2) Proteins are polypeptide chains consisting of monomers called amino acids, which are made up of carbon, hydrogen, oxygen and nitrogen. Amino acids are made up of an amino group, an R group a carboxyl group and an alpha carbon, the different R groups of each individual amino acids determines which amino acid they will form.…
A cyclist rides her bike up a very steep hill. Which choice below properly describes this example in energetic terms? Both a) and d) are correct.…
Enzymes are a type of proteins that are formed by Amino acids and help speed up…
The toxins of A. phalloides target RNA polymerase II by inhibiting its ability to produce new mRNA. Without mRNA translation cannot occur as the template used to synthesize new proteins would be absent, cell metabolism would not occur and would eventually result in cell death also known as necrosis.…
Bio 101 Review Sheet Test #3 (Chapters 7,8,9) Chapter 7 1. 3 effects of mutations a. Good, bad, silent i. What silent is in terms of amino acids 2.…
Chymotrypsin is a protease which cleaves proteins by a hydrolysis reaction, it does this by adding a molecule of water to a peptide bond. Although the hydrolysis reaction is thermodynamically favoured in the absence of a catalyst the half-life for a typical hydrolysis reaction by a protease is between 10 and 100 years, needless to say it is extremely slow1. Though this is true peptide bonds are hydrolysed within milliseconds in the body in the presence of catalysts. The kinetic stability of chymotrypsin which gives it hydrolysis resistance is due to the resonance structure that accounts for the planarity of the peptide bond. Such is the strength of this resonance structure that it confers partial…
Part B: Click on the links below to learn about the three major groups of protists!…
The importance of identification of a certain microorganisms can range between a life threatening diseases to a creation of certain antibiotic. Understanding the principals of living microbes and identifying my unknown bacteria through numerous biochemical and metabolism tests, with the outmost confidence, Proteus vulgaris had the precise qualifications. The point of this report is to further explore the identification of my unknown bacteria by revealing the results of the experiments and comparing them to the other six known bacteria: Micrococcus luteus, Staphylococcus aureus, Staphylococcus epidermidis, Alcaligenes faecalis, Escherichia coli, and Proteus vulgaris that were used in the lab, as well as comparing and contrasting the actual and factual results.…
References: 1. Carniol, K. and M.S. Gilmore. 2006. The comprehensive sourcebook of bacterial protein toxins, p. 717 3rd ed. Alouf, J.E., and M.R. Popoff (ed), Academic Press, San Diego, CA.…
Despite such, the enzyme is associated with a number of pathophysiological issues due to therapeutic target a number of inhibitors have been described for the enzyme. Thompson & Webster, (2015) explains that the enzyme is derived from natural sources but there are those derived from chemical synthesis. Additionally, an overview of functional groups that have been used as warheads of calpain inhibitors is presented along with a discussion of the structure activity relationship studies of the address region of peptidyl Calpain…
Argiolas, A., and JJ Pisano. "Facilitation of Phospholipase A2 Activity by Mastoparans, a New Class of Mast Cell Degranulating Peptides from Wasp Venom." The Journal of Biological Chemistry 258.11 (1983): 13697-3702. PubMed. Web. 01 May 2013. <http://www.ncbi.nlm.nih.gov/pubmed/6643447>.…
. These novel toxin peptides are composed of two wasp kinins, two chemotactic components, three mastoparans, and two peptides with an unknown function. The seven novel toxin of peptides with recognized functions turns out to act unitedly with the other peptides that are known previously naming the three well-known kinds of peptides of novel toxin in the venom of the social wasp which are the wasp kinins, chemotactic peptides and mastoparans. But apparently, those three functional toxins may cause some disadvantages in some organisms or in our body. It may cause pain, chemotaxis, edema formation, and destruction of red blood…
volitans that may contribute to its success, both in its native and invasive ranges, is the venomous spines in its fins. There are venom glands along 13 dorsal spines, three anal spines, and two pelvic spines that extend about three quarters of the way up from the base to the tip (Morris 2009, 119). Lionfish venom possesses a toxin containing acetylcholine, which impacts neuromuscular transmission, and can cause neuromuscular and cardiovascular effects in both humans and animals (Morris 2009, 119). This venom may help protect lionfish from predators, and may cause potential predators to avoid the species. There is even evidence that the Indo-Malayan octopus has been observed mimicking the lionfish, potentially as a way to protect against predation (Morris 2009, 128). There is also research that suggests that this venom may be useful for biomedical applications, such as reduction of cancer growth in humans (Morris 2009,…
The female bees, or worker bees, have hollow, serrate stingers that are attached to a venom sac (Christiansen). Once the bee stings a human, its abdomen is torn from the body, leaving the muscles surrounding the venom sac to work the stinger further into the skin and continue to pump venom into the wound (“Loveridge”). The cytotoxic venom consists of sixty-three components, including histamine, pheromones, peptides (tiny enzymes), and several different enzymes (“Loveridge”). While the enzymes of the venom work to break down the membranes of cells, it’s the peptide melittin that does the most damage. Making up half of the venom’s dry weight, melittin induces histamine and cortisol release and is the culprit behind the pain of a sting (“Loveridge”). This 26-amino long peptide targets cells and attacks their membranes, effectively destroying them (“Loveridge”). The ability of melittin to destroy cell membranes is what scientists are most interested in manipulating to treat acquired immune deficiency syndrome and various…
Pepsin is an active form of pepsinogen which is released into the stomach. Hydrochloric acid is also released into the stomach from parietal cells and makes the pH acidic, of a pH 1-3. This then activates chief cells to release pepsinogen, which functions in an autocatalyctic fashion. The hydrochloric acid mixed with pepsinogen generates pepsin, which can digest 20% of ingested carbon bonds. The primary structure of pepsin has an additional 44 amino acids which is useful in breaking proteins into smaller pieces called polypeptides (Whitman, 2002). The peptides are further digested by other protease in the duodenum and then absorbed by the body. However pepsin can only break certain amino acid bonds into shorter chains, and as other bonds are broken in the small intestines.…