single taste bud contains 50–100 taste cells representing all 5 taste sensations (so the classic textbook pictures showing separate taste areas on the tongue are wrong). • Each taste cell has receptors on its apical surface. These are transmembrane proteins which o admit the ions that give rise to the sensations of salty and sour; o bind to the molecules that give rise to the sensations of sweet‚ bitter‚ and umami. • A single taste cell seems to be restricted to expressing only a single type of receptor
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hydrogen ions in body fluids and must be regulated carefully to prevent problems. 6.9) Name the 4 main Organic Molecules in Biochemistry. Describe each one‚ and provide an example. What are the “building blocks” of each molecule? For example‚ protein = Amino Acid. 1. carbohydrates: organic molecule with a carbon/hydrogen/oxygen ratio of about 1:2:1‚ including sugars and starches. EX: monosaccharides‚ disaccharides‚ polysaccharides 2. Lipids:
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makes it such a powerful food Proteins Our bodies use amino acids as building blocks for protein. Depending on who you ask‚ we need 20-22 of them for this task Eight of them are considered essential‚ in that we have to get them from our food The remaining 12-14 we can make from the first eight via complex metabolic pathways in our cells Raw cow’s milk has all 8 essential amino acids in varying amounts‚ depending on stage of lactation About 80% of the proteins in milk are caseins- reasonably
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Pg. 287 #1‚3‚4 1. Describe the structure of a nucleotide. A nucleotide is a sugar molecule that has 3 parts including a simple sugar‚ a phosphate group and a nitrogenous base. Nucleotides join together forming long chains‚ with the phosphate group of nucleotide bonding to the deoxyribose sugar of an adjacent nucleotide. 3. Explain why the structure of a DNA molecule is often described as a zipper. The structure of a DNA molecule is often described as a zipper because it is made of tow chains
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high to low concentration‚ small non-polar particles fit between phospholipids 2. Facilitated Transport (a.k.a facilitated diffusion)- Diffusion‚ uses a channel protein‚ large or charged particles a. Ex: Fructose‚ amino acids 3. Active Transport- Pushing particles from low to high concentration (against the gradient)‚ uses a carrier protein 4. Vesicle Formation or Membrane assisted transport- Compounds enter/exit in vesicles A. Diffusion- any small and not charged particles diffuse (goes down
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I think that this will happen because generally hydrochloric acid causes more damage to things and also it produces more aggressive reactions causing greater effects this I think means that the acid is more likely to effect or disable the proteins in the lipid bi-layer this means that if this happens the membranes selective permeability will be lessened and the restriction of the flow of pigment out of the beetroot will also be lessened so more pigment can and will flow out. I think
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biophysical measurements of several non-enzymic mesophilic proteins at about -65 °C and reflecting a sharp decrease in protein flexibility as the overall motion of groups of atoms ceases. INTRODUCTION It is now accepted that‚ in general terms‚ enzyme activity is dependent on protein dynamics [1-5]: in other words‚ an enzyme must be flexible to function. A number of biophysical studies [6-12] have shown that the flexibility of mesophilic proteins undergoes a transition at about -65 °C. Below this transition
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Bromelain The pineapple plant contains protein-digesting enzymes called‚ as a group‚ bromelain. In the health world‚ these enzymes are regarded as useful in reducing muscle and tissue inflammation (hence the joint pain and wound-healing possibilities)‚ as well as acting as a digestive aid. In the cooking world‚ on the other hand‚ bromelain is regarded as the enemy of the gelatin dessert. If you use fresh pineapple in gelatin‚ the enzyme eats the protein and the gelatin will not gel—in fact
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Christian Hogdohm Gel Electrophoresis I. Introduction: A typical electrophoresis has five major parts: the electrical current‚ DNA‚ RNA‚ or protein sample‚
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the active site and then causes the active site to change shape meaning the substrate is no longer complementary so it wouldn’t bind together. 1ci. Peptide 1cii. The 35 and 52 amino acids are held close to form the active site due to the tight folding of the polypeptide chains 2ai. There will be more kinetic energy which means there wil be more successful collisions and then more enzyme-substrate complexes. 2aii. The enzyme is denatured‚ this means that the substrate will no longer fit into
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