protein by altering the DNA sequence of cloned gene4. A particular amino acid is very important in catalytic activity, ligand binding, protein folding or other function. Amino acid residue significance is tested by making conservative substitutions or by changing the
TPP1 is identified as a bridge protein in the shelterin where it binds with POT1 with the PBD, and bind with TIN2 with its CTD-CC22 domain. The interaction between TPP1 and other shelterin protein is revealed using the Oxytricha Nova telomere end binding proteins (TEBP). In O. Nova, TEBP has two heterodimers TEBP-α and TEBP-β that cap the ends of the chromosomes [13]. The TEBP-α is the homologue unit of the human POT1demostrates similar sequence to mammalian POT1 protein [15]. The TEBP-β unit homologous
discovered the interactions between molecules and proteins within the cell that inhibit or stop the body’s ability to repair DNA damage over time. As the body ages, its ability to repair DNA gradually declines and that loss leads to bodily degeneration and a higher risk for cancer, the uncontrolled and abnormal growth of cells that don’t undergo apoptosis or cell death. This discovery is important to the scientific and medical community because it identifies the main players in the protein bindings and
eukaryotes and their viruses. Some of the properties that make yeast suitable for studies include the existence of both stable haploids and diploids, rapid growth, clonability, and the ease of replica plating and mutant isolation. The development of DNA transformation has made yeast particularly accessible to gene cloning and genetic engineering techniques. Plasmids can be introduced into yeast cells either as replicating molecules
to form the shape of DNA. The 4 different types of covalent bonds are: electrostatic interactions, hydrogen bonds, van der Waals interactions, and hydrophobic interactions. They are very different in their strength, specificity, geometry, and the way they are affected by water. Electrostatic interactions occur when a charged group on one molecule interacts with an oppositely charged group on a different molecule. Coloumb’s law gives the energy of an electrostatic interaction in the following equation:
of a protein that interacts with the EccA1, another virulence factor mains unknown. ("W1 Mycobacterium Secretion: Background Information” 2005) The overall objective of the project is to identify the proteins that interact with EccA1 using a yeast two-hybrid assay test and to characterize the particular regions of the proteins that interact. The TB DNA was isolated from a PCR colony to be used as a template for a PCR reaction. An agarose gel was created and used for electrophoresis of the DNA. A UV
importance of RNA-protein interactions in essential biological processes, there is still only a small number of RNA-protein complexes with high resolution three dimensional structures compared to other biomolecules. In this study, we investigate RNA nucleotide base-amino acid residue interactions by counting contacts in the helical and backbone regions. Contact frequency data from non-redundant RNA-protein complexes is used to estimate relative potential energy of interactions that will be used
Origin of replication is the starting point of DNA replication. It cannot replicate in the host cells without this site. Antibiotic resistance gene can be served as a select agent to find the right clone and then improve the plasmid transformation efficiency. Antibiotic resistance gene can also give the bacteria a pressure to have the plasmid, because the bacteria would use more energy to replicate both the plasmid and its own DNA. (1) The protein needs complex eukaryotic post-translational modifications
control expression of DNA at the level of transcription is vital for cells not only to have the correct proteins expressed when they are needed, but also to save on resources and energy by only making proteins and RNA needed at the correct time, rather than beginning the process of expressing DNA and degrading the results later on. Though there are several different ways that DNA transcription can be controlled, histone deacetylation is the one focused on in the Vershon lab. DNA, which has a negative
water in the surrounding. This arrangement reduces the free-energy of protein folding by burying the hydrophobic residues in the interior of the protein, while exposing the hydrophilic residues to the water containing environment and thereby, stabilizing the coiled-coil structure. Q37. The α helices of the leucine zipper motif can recognize and bind to DNA specifically, providing a scaffold for interaction of proteins with DNA. Q38. The coiled coil structure contains approximately 3.5 residues