Tertiary structure has a three-dimensional structure, which is from non-covalent contact between the amino acids. Lastly, quaternary structures form into one larger protein because of non-covalent interactions that combine many polypeptides together. The three-dimensional shape of a protein is determined by its primary structure. The way the amino acids are lined up makes a protein 's structure and specific function. The instructions for the order of amino acids are made by the genes in an organisms cell.
However, certain ribonucleic acid (RNA) molecules can also be biological catalysts, forming ribozymes. A very important example of a ribozyme is the ribosome, a large assembly of proteins and catalytically active RNA molecules responsible for the synthesis of proteins in the cell. The structure of the active site is specific to the reaction that it catalyzes, with groups in the substrate
The microtubules are polar structure i.e. the beta-tubulin is exposed at the minus end and alpha- tubulin towards the plus end and the polymerization is three times faster at the plus end than that of the minus end in vitro. The minus end of the microtubule is embedded inside the centrosome and the plus end directed outwards. Centrosome and basal body are the microtubule organizing centre (MTOC), where nucleation of microtubule occurs. In plant and fungi, microtubule organizing centre is called as Spindle Pole Body (SPB).
• Mild or even moderate phenylketonuria : Phenylalanine tolerance can range from 250 to 400 mg per day. THE PHENYLALANINE HYDROXYLASE (PAH) ENZYME : The human phenylalanine enzyme is expressed in liver as well as in the kidney. This enzyme is involved in the conversion of phenylalanine to tyrosine. The phenylalanine hydroxylase enzyme has two forms among which tetrameric form is active and dimeric form is inactive. Additionally, there exists three domains of the enzyme namely C- terminal catalytic domain, an N- terminal regulatory domain and a tetramerization domain.
INTRODUCTION: DNA as well as Proteins are very essential macromolecules for any living cell. They are involved in various bio-molecular function, hence very essential for any living being. DNA protein interaction is one of the key biological function in a living cell. This type of interaction is happened during replication, transcription, translation, recombination, DNA repair, etc. DNA is a negatively charged macro molecule.
However, different molecules will move at quite different and individual rates depending on the physical characteristics of the molecule and on experimental system used. The velocity of movement, ν, of a charged molecule in an electric field depends on variables described by Eq/ f • Nucleic acid molecules are size separated by the aid of an electric field where negatively charged molecules travel toward anode (positive) pole. The migration flow is resulted solely by the molecular weight where small weight molecules migrate faster than larger ones. In addition to size separation, nucleic acid fractionation using agarose gel electrophoresis can be an initial step for further purification of a band of interest. Extension of the technique includes expunging the desired “band” from a stained gel viewed with a UV transilluminator.
The movement of the endocytosed protein which is destined for the apical surface to fuse with and also the movement of extracellular materials from one side of the epithelial cells to another can be termed as transcytosis. With respect to concept, transcytosis can be grouped into three processes namely; endocytosis, exocytosis and transcellular transport (Pravda,2011). Though transcytosis is tightly controlled by the cell it also has the potential for transepithelial movement of bacteria and other pathogens, hence it sometimes becomes an etiologic factor in the body(Pravda,2011). Trancytosis occurs in hepatocytes and this phenomenon is a typical example of transcellular transport . Here the apical membrane form bile and the basolateral membrane face blood.
They are proteins that are complexly folded to allow smaller molecules to fit into them; this active site is where substrate molecules bind. Enzymes must collide with one another at a precise position with enough activation energy. The active site must bind to the reacting molecule, or the substrate (1). Enzyme-catalyzed reactions require lower activation energy. The activity of an enzyme is affected by its environmental factors, and any change results in an alteration in the rate of the reaction caused by the enzyme (2).
Active transport requires chemical energy because it is the movement of biochemicals from areas of lower concentration to areas of higher concentration. On the other hand, passive trasport moves biochemicals from areas of high concentration to areas of low concentration; so it does not require energy. 3. Difference between endocytosis and exocytosis Exocytosis ‘“ the process by which a cell expels molecules and other objects that are too large to pass through the cellular membraneEndocytosis ‘“ the process by which a cell takes in molecules and other objects that are too large to pass through the cellular membrane 1. Endocytosis brings molecules into a cell while exocytosis takes molecules out of a cell.2.
pruriens seed extract and FeMPn were characterized with FTIR to determine the biomolecules contained in the extract that involved in the reaction to form FeMPn. The FTIR spectra of the extract and FeMPn are shown in Fig. 5. The FTIR spectrum of the extract showed a broad absorption band in an absorbance area of 3384.8 cm-1 that assigned to the overlapping of O-H stretching vibration of flavonoids, alkaloids, polyphenols, alcohols or water and N-H stretching vibration of amine compounds, due to the hydrogen bonding. The absorption band at 1627.8 cm-1 referred to C=C stretching vibration which is possible to be derived from aromatic ring in amino acid, while the absorption band in 1529.4 cm-1 referred to N-H bending vibration of amine which is possible to be derived from the L-dopa.
The Diverse Parts of Macromolecules in Science There are four sorts of macromolecules that I am going to portray: Proteins, starches, lipids and nucleic corrosive. I will likewise depict the capacities and why they are critical in our bodies. Proteins Proteins are polymers of amino acids that are joined head-to-tail in a long chain that is then collapsed into a three-dimensional structure one of a kind to every sort of protein. The covalent linkage between two contiguous amino acids in a protein (or polypeptide) chain is known as a peptide bond. There are twenty amino acids that make up proteins.
It is an analytical method where in a protein sample is electrophoresis on an SDS- PAGE and electro transferred on the nitrocellulose membrane. The transferred protein is detected using specific primary enzymes labeled antibody. Antibodies bind to specific sequences of amino acids, known as the epitope. Because amino acid sequences are different from protein to protein, antibodies can recognize specific proteins among a group of many. Therefore, a single protein can be identified in a cell lysate that contains thousands of different proteins and its abundance quantified through western blot
Steered molecular dynamics (SMD) simulation has been used to apply external force on certain atoms in specific pulling direction in silico, which is perfect for pulling the knotted proteins. Sułkowska et al have stretched 20 proteins with a knotted topology by SMD simulations using a coarse-grained model. (105) When a stretching force is applied onto the two ends of a knotted protein, the knot shrinks and one end of the knot move along the polypeptide chain with sudden jumps. This is quite different from the tightening of a homopolymer in which the knot