Biology190 Unit 2
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This 4 page Study Guide was uploaded by Stacy Downing on Saturday January 30, 2016. The Study Guide belongs to BIOL 190 at Towson University taught by preeti shah in Spring 2016. Since its upload, it has received 39 views. For similar materials see Introductory Biology for health professions in Biology at Towson University.
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Date Created: 01/30/16
BIOL 190 Study Guide for Unit 2 1. Protein Structure and Function: The first level of structure can be determined by a sequence of amino acids also known as a polypeptide chain. The amino acids that are adjacent to one another are strongly covalently bonded. In the second structure of protein, there are alpha helices and beta pleaded sheets. The amino acids that are farther apart are weakly hydrogen bonded together. The third level of structure is when the alpha helices and beta pleaded sheets are folded together creating a 3D model shape of the protein. The protein bend and coil to achieve stabilization in the protein. There are hydrogen bonds between the polar R-groups (side chain), ionic bonds between charged R-groups, hydrophobic bonds, and disulfide bonds between two CH mol2cules. The fourth level of structure can be determined by more than one individual polypeptide chain. Amylase is functional at the third level of structure in proteins in which hydrolyzes starch in the mouth which is also known as saliva. Amylase possesses the 3D overall shape from the irregular folding from the second level of structure. Hemoglobin is made up of 4 subunits which consist of 2 alpha helices and 2 beta pleaded sheets. Hemoglobin carries oxygen from the lungs to the tissues of the body and also helps transport CO an2 hydrogen ions back to the lungs. Polypeptides are linear chain of amino acid chain with coiling and folding but has no structure concluding that it doesn’t have any function. Proteins consist of one or more polypeptides with the level of structure that allows the protein to function. Denaturation involves the breaking of bonds in the second, third, and fourth level of structure which are directly affected by this process. Denaturation requires no enzyme, however it occurs with conditions such as a rise in temperature, a rise in pH, and a rise or lowering of salt concentration. The function of the protein is lost during this process because the structure is lost. The reversibility of denaturation is renaturation however, it is usually done in vitro. Hydrolysis is the breakdown of protein into smaller peptides and free amino acids that get recycled into the cytoplasm. Hydrolysis do require an enzyme which breaks apart the amino acids from the polypeptide chain. The only level of protein structure that is affected is the primary structure and since there is no longer a structure of protein, there is no longer a function. Functional categories of proteins are hormones, structural, and protection. In the hormone functional category, it consist of chemical signaling around the body and the proteins that are involved are insulin and glucagon which assist in regulating the blood sugar levels. In the structural category, they help in structural support and toughness in the cell and a protein that is used in this category is collagen which is a fibrous protein that holds together muscles, tendons, skin, bone and teeth. In protection category, the protein that is involved is antibodies which are immunity in the white blood cells and stimulates the immune system to destroy the pathogens. Word Count:503 2. Molecular Diversity: BIOMOLECULE MACROMOLECULE SUBUNITS (MONOMER) (POLYMER) Nucleic Acidsfunctions in DNA and RNA Nitrogenous Base: adenine, encoding and transmitting thymine. Cytosine, genetic information Guanine, Urine. Carbohydrates deals starch, glycogen, cellulose, Monosaccharides with energy storage wither and chitin (Polysaccharides) short or long Proteinsfunctions with Proteins Amino Acids support, hormones, contractile, and enzyme. Lipids functions are Phospholipids, steroids, Fatty Acids and glycerol insulation, long term waxes triglycerides energy storage, membrane structure, and protection. Chemical reactions toChemical Chemical groups, water solubility/ produce them Composition insolubility Carbohydra 1C:2H:1O Monosaccharides and disaccharides tes are water soluble since each molecule has OH groups that hydrogen bond to water easily. Polysaccharides are insoluble in water. Protein Proteins Water Soluble since amino acids are contain the hydrophilic which means water element loving. nitrogen, carbon, hydrogen, and oxygen. Lipids Not solubility in water since its nonpolar molecules and their ends are not charged. Water is polar, lipids are not soluble in water. That means the lipid molecules and water molecules do not bond. Nucleic Nitrogen Soluble in water since they have Acids bases, PO4 sugar and phosphate components group, and a that are polar molecules, which sugar would have a positive end and a molecule negative end. Water is also made from polar molecules which means that water molecules will attract the phosphate and sugar molecules and dissolve the nucleic acid bonds. A good source of carbohydrate is potatoes since it’s a starch. The starch in potatoes is easier to break down and digest. A good sources of Protein would be eggs because they have more muscle building amino acids. A good source of lipids would be olive oil which is high in fat and reduces blood pressure and cholesterol. There is no source of food that possess nucleic acids that humans can consume because humans make their own genetic material and genetic material cannot be eaten. BIOMOLECULE EXAMPLE 1Function EXAMPLE 2Function Carbohydrates Cellulose: it’s a Glucose: is an energy component in cell walls source in cells. that surround plant cells, and it makes up plant stems, leaves, and branches that are strong. Protein Glucagon: It’s released Collagen: It holds the body when glucose in the together by connecting bloodstream is too low. muscles, ligaments, skin, Glucagon causes the liver bone and teeth. to convert stored glycogen into glucose, which is released into the bloodstream. Lipids Nucleic Acids DNA: It contains the RNA: mRNA has the genetic instructions and the message exiting the role of DNA in the cell is the nucleus, tRNA interprets long-term storage of the the message to make genetic information. amino acids rRNA links to form proteins. 3. Mutation: A gene mutation is a permanent change in the base sequence of DNA. It can arise when proofreading doesn’t correct the error during DNA replication and in environmental mutagens. Error usually occurs during the Synthesis(S) phase of the cell cycle and there are environmental damage throughout the cycle. If there is an error in the DNA then the RNA copies and protein will be all incorrect. If there is an error in the protein then there will be only one protein out of millions that will be incorrect. The two main classes of gene mutation is base substitution and base insertion/ deletion. In base substitution, there is only a single nucleotide base that changes of the genetic material. Point mutations can result in a couple of effects. There can be a silent mutation, a missense mutation, a nonsense mutation. In a silent mutation, there is one nucleotide base that changes in a codon but the codon and amino acid doesn’t change in the protein. In a missense mutation where a codon is changed and the amino acid becomes different. In a nonsense mutation, a base changes which results into a STOP codon which permanently stops the amino acid sequence. In a base insertion/deletion mutation, an insertion or deletion would change the bases in a gene by adding or dropping a base and as a result, the protein may not function properly. Frameshift mutation is an effect or insertion or deletion mutation. In a frameshift mutation, the reading frame is shifted. When adding only one or two bases, the protein sequence is incomplete which may affect the structure and function of the protein. When inserting or deleting three bases, it’s known as amino acid insertion which is when an extra codon is either inserted or deleted, but there is the same reading frame. In the primary level of structure, it’s made up a sequence of amino acid also known as a polypeptide chain. There is no function at this level because it’s only a chain and there’s no structure. In the secondary structure, there are alpha helices and beta pleaded sheets that use hydrogen bonded. In the tertiary level, the alpha helices and beta pleaded sheets fold together to form an overall 3D shape of the protein. All of the levels of structure would be effected by a missense mutation because it would affect the primary structure by having a different amino acid in replace for the original one. Since the secondary and tertiary structure consist of the primary structure, they would also be affected by the mutation. The function of the protein would be affected by either doing a different job or not having any function at all since there would be no structure. In sickled cell anemia, a hemoglobin gene is mutated. This mutation is a result of a point mutation or a missense mutation that switches one base. This mutation causes the hemoglobin in red blood cells to change to a sickle shape. The amino acid that is mutated is located on the surface of the protein. The Glu becomes a Val which results in a sickled hemoglobin. It changes the 3D overall shape of the protein because its less efficient in binding with oxygen, it stacks the red blood cells and distorts their shape. Sickle cells can destroy the function of the spleen which results in the amnesia and there is chronic pain that is brought from the disease which is because of the sickled red blood cells get stuck in capillaries, block the blood flow, and cause pain cries. DNA codes for proteins and proteins have certain functions in the body which includes breaking down carbohydrates and lipids that are used in the body. When a mutation occurs in the DNA, it could alter the protein that is necessary for the use of carbohydrates or lipids.
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