Hemoglobin Synthesis Lab Report

When the pH is not at its optimum, the differing pH's will disrupt the bonding between the R groups of the amino acid causing its structure and the shape of the activation site to change

Since the side chains are bonded to ions in solution, they are unavailable to bond with each other. This lack of bonding amongst the side chains effects the tertiary structures of the protein, changing its shape. The tertiary structure is important because for an enzyme to work, it must have a very specific shape to fit, lock and key style, onto the substrate. As the substrate and enzyme bind the shape of the substrate molecule slightly bends. This strains the bonds of the substrate, allowing them to be broken easy.

1. There are ~280 million Hb molecules in one RBC. A single Hb molecule carries ___ molecule(s) of O2, which means that a single RBC carries about ___ O2 molecules.

The amino acid structures found in living cells from planet Mehcoib will be identical to the ones from the Earth. However, there will be different patterns of protein folding due to the affected hydrophobic interaction, which is important in tertiary and quaternary proteins structures. In this interaction, since water molecules are hydrophilic (polar), they do not place close to hydrophobic molecules. As a result of this lack of surrounding hydrophobic molecules, hydrophobic parts of proteins will not be incorporated with hydrophilic solutions and usually placed in the inner core of proteins. In the planet Mehcoib where heptane has replaced water, hydrophobic interactions will happen differently because of this replacement. Since heptane is non-polar molecule, it acts as a hydrophobic molecule. In living cells from the planet Mehcoib, heptane molecules will place closely to hydrophobic molecules and carry them as a part of solution. However, it will keep distant from hydrophilic molecules; as a result, hydrophilic parts of proteins will be placed in the inner core part of proteins. There also will be the lack of the hydrogen bonds that result from two water molecules placed next to each other and form non-covalent linkage. Thus, the presence of heptane instead of water in the planet Mehcoib will not change proteins' primary and secondary structures, but

The genes for haemoglobin behave exactly as predicted by Mendel’s Law of Inheritance. A child must inherit one haemoglobin

It is with these free coordination sites of the metal that the proteins, acting as Lewis bases, will interact with and bind to the metal chelate to form a metal-protein complex. In IMAC, the interaction of the electron donating group, Lewis base, on the surface of a protein and the accessible coordination sites from the metal ion, interact which results in the binding of proteins to metal ions. (Nes, 1999) Certain amino acids exposed on the protein’s surface are responsible for the binding. Histidine has the strongest affinity for metal ions while tryptophan and cysteine are also involved in the binding of proteins in IMAC. The strong metal affinity of these amino acids can be attributed to their functional groups: thiol in cysteine, indoyl in tryptophan and imdizole in histidine. Binding of the protein product to an IMAC resin is specific for the amino acid targeted by the affinity ligand. This general binding mechanism is attributed to the interaction of the amino acid group and the affinity ligand. The affinity ligand does not possess the ability to discriminate between multiplicities of the target amino acid and therefore will bind proteins containing single and multiple

The position of His57 is assisted by Asp102. Ser195 becomes a powerful nucleophile that attacks the carbonyl carbon of the target protein in a nucleophilic attack. A tetrahedral intermediate is formed, stabilised by the presence of an Oxyanion Hole that forms hydrogen bonds with the negatively charged oxygen atom above the serine residue. It is usually made up of positively charged amines, such as Gly193. The tetrahedral intermediate then collapses and the acyl-enzyme is formed, resulting in the release of an amine.

Normally, humans have haemoglobin A2, haemoglobin A and haemoglobin F. Out of these three types, haemoglobin F dominates initially for upto 6 weeks. Later, haemoglobin A dominates through life. Hemoglobin consists of two subunits of alpha-globin and two subunits of beta-globin. Various versions of beta-globin result from different mutations in the HBB gene. One HBB gene mutation produces an abnormal version of beta-globin known as hemoglobin S (HbS). Other mutations in the HBB gene lead to additional abnormal versions of beta-globin such as hemoglobin C (HbC) and hemoglobin E (HbE). HbS contains alpha-globin and mutated beta-globin. It carries oxygen perfectly well but when deoxygenated, it changes its shape. This will damage the cell membrane. The type of

Finally, when both beta globin genes are mutant, we denote the presence of homozygous beta thalassaemia( thalassaemia major) which is considered as the most serious case. Indeed, people in this condition have haemoglobin entirely constituted of alpha globin

Investigating haemoglobin (Hb) concentration in blood samples using the haemoglobincyanide method and in foetal haemoglobin samples

This suggests that the orange colony was due to contamination, indicating that there was an error in the experimental procedure used. The team results indicate no protein-protein interaction between the strain Bub1B (328-1052) and any of the four potential interactors. These results differ from those produced by the class for the strain Bub1B (328-1052), which instead indicate protein-protein interactions occurring between the Bub1B protein and BUB3 as well as Bub1B and Ppp2rc, for the strain Bub1B (328-1052).

This experiment was completed in order to test the dependability of agarose gel electrophoresis on identifying normal (HbA) and mutant (HbS) β-globin in blood protein samples. The procedure of native gel electrophoresis was utilized, because normal and mutant β-globin have negative and positive charges, respectively. The samples in the agarose gel were exposed to an electric field inside the agarose gel apparatus for one hour. Our samples included purified normal hemoglobin, purified sickle trait hemoglobin, and purified sickle hemoglobin, a student sample, and an unknown. The migration of each sample informed us of the intrinsic charge of the hemoglobin proteins.

Hb consists of 4 globin polypeptide chains (tertiary structure of 2 alpha globin chains and two beta globin chains), of which each has an attached prosthetic haem group. This haem group consists of 4 pyrroles linked by methane bridges. Each pyrrole is bound to a central Fe2+ ion. Fe2+ is capable of forming 6 bonds, 4 bonds are formed

When the normal hemoglobin amino acid glutamic alter to amino acid valine that leads to mutation in hemoglobin known as hemoglobin (Hb S) which cause sickle cell anemia. The substitution leads to abnormalities in the structure and function of hemoglobin. Unlike normal hemoglobin, Hb S has a hydrophobic patch on the exterior surface of the protein; these hydrophobic regions make the molecules of the protein joining to each other and form rigid chain of insoluble polymers. Polymerization happen only in deoxygenated Hb S, after RBCs released the oxygen. These insoluble polymers change the shape of RBCs into sickle shape which make them fragile. Sickled RBCs lose their flexibility, and they will become sticky. As a result, it will stick in the

Campbell and Farrell define proteins as polymers of amino acids that have been covalently joined through peptide bonds to form amino acid chains (61). A short amino acid chain comprising of thirty amino acids forms a peptide, and a longer chain of amino acids forms a polypeptide or a protein. Each of the amino acids making up a protein, has a fundamental design that comprises of a central carbon or alpha carbon that is bonded to a hydrogen element, an amino grouping, a carboxyl grouping, and a unique side chain or the R-group (Campbell and Farrell 61).