DNA consist of macromolecules which are; nitrogenous base, a phosphate sugar backbone and a pentose sugar. DNA has a double helical structure due to the coiling of two biopolymer strands. This double helix structure is made of nucleotides composed of either, thymine, guanine, cytosine or adenine, a monosaccharide(deoxyribose) and a phosphate group. Covalent bonds join the nucleotides together in a chain form. This is between the deoxyribose sugar of one nucleotide and the phosphate component of the other nucleotide, which brings about the alternating sugar phosphate backbone.All biological information is stored in DNA which makes every organism unique.
Eg. Ferritin. Nucleic Acids  Nucleic acids are known as genetic materials. They are macromolecules meaning that they are polymers of nucleotides (phosphate group, pentose sugar, and a nitrogenous base). Living matter is composed of nucleic acids in the form of deoxyribonucleic acid (DNA) or ribonucleic acid (RNA).
Sodium dodecyl sulfate polyacrylamide gel electrophoresis also known as SDS-PAGE is one of the methods for determining the molecular weight of unknown proteins. SDS is an anionic molecule which denaturizes proteins and brings it back to its’ primary structure and it also provides a negative charge to the uncharged molecule. The SDS-PAGE enables the separation of proteins based on their sizes. The larger the size of the protein, the harder it is to travel through the gel thus heavier proteins stay near the cathode side of the gel. For this experiment, a software named Gel Analyzer was used in order to obtain the molecular weight of the unknown proteins with the help of a protein ladder with known molecular weight and protein concentration.
Tannins Tannins are polyphenolic compounds that are broadly categorized into two major groups: 1. Condensed tannins, or proanthocyanidins, consisting of oligomers of two or more flavan-3-ols, such as catechin, epicatechin, or the corresponding gallocatechin. 2. Hydrolysable tannins, consisting of a central core of carbohydrate to which phenolic carboxylic acids are bound by ester linkage. Tannins have a very high affinity for proteins and form protein-tannin complexes.
Homologous recombination (HR) can be explained as a process where DNA is exchanged or copied between two chromosomes or different regions of the same chromosome. The process requires homology between the exchanging DNA regions. Homologous recombination repairs DNA breaks, especially double stranded breaks (DSBs), stabilizes and repairs stalled forks. HR consists of a series of inter related pathways that function in repair of DNA breaks (Figure 4). Initially, stretches of single stranded DNA (ssDNA) are resected at the stalled forks or DSB ends which are quickly bound by replication protein A (RPA).
The Cu1+ then react to bicinchoninic acid assay forming a purple water soluble complex. Moreover, the total volume of protein concentration can be measured by the colorimetric technique which will change the colour of sample solution from green to purple in proportion to protein concentration. SDS-PAGE electrophoresis Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE electrophoresis) is probably the most common analytical technique widely used to separate biological molecules, usually a nucleic acid or protein based on their electrophoretic mobility. The motility is a function of conformation, the length of their peptide chain and charge of the molecule. Depending on their size, small biomolecules move faster and more easily fit through the pores in the gel than larger ones.
The three things that can cause the enzyme to denature is a large change in pH level, High Temperature, and substrate concentration. According to our knowledge, we know that a large change in pH will cause instability in the protein structure thus resulting in denaturation of the enzyme. From the data, we can see that pH 3 (total:6.3) and 10 (total:6.2) were the slowest because pH 3 is probably the highest acid and pH 10 is the highest base. The highest acid or base pH represents a large change which would cause the enzyme to denature. The fastest pH was 6 (total:34.5), and it seems that there wasn’t a large change which resulted in a stable structure.
The amyloid fibrils are made up of amyloid fibrils which constitute 4-6 protofibrils and each protofibril contains several beta beta sheets and beta sheets are made up of beta strands which run antiparallel. These amyloids are the most stable aggregates which are very difficult to digest with the proteolytic enzymes so these are very difficult to target by these enzymes and these are very difficult to remove from the tissues where these aggregates are deposited. If these types of aggregates are formed in other tissues such as the tissues which are not the part of brain then these aggregates can be removed by surgically. However in case of Alzheimer there’s a gradual loss of neurons by the small toxic oligomers which are produced by the aggregation of these amyloid peptide and these oligomers cause the death of these neurons. Previously it was thought that these amyloid aggregates are extracellular but now it is clear that these aggregates can be formed intracellular or extracellular nearly all types of aggregations associated with degenerated disease.
Amino acids are the building blocks of proteins. All amino acids have the same basic structure but differ in their R-side chains. Each amino acid consists of an amino group (-NH3), a carboxyl group (-COOH) and a hydrogen atom (H). The amino and carboxyl groups are attached to a central alpha carbon together with a hydrogen atom and an R-side chain. There are currently known that over 170 amino acids occur in organisms but only 20 are commonly found in proteins.
There is a non-covalent interaction between four chains. The four heme groups provide four binding sites for oxygen (Marengo; 2006) As described by Max Perutz in 1959, the three dimensional structure of hemoglobin is similar to myoglobin but oxygen affinity in hemoglobin is more than that of myoglobin. Figure 1: Structure of Hemoglobin (http://www.infobiochem.com/2014/12/Hemoglobin-and-its-defects.html) Synthesis: This complex protein molecule is synthesized in series of steps, it begins with synthesis of d-aminolevulinic acid (ALA) and porphobilinogen and then modification of terapyroll ring. The synthesis of heme part involves enzymes of mitochondria and
1. How does DNA encode information? DNA is a double-stranded helix composed of a phosphate backbone and deoxyribose, and encodes information by the sequence of its nucleotide bases, which are composed of adenine, thiamine, guanine and cytosine. DNA undergoes transcription, which produces single-stranded mRNA, which uses uracil in place of thiamine. Next step is translation, in which the RNA becomes a protein, which then can act as structural units or enzymes.
The Solid sequencing platform, produced by Technologies/Applied Biosystems (ABI), performs sequencing by ligation method. Similar like the Roche 454 library preparation, genomic double strand DNA were sheared into small pieces and ligated with two types of adatptors P1 and P2 on two ends. One end with P1 adaptor binds onto the surface of the magnetic bead and emulsion PCR takes place to amplify single nucleotide fragment. Then the oil was washed out and four fluorescent labeled di-bases probes were added into the beads mixture. By matching the 1st and 2nd position of the template by di-base probes, fluorescence was detected and the extra tail with fluorescent probe is cleaved out.
The purpose of this experiment is to create a complete genomic library of Aliivibrio fisheri through the use of the lux operon. The examination of the lux operon gene occurs through the extraction of the DNA of Aliivibrio fischeri and digest a large piece of DNA to smaller random pieces. The fragment of DNA will later be ligated together in plasmid. Plasmid acts as vectors to transport DNA from one organism to another. The DNA will then run through a UV-visible spectrophotometer to test the absorbance of the extracted DNA.
Tertiary structure is the "worldwide" collapsing of a solitary polypeptide chain. A noteworthy main impetus in deciding the tertiary structure of globular proteins is the hydrophobic impact. The polypeptide chain overlap such that the side chains of the non-polar amino acids are "covered up" inside the structure and the side chains of the polar buildups are uncovered on the external surface. Hydrogen holding including bunches from both the peptide spine and the side chains are imperative in balancing out tertiary structure. The tertiary structure of a few proteins is balanced out by disulfide bonds between cysteine
DNA Restriction Mapping Danielle Niemeier firstname.lastname@example.org BCH 467 Analytical Biochemistry Lab Section: 16371 Abstract The purpose of this experiment was to determine whether the vector PRSETB or pQE30 is present and to create a restriction map for the unknown plasmid A. The plasmid A was digested with enzymes BAMH1, PstI, and ScaI and then the resulting fragments were run through an agarose gel via electrophoresis. From the gel electrophoresis and deriving an equation by plotting the log of the size of the DNA size markers and distance migrated, a restriction map was constructed. The restriction map showed that the plasmid has only one ScaI site, which supports that vector PRSETB, is present in the plasmid. From the gel electrophoresis, it