Proteins are formed through condensation reactions which bond amino acids together with peptide bonds in a particular sequence and the type of protein that is created is defined by the unique sequence of the amino acids. DNA and RNA are nucleic acids that are formed in the nucleotides and are both involved in the process of protein synthesis. Deoxyribonucleic acid, more commonly known as DNA, is located within the nucleus of the cell and contains the entire genetic code for an organism within its structure. DNA has two very important functions which are: to convey information from one generation of cells to the next by the process of DNA replication and to provide the information for the synthesis of proteins necessary for cellular function. Basically, DNA controls protein synthesis.
Through a series of condensation reactions, many amino acid monomers can be joined together in a process called polymerisation, resulting in a polypeptide. The sequence of amino acids in a polypeptide chain forms the primary structure of any protein. This primary structure determines the ultimate shape and hence the function of the protein. The secondary structure is the shape which the polypeptide chain forms as a result of hydrogen bonding. This is most often an alfa-helix or beta-pleated sheet.
These charged molecules combine with oxygen and produce ATP molecules. This process is known as oxidative phosphorylation. Ribosomes: the ribosomes are the cellular component that make proteins from all amino acids. Ribosomes are made from complexes of RNAs and proteins.They assemble amino acids to form specific proteins, proteins are essential to carry out cellular activities. Rough endoplasmic reticulum: The surface of the rough endoplasmic reticulum is studded with the protein manufacturing ribosome, which gives it a rough appearance.The rough
Secondary structure & amino acids Proteins are large macromolecules which are made up of a long chain of amino acids. The naturally occurring amino acids have a common structure. Amino acids, as the name implies, have two functional groups, an amino group (–NH2) and a carboxyl group (–COOH). These groups are joined to a single (aliphatic) carbon. In organic chemistry, the carbon directly attached to a carboxyl group is the alpha (α) position, so the amino acids in proteins are all alpha-amino acids.
These proteins consist of macromolecules which are polymers consisting of one or more chains that are un-branched from monomers that are called amino acids. This molecule consists of both an amino and a carboxyl group. Proteins can contain from as few as three to fifty-thousand amino acid units and range from shape and form, to being completely soluble or insoluble to water solutions. When a protein is formed it is linked together by a peptide bond using covalent bonds to form between an amino group of one amino acid and a carboxyl group. Similarly dipeptides are formed when the peptide bond joins the two amino acids.
The primary structure is unique to a given protein. The primary structure can fold regularly to form either an α-helix or β-pleated sheet. The secondary structure is held together by hydrogen bonds between adjacent peptide bonds. The primary structure can further fold to form an overall three dimensional shape that more specifically determines the biological functions of the individual protein. This 3D structure is held together by bonds formed between the R-groups of amino acids.
Each genome contains the information needed to maintain and create the organism. The process of genetic engineering involves extracting of a small piece of cellular DNA, called a plasmid, from the bacteria if organism involved in the manipulation. A very small section of the circular plasmid is then cut out by the restriction enzymes which act as molecular scissors. The gene from the organism being modified is then inserted into this space and the plasmid is therefore modified. The genetically modified plasmid is now inserted and introduces into a new organism which starts divides rapidly.
As this bonds are the ones that join the individual amino acid residues in a protein the biuret reagent can effectively confirm the presence of protein in a substance. A polypeptide is a single linear polymer chain from the condensation of amino acids.. The sequence of amino acid residues in a protein is defined by the sequence of a gene, which is encoded in the genetic code. In general, the genetic code specifies 20 standard amino acids. There are seven main groups of proteins, this groups are: structural proteins, storage proteins, defensive proteins, transport proteins, signal proteins, contractile proteins, and enzymes.
Describe the induced fit model of enzyme action. Also, describe at least four factors that modify the action of enzymes: The cycle of the induced fit model of enzyme action starts with the enzyme molecule, made from amino acids chained together by bonds such as hydrogen, inside a cell. This long chain folds into a special shape that will allow a very specific chemical reaction to happen. The reactant molecules in the cell are called substrates, these bind to a pocket in the enzyme called the active site. According to the induced fit model, substrates are not always the same shape of the active site.
Enzymes called topoisomerases produce breaks in the DNA molecules and then reconnect the strands, relieving strain and effectively preventing tangling and knotting during replication. DNA polymerase adds new nucleotides to a growing strand of DNA. Because DNA polymerase must adhere to an existing template, an RNA primer is first created at the site of replication. The RNA primer is synthesized by primase, an enzyme that is able to start a new strand of RNA opposite a DNA strand. After a few nucleotides have been added, the primase is displaced by DNA polymerase, which can then add subunits to the 3’ end of the short RNA primer.