The competitive inhibitor that was added was lactose. We predicted this because competitive inhibitors block and bind to the active site so it will slow down the binding of the desired substrate. An alternative hypothesis that came up was that the reaction of substrate would stay consistent as if no inhibitor was added. The enzyme could reject the inhibitor if it does not fit in the active site, causing the substrate to bind as it normally would. Our results showed that with the addition of lactose, the reaction did slow down a considerably
Cycloheximide applies its impact by interfering with the translocation steps in protein synthesize (development of two tRNA atoms and mRNA in connection to the ribosome), hence blocking translational prolongation. Cycloheximide is generally utilized as a part of biomedical research to repress protein synthesize in eukaryotic cells except for S.aureus and E.coli contemplated in vitro (i.e. outside of microorganism). It is cheap and works quickly. Actually after the interaction of 72 hours, both growth of E.coli and S.aureus will be inhibited by Cycloheximide antibiotic.
The effect of pH on the speed of enzyme interaction with substrate chemicals Hypothesis: About pH: If the pH level is less than 5, then the speed of the enzyme reaction will be slower. About temperature: If the temperature stays the same, then the speed of the enzyme reaction will not be completely affected. Background information: The function of enzymes is to speed up the biochemical reaction by lowering the activation energy, they do this by colliding with the substrate. All enzymes are under the class of protein biomolecule. Amino acids are the basic units that are combined to make up an enzyme.
Acetylcholine then binds to receptors on the muscle fibre membrane (sarcolemma) causing depolarisation. A wave of depolarisation travels down tubules (T system). T system depolarisation leads to Ca2+ release from stores in sarcoplasmic reticulum. Ca2+ binds to proteins in the muscle, which leads to contraction. Acetylcholinesterase in the gap rapidly breaks down acetylcholine so that contraction only occurs when impulses arrive continuously.
This enzyme acts as an escort for ubiquitin to its next destination E3 ligase enzyme. E2 ubiquitin conjugating enzyme Figure 16: Schematic representation of transfer of activated Ubiquitin from E1 activating enzyme to E2 conjugating enzyme The E3 enzyme act as a platform on which the target protein substrate and the active E2 ubiquitin complex can meet and interact. The E3 enzyme is extremely fussy about exactly which E2 enzyme and which protein can interact. The correct E2 enzymes loaded with activated ubiquitin could move in position itself correctly on the E3 ready for action. Skp 1 Target Protein Figure 17: Schematic representation of Target protein and ubiquitin conjugation in skp 1 Note: The Target Protein attached to the Skp 1 through F Box (Atrogin-1) which was not depicted in the figure.
During the binding process the substrate requires some assistance in order to bind to the enzyme properly. This is done by several different catalytic mechanism. The most abundant catalytic mechanism is known as the general acid-base catalysis. For this reaction to occur, one of the eight amino acid residues, shown in fig 6-9, will act as a proton donor or a proton acceptor. The amino acid residues known for their acidic form will function as the proton donor and the residues that form a base will act as a proton acceptor.
This method has been specially valuable for the separation of closely related amino acids. The mixture is dissolved in a fluid called mobile phase , which carries it through the structure holding another material called the stationary phase . The various amino acids travel at different speed , causing them to separate based on its R group . Amino acid Amino acid play central roles as building blocks of proteins and as intermediates in metabolisms . The 20 amino acids are found within proteins convey a vast array of chemical versatility (The Biology Project.2000).All amino acids found in proteins have a basic structure , different only in the structure of the R group or the side chain(Figure).
Research Question How does the change in temperature affect the effectiveness of protease on breaking down egg whites? Introduction Enzymes are a substance known as biological catalysts, this basically means they can, without being used up, speed up chemical reactions. Enzymes are made up proteins that create elaborate shapes that smaller molecules, such as protein particles, can then fit in. These areas that allow the molecules to fit in are called active sites. Some different enzymes such as protease, amylase and lipase, all work well in different conditions, and in different parts of the digestive system.
On the other hand chlorine when reacts with any substance it adds chlorine molecule or substitutes chlorine atom from substance. Chlorine dioxide responds specifically with amino acids and the RNA in the cell. It is not clear whether chlorine dioxide attacks the cell structure or the acids inside the cell. The generation of proteins is avoided. Chlorine dioxide influences the cell layer by changing film proteins and fats and by anticipation of
They noted that bacterial cytoplasm is crowded, poly-disperse and in the absence of known motors, diffusion-reliant for metabolic activities. Yet, how metabolism affects the cytoplasm remained untested. Their results suggest that the cytoplasm appears like a simple viscous fluid to particles below a certain size scale (< 30nm), and like a glass-forming liquid to particles above this size. The glass-like properties include caging, dynamic heterogeneity and non-ergodicity. Under natural conditions, this behaviour might reduce diffusion of large macromolecules & hinder cellular activities, yet it does not.
Since the production of light requires a large amount of energy expenditure, Vibrio fischeri uses quorum sensing to regulate its gene expression after detecting changes in extracellular density. Quorum sensing is used by both Gram-positive and Gram-negative bacterium . Lux R and lux I are genes encoding proteins that regulates light production.Aliivibrio fischeri also forms a symbiotic relationship with animal hosts. Aliivibrio fischeri utilizes the nutrients provided by its host to emit light that is later used by the host for various purposes. The light emitting reaction of Aliivibrio fischeri is catalyzed by
Since the current run from negative (top) to positive (bottom), the proteins move toward the bottom. When the electricity is turned on, the proteins and Tris-glycine enter the stacking gel. In stacking gel with pH 6.8, the N-terminal amino group of the proteins and amino acids are protonated at equilibrium, which makes them less negative. The average electrophoretic mobility is very slow. A Gly-chloride ion boundary is formed since glycine moves slower than chloride ion.