Experiment 11 is composed of cold liver and 2 mL H2O2. We anticipated that the reaction rate should be very low because a low temperature means a low reaction rate. At low temperatures, particles move slower and therefore there is a lower amount of collisions between the enzymes and the substrates. Based on observations, the reaction rate was fairly high which came as a surprise for us, this is not what we had anticipated. The reaction rate was given a 3.
Haemoglobin and myoglobin structures were discovered by Mark Perutz and John Kendrew and co-workers. Haemoglobin oxygen binding is cooperative. Cooperative is the binding of one ligand or substrate molecule that influences the affinity of the protein for additional molecules of the same substrate. The binding oxygen molecules to haemoglobin as a function to the oxygen pressure is sigmoidal, with relatively weak binding at low oxygen pressure. This is in contrast to myoglobin, which binds strongly at all oxygen levels.
Since propane is made up of 3 carbon atoms it has no single central bond that is present in the molecule. C3H8 is a linear molecule because of it not having that central atom to change the molecule angle. Being that the molecule is linear its angle bonds are 180 degrees. 2. Line angle drawings are organic chemists’ shorthand for depicting chains of atoms.
Moco is special derivative of pterin because of its four-carbon side chain that coordinates the metal via an enedithiolate group within the chain. (2) The catalytic role of Moco generally is to transfer an oxygen atom to and from a substrate (3) The reaction can be either a reduction or oxidation and includes the transfer of two electrons. This causes a change in the molybdenum oxidation state in the substrate-binding site. The change in oxidation state can go from IV to VI and also vice versa. Another unique part of molybdenum catalytic role is that the atom of molybdenum is not directly attached to the catalytic site but is within a certain low molecular scaffold.
Kirstie Javier AP Biology Period 4 November 14, 2011 Proteins Proteins are biochemical compounds consisting of one or more polypeptides typically folded into a globular or fibrous form, facilitating a biological function. Some types of chemical bonds/ interactions are disulfide bonds, hydrogen bonds, ionic bonds, and hydrophobic interactions. Disulfide bonds form when two cytosine molecules join together to form a bond between their two sulfur atoms. Such bonds cross-link polypeptide chains or parts of chains. Because they are nonpolar covalent bonds, they are very strong bonds and not easily broken.
Purines however are made of a six-sided ring joined to a five-sided ring. These rings are joined with hydrogen bonds and the bases in this group are adenine and guanine. This means that to make a base pairing a pyrimidine must bond with a purine. There are different numbers of bonds between the four bases, when adenine and thymine are joined there are only two hydrogen bonds, but when cytosine and guanine join there are three hydrogen bonds. Original DNA model by Watson and Crick.
RuBisCO has a catalytic rate of a few CO2 molecules per second at 25 °C 19. Besides it has a low affinity for atmospheric CO2 and uses O2 as an alternative substrate. For these reasons RuBisCO is an inefficient enzyme as the initial CO2-fixing enzyme for photosynthesis. Therefore, plants and algae must contribute a major part of their nitrogen to RuBisCO. The total soluble protein content inside the plants can comprise up to 50%20.
The most effective way to find peptide bonds, which join amino acids to form a protein, is by using Biuret reagent. In the presence of peptide bonds, Biuret reagent turns from blue to violet (Stallsmith). The greater the presence of peptide bonds, the darker the color of the solution will be. In
HSP60 family (chaperonins): resembles a cage and has a highly hydrophobic inner rim that attracts amino acids with exposed hydrophobic regions of an unfolded protein to bind to it. The inside of the cage is hydrophilic which the hydrophobic amino acids don’t work well with, therefore; the trapped molecule is forced to change shape to its correct conformation. HSP70 family: in contrast to HSP60 grab their substrates instead by the “elbow” so to speak to chaperone them along. HSP70 has a peptide-binding cleft which is open when HSP70 is bound to the ATP, as the ATP undergoes hydrolysis and becomes ADP the cleft closes and the polypeptide in the HSP70 is then folded to its correct conformation.
It also would have effect on the amount of toxins that build up in our body; this would lead to a reduction to the supply of respiratory substrate. Enzymes are specific, meaning they can only catalyse one or sometimes two reactions. A protein called the active site uses the same arrangement of amino acids which causes the specific shape. It is the small part of the enzyme where the substrate binds and where catalysis occurs. The substrate finds a place to bind within the enzymes 3D shape.