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Four Types of Organic Molecules Made by cells Contains carbon Importance of Carbon Although cells are 70-95% water, the rest are composed mainly of carbon compounds. Proteins, carbohydrates, DNA, and other molecules are compounds of carbon bonded to other elements. Carbon often bonds to H, O, N, S, and P in organic compounds. Properties of Carbon Has four valence electrons; can form covalent bonds with four other atoms Carbon can form single, double, or triple bonds with other atoms. Carbon chains form the backbone of most organic molecules. Chains can be straight, branched, or arranged in closed rings. Hydrocarbons contain carbon and hydrogen only, and are hydrophobic. H—C and C—C bonds are nonpolar. Hydrocarbons make up fossil fuels, and parts of cellular organic molecules such as fats and phospholipids. Organic Molecules are made by cells and contain carbon 4 Types of Organic Molecules: 1. Carbohydrates- used as fuel and building material 2. Lipids-energy storage 3. Proteins-structure, movement, enzymes 4. Nucleic acids-store and transmit hereditary information. They are macromolecules because of their large size. The largest Macromolecules are called polymers Created by linking smaller subunits called monomers. Dehydration Monomers are linked together to form polymers through dehydration reactions, which remove water This process is called dehydration because water is removed Monomers are linked together by covalent bonds Short polymer Dehydration reaction Longer polymer Unlinked monomer Hydrolysis Polymers are broken apart by hydrolysis, the addition of water Hydro means water and lysis means to rupture or break apart. You break apart molecules by adding water. Breaks covalent bonds between monomers Hydrolysis Review Q: Hydrolysis is involved in which of the following? A) Formation of starch B) Hydrogen bond formation between amino acids C) Peptide bonds in proteins D) The hydrophobic interactions in lipids E) The digestion of maltose to glucose Hydrocarbons Compounds made of only carbon and hydrogen. Found in a variety of structures. 1. Length 2. Branching 3. Double bonds 4. Rings Isomer – same molecular formula, different structure. Length. Carbon skeletons vary in length. Branching. Skeletons may be unbranched or branched. Skeletons may have double bonds, which can vary in location. Rings. Skeletons may be arranged in rings. functional group determine the properties of organic compounds Compounds containing functional groups are hydrophilic (water-loving) 6 Functional groups – – – – – – Hydroxyl group —a hydrogen bonded to an oxygen Carbonyl group — a carbon linked by a double bond to an oxygen atom Carboxyl group —a carbon double-bonded to both an oxygen and a hydroxyl group Amino group —a nitrogen bonded to two hydrogen atoms and the carbon skeleton Phosphate group —a phosphorus atom bonded to four oxygen atoms Methyl group – a carbon bonded to three hydrogens. 4 different types of Organic Molecules 1. Carbohydrates (monomer = monosaccharide) Function: Most carbohydrates are used for energy, but some of them are used for structure All carbs are in a 1:2:1 ratio of C:H:O • The common name for carbohydrates is “sugars” • Most carbohydrates (but not all) end in the letters “ose”. • Carbohydrates occur in the form of 1 (mono), 2 (di), or more (poly) rings There are 3 different types of carbohydrates: 1. 2. 3. Monosaccharide Disaccharide Polysaccharide 3 different types of carbohydrates monosaccharides – simple (one) ring sugars Chemical Formula: C6H12O6 • Monosaccharides give energy quickly because they can be broken down easily by the body. Even so, this energy does not last for long because it is used up very quickly. Types: a. Glucose – 6 carbon sugar found in blood b. Fructose – 6 carbon sugar found in fruit c. Galactose – 6 carbon sugar found in peas • Monosaccharides Monosaccharides Diabetes Disease characterized by high levels of blood glucose resulting from defects in insulin production Monitored with blood glucose device. 2. Disaccharides – 2 ring sugar • Made by joining 2 monosaccharides by process of dehydration • These sugars give energy that lasts a little longer than monosaccharides because the glycosidic bond (a covalent bond between two monosaccharides) must be broken before the sugar can be used for energy Examples Sucrose = table sugar (made by Glucose + fructose) Lactose = milk sugar (made by Glucose + galactose) Maltose = malt sugar (made by glucose + glucose) Remember dehydration reaction! (Makes a glycosidic linkage – O binds 2 monosaccharides) What kind of bond would this linkage be? Glucose Glucose Maltose Lactose intolerant If the enzyme lactase is not present, the body is unable to break down lactose. Allowing it to reach the large intestines. Normally, sugars do not reach the large intestine. This is what causes a stomach ache! 3. Polysaccharides – many ringed sugar (repeating units of monosaccharides) Usage: energy storage and as structural components. Examples: Energy starch (plants produce for a storage molecule.) glycogen (storage molecule in muscle and liver cells.) Structural (only 2 carbs we’ll talk about that aren’t used for energy) cellulose (plants produce for cell wall construction.) indigestible because we lack enzymes to break it down. chitin (used by insects and crustaceans to build an exoskeleton.) Starch, Cellulose & Glycogen All the sugars are oriented in the same direction Branched or "forked" Every other sugar molecule is "upside-down Review Q: Polymers of carbohydrates are all synthesized from monomers by A) the joining of disaccharides. B) hydrolysis. C) dehydration synthesis. D) ionic bonding between monomers E) cohesion. 2. Protein Made of a long chain of amino acids linked by dehydration reaction Amino acids (monomer for protein) Have an amino group and a carboxyl group Also a chemical group symbolized by R Amino group Carboxyl group – Dehydration reaction links the carboxyl group of one amino acid to the amino group of the next amino acid – The covalent linkage resulting is called a peptide bond Carboxyl group Amino group Dehydration reaction Peptide bond Dipeptide Amino acid Amino acid Peptide bonds Peptide bonds are covalent bonds formed by a condensation reaction that links the carboxyl group of one amino acid to the amino group of another. Has polarity with an amino group one end (Nterminus) and a carboxyl group on the other (C-terminus). Has a backbone of repeating N-C-C-N-C-C Polypeptide chains range in length from a few monomers to more than a thousand, and a unique linear sequence of amino acids. The R group determines if the amino acid is hydrophobic or hydrophilic. Hydrophobic Leucine (Leu) Hydrophilic Serine (Ser) Aspartic acid (Asp) A protein’s specific shape determines its function A polypeptide chain contains hundreds or thousands of amino acids linked by peptide bonds – – The amino acid sequence causes the polypeptide to assume a particular shape The shape of a protein determines its specific function A.A. sequence = shape = function! Proteins have many functions Structural proteins (support) keratin for hair and nails collagen for bones, ligaments, tendons, skin Proteins function as… Contractile Found in muscle cells, enables them to move. Proteins function as… Enzymes - proteins that promote chemical conversions, as well as speeds up reactions. Example: Amylase is an enzyme in saliva that breaks starch into glucose monomers. Saliva Saliva Identification - Amylase Proteins function as… Transport across cell membranes Ex. Hemoglobin Defense from infection Antibodies Signal hormones Insulin Insulin is a hormone that helps your body use glucose. Proteins function as… Storage Source of food for developing embryos. Albumin (egg whites) experiences heat coagulation (denaturation) Protein in seeds. Receptor Built in cell membrane. Transmits signals to the inside of the cell. A protein can have four levels of structure 1. The primary structure of a protein is its unique amino acid sequence 2. Protein secondary structure results from coiling or folding of the polypeptide held by hydrogen bonds. – – Coiling = alpha helix structure Folding = pleated sheet structure A protein can have four levels of structure 3. The overall three-dimensional shape of a protein is called its tertiary structure – results from interactions between the R groups of the amino acids 4. Two or more polypeptide chains (subunits) associate providing quaternary structure Four Levels of Protein Structure Primary structure Amino acids Hydrogen bond Secondary structure Alpha helix Tertiary structure Quaternary structure Pleated sheet Polypeptide (single subunit of transthyretin) Transthyretin, with four identical polypeptide subunits Protein structure is key to their ability to function. **A protein can be denatured, heat, salinity, pH can cause it to lose its shape, and its functionality.. Denature Protein structure is key to their function Denature – a protein loses its shape (and consequently its function) when it is taken out of its natural range for factors such as temperature, pH, or salinity Review Q: The linkage between the monomers of proteins are identified as A) Peptide bonds B) Glycosidic linkages C) Ionic bonds D) Covalent bonds E) Ester linkages Review Q: Which two functional groups are always found in amino acids? A) Amine and sulfhydryl B) Carbonyl and carboxyl C) Carboxyl and amine D) Alcohol and aldehyde E) Ketone and amine 3. Nucleic Acids Function: Hereditary material and instructions for making proteins Two types: DNA (deoxyribonucleic acid) RNA (ribonucleic acid) Nucleotides are the building blocks of Nucleic acids. Have 3 parts: * 5 carbon sugar * phosphate group * nitrogenous base group 4 base pairs DNA nitrogenous bases are adenine (A) thymine (T) cytosine (C) guanine (G) RNA also has A, C, and G, but instead of T, it has uracil (U) Double helix Two DNA strands wrap around each other to form a double helix – – – The two strands are connected by a hydrogen bond between the base pairs. A pairs with T C pairs with G RNA is usually a single strand Genes are enough DNA to code for the sequence of amino acids for 1 protein (primary structure of proteins). Genes do not use DNA to code directly. Genes use an intermediary (RNA). The DNA is transcribed into RNA, which is then translated into the amino acid sequence. Flow of information: DNA RNA Proteins Review Q: Which list of components characterizes RNA? A) A phosphate group, deoxyribose, and uracil B) A phosphate group, ribose, and uracil C) A phosphate group, ribose and thymine D) A phosphate group, deoxyribose, and adenine 4. Lipids Functions: 1. Energy storage- fats store twice as many calories/gram as carbs. 2. Protection of vital organs and insulation in humans and other mammals. 3. Phospholipids make up cell membranes. 4. Steroids are often in cell membranes (cholesterol) and make up some hormones (estrogen and testosterone) Monomer: No single monomer for lipids (each type of lipid has its own monomers) Lipids are Hydrophobic – Will not mix with water Types of Lipids 1. Fats Risk factors to Saturated fats Atherosclerosis Heart Disease Types of Lipids: 2. Phospholipids - form cell membranes Hydrophilic head Hydrophobic tails The polar heads are towards the water, the nonpolar tails are on the inside of the cell. Phospholipids Where fats have a third fatty acid linked to glycerol, phospholipids have a negatively charged phosphate group. This makes the “head” of the phospholipid hydrophilic; the hydrocarbon “tails” are hydrophobic. Phospholipids are the major components of cell membranes. In a cell membrane, the hydrophobic tails are orientated inward, while the hydrophilic head face outward. Steroids cell messengers examples: testosterone, estrogen (estradiol) Waxes protection & waterproofing Review Q: Which macromolecule is the main component of cell membranes? A) Glucose B) Steroids C) Carbohydrates D) Phospholipids E) DNA Review Q: Which of the following macromolecules below could be structural parts of the cell, enzymes, or involved in cell movement or communication? A) Nucleic acids B) Proteins C) Lipids D) Carbohydrates E) Minerals