Vocabulary: macromolecule, polymer, monomer, condensation reaction (dehydration reaction), enzyme, hydrolysis, carbohydrate, monosaccharide, glycosidic linkage, polysaccharide, starch, glycogen, chitin, cellulose, lipid, fatty acid, fats/oils, saturated fatty acid, unsaturated fatty acid, ester bond, phospholipid, steroid, cholesterol, catalyst, polypeptide, protein, amino acid, peptide bond, hydrophobic interaction, disulfide bridge, denaturation, chaperonins, nucleic acids, nucleotides, phosphodiester bond, deoxyribonucleic acid, ribonucleic acid, ATP, double helix, antiparallel, nitrogenous base
Objectives:
After attending lectures and studying the chapter, the student should be able to:
1. Distinguish between inorganic and organic substances and give examples of each.
2. For each of the functional groups listed below, show the structural formula of the groups, give an example of a biologic organic molecule on which is can be found.
hydroxyl group
carbonyl group
carboxyl group
amino group
sulfhydryl group
phosphate group
3. List the 4 categories of organic macromolecules that make up all living things and the
main functions of each
4. Explain how organic macromolecules are polymers made up of monomer subunits.
5. Recognize the condensation reaction (dehydration synthesis) process of making
organic macromolecules from monomers
6. Know the following bonds made as a result of dehydration synthesis and the
macromolecules that result:
2 amino acids -----peptide bond (proteins)
2 sugar molecules -----glycosidic bond (carbohydrates)
2 nucleotides ---------- phosphodiester bond (nucleic acid)
glycerol and fatty acid ------ ester bond
7. Describe the hydrolysis process of breaking down organic macromolecules to monomer subunits.
8. Relating to carbohydrates:
a. Distinguish between and give examples of monosaccharides, disaccharides,
and polysaccharides.
Know which types of organism make the following polysachharides as well as the function of each
Cellulose, glycogen, chitin, starch
b. State the monomer subunits that make up carbohydrates.
c. State the name given to the bond between monosaccharides.
9. Relating to lipids:
a. Describe a major difference between carbohydrates and lipids.
b. Give examples of lipids and the function of each
Triglycerides (fats/oils), phospholipids, steroids, waxes
c. State the subunits that make up fats.
d. Describe a triglyceride molecule and state the name given to the bond between
glycerol and a fatty acid.
e. Distinguish between the structure of saturated and unsaturated fatty acids, and between monounsaturated and polyunsaturated fatty acids.
10. Relating to proteins:
a. Give examples of protein functions (p.90)
b. State the monomer subunits that make up proteins.
c. Show the structural formula of an amino acid, including the amino group, the carboxyl group, and the R group.
d. Describe the hydrophilic/hydrophobic nature of each of the following types of amino acids: nonpolar, polar, and electrically charged.
e. State the name given to the bond between amino acids.
f. Distinguish between a polypeptide and a protein.
g. Specifically describe the four levels of protein structure that give proteins their specific shape: primary, secondary, tertiary, and quaternary structure.
h. Describe what is meant by denaturation and renaturation of a protein.
i. Explain why proteins function best under optimum pH and optimum temperature conditions.
11. Relating to nucleic acids:
a. State the 2 kinds of nucleic acids.
b. State the monomer subunits that make up nucleic acids.
c. Describe the molecular structure of a nucleotide.
d. State the name given to the bond between nucleotides.
e.Explain the function of DNA.
f. Explain the function of RNA
| 5137920240 | macromolecule | There are Four major types of biological macromolecules that make up the human body: nucleic acids (DNA & RNA), Carbohydrates, Proteins and Fats |  | 0 |
| 5137920241 | polymer | a long molecule consisting of many similar or identical monomers linked together by covalent bonds | 1 | |
| 5137920242 | monomer | the subunit that serves as the building block of a polymer | 2 | |
| 5137920243 | enzyme | a macromolecule serving as a catalyst, a chemical agent that increases the rate of a reaction without being consumed by the reaction. Most are proteins. | 3 | |
| 5137920244 | dehydration reaction | a chemical reaction in which 2 molecules become covalently bonded to each other with the removal of a water molecule |  | 4 |
| 5137920245 | hydrolysis | a chemical reaction that breaks bonds between 2 molecules by the addition of water; functions in disassembly of polymers to monomers |  | 5 |
| 5137920246 | carbohydrates | a sugar (monosaccharide) or one of its dimers (disaccharide) or polymers (polysaccharide) |  | 6 |
| 5137920247 | monosaccharide | the simplest carbohydrate, active alone or serving as a monomer for disaccharides and polysaccharides. Also known as simple sugars, that are generally some multiple of CH2O |  | 7 |
| 5137920248 | disaccharide | a double sugar, consisting of two monosaccharides joined by a glycosidic linkage formed by a dehydration reaction | 8 | |
| 5137920250 | polysaccharide | Polymers of simple sugars covalently linked by glycosidic bonds |  | 9 |
| 5137920251 | starch | a storage polysaccharide in plants, consisting entirely of glucose monomers joined by alpha glycosidic linkages |  | 10 |
| 5137920252 | glycogen | an extensively branched glucose storage polysaccharide found in the liver and muscle of animals; the animal equivalent of starch |  | 11 |
| 5137920253 | cellulose | a structural polysaccharide of plant cell walls, consisting of glucose monomers joined by beta glycosidic linkages |  | 12 |
| 5137920254 | chitin | a structural polysaccharide, consisting of amino sugar monomers, found in many fungal cell walls and in the exoskeletons of all arthopods |  | 13 |
| 5137920255 | lipid | Hydrophobic. Considered monomers. Any of a group of large biological molecules, including fats, phospholipids, and steroids, that mix poorly, if at all, with water. Provide an efficient form of energy storage. |  | 14 |
| 5137920256 | fat | a lipid consisting of 3 fatty acids linked to one glycerol molecule; also called a triacylglycerol or a triglyceride. |  | 15 |
| 5137920257 | fatty acid | a carboxylic acid with a long carbon chain; vary in length and in the number and location of double bonds; 3 fatty acids linked to a glycerol molecule form a fat molecule, also known as a triacyglycerol or a triglyceride |  | 16 |
| 5137920259 | saturated fatty acid | a fatty acid in which all carbons in the hydrocarbon tail are connected by single bonds, thus maximizing the number of hydrogen atoms that are attached to the carbon skeleton |  | 17 |
| 5137920260 | unsaturated fatty acid | a fatty acid that has one or more double bonds between carbons in the hydrocarbon tail. Such bonding reduces the number of hydrogen atoms attached to the carbon skeleton |  | 18 |
| 5137920261 | trans fat | an unsaturated fat, formed artificially during hydrogenation of oils, containing one or more trans double bonds | 19 | |
| 5137920262 | phospholipid | a lipid made up of glycerol joined to 2 fatty acids and a phosphate group. The hydrocarbon chains of the fatty acids act as nonpolar, hydrophobic tails, while the rest of the molecule acts as a polar, hydrophilic head.; form bilayers that function as biological membranes |  | 20 |
| 5137920263 | steroids | a type of lipid characterized by a carbon skeleton consisting of 4 fused rings with various chemical groups attached |  | 21 |
| 5137920264 | cholesterol | a steroid that forms an essential component of animal cell membranes and acts as a precursor molecule for the synthesis of other biologically important steroids, such as many hormones |  | 22 |
| 5137920265 | Polypeptide | A chain of amino acids linked together by peptide bonds or dehydration reactions | 23 | |
| 5137920266 | protein | a biologically functional molecule consisting of one or more polypeptides folded and coiled into a specific 3D structure |  | 24 |
| 5137920267 | amino acid | An organic molecule possessing both a carboxyl and an amino group; serve as monomers of polypeptides |  | 25 |
| 5137920268 | peptide bond | the covalent bond between the carboxyl group on one amino acid and the amino group on another, formed by dehydration reaction |  | 26 |
| 5137920269 | primary structure | the level of protein structure referring to the specific linear sequence of amino acids |  | 27 |
| 5137920270 | secondary structure | regions of repetitive coiling or folding of the polypeptide backbone of a protein due to hydrogen bonding between constituents of the backbone (not the side chains). |  | 28 |
| 5137920271 | alpha helix | a coiled region constituting one form of the secondary structure of proteins, arising from a specific pattern of hydrogen bonding between the atoms of the polypeptide backbone (not the side chains) |  | 29 |
| 5137920272 | beta pleated sheet | one of the secondary structure of proteins in which the polypeptide chain fold back and forth. 2 regions of the chain lie parallel to each other and are held together by hydrogen bonds between atoms of the polypeptide backbone (not the side chains). |  | 30 |
| 5137920273 | tertiary structure | The overall shape of a protein molecule due to interactions of amino acid side chains, including hydrophobic interactions, ionic bonds, hydrogen bonds, and disulfide bridges |  | 31 |
| 5137920274 | hydrophobic interaction | a type of weak chemical interaction caused when molecules that do not mix with water coalesce to exclude water | 32 | |
| 5137920275 | disulfide bridge | a strong covalent bond formed when the sulfur of one cysteine monomer bonds to the sulfur of another cysteine monomer | 33 | |
| 5137920276 | quaternary structure | the particular shape of a complex, aggregate protein, defined by the characteristic 3D arrangement of its constituent subunits, each a polypeptide |  | 34 |
| 5137920277 | denaturation | in proteins, a process in which a protein loses its native shape due to the disruption of weak chemical bonds and interactions, thereby becoming Biologically inactive; in DNA, the separation of the two strands of the double helix. Occurs under extreme (noncellular) conditions of pH, salt concentration or temperature | 35 | |
| 5137920279 | gene | a discrete unit of hereditary information consisting of a specific nucleotide sequence in DNA (or RNA, in some viruses) | 36 | |
| 5137920280 | nucleic acid | a polymer (polynucleotide) consisting of many nucleotide monomers; serves as a blueprint for proteins and, through the actions of proteins, for all cellular activities. the 2 types of nucleic acid are DNA and RNA |  | 37 |
| 5137920281 | deoxyribonucleic acid (DNA) | a double-stranded, helical nucleic acid molecule, consisting of nucleotide monomers with a deoxyribose sugar and the nitrogenous bases adenine (A), cytosine (C), guanine (G) and thymine (T); capable of being replicated and determining the inherited structure of a cell's proteins |  | 38 |
| 5137920282 | ribonucleic acid (RNA) | a type of nucleic acid consisting of a polynucleotide made up of nucleotide monomers with a ribose sugar and the nitrogenous bases adenine (A), cytosine (C), guanine (G), and uracil (U); usually single-stranded; functions in protein synthesis, gene regulation, and as the genome of some viruses | | 39 |
| 5137920283 | nucleotide | the building block of a nucleic acid, consisting of a 5 carbon sugar covalently bonded to a nitrogenous base and one or more phosphate groups | 40 | |
| 5137920286 | deoxyribose | the sugar component of DNA nucleotides, having 1 of fewer hydroxyl group than ribose, the sugar component of the RNA nucleotide | 41 | |
| 5137920287 | ribose | the sugar component of RNA nucleotides | 42 | |
| 5137920289 | What are 6 functions of Proteins? | Structural support Storage Transport Cellular Communications Movement Defense against substaces | 43 | |
| 5137920291 | nitrogenous base | ..., A carbon ring structure that contains one or more atoms of nitrogen, Cytosine, thymine, adenine, and guanine in the DNA molecule (slightly different in RNA) | 44 | |
| 5137920292 | Enzymes | Proteins that act as a catalyst to speed up chemical reactions | 45 | |
| 5137920293 | Collagen | A fibrous protein consisting of three polypeptide coiled like a rope |  | 46 |
| 5137920294 | Hydroxyl Group |  | 47 | |
| 5137920295 | Carbonyl Group |  | 48 | |
| 5137920296 | Carboxyl Group |  | 49 | |
| 5137920297 | Amino Group |  | 50 | |
| 5137920298 | Sulfhydryl Group | ... |  | 51 |
| 5137920299 | Phosphate Group | ... |  | 52 |
| 5137920300 | Monosaccharide | The simplest carbohydrate, active alone or serving as a monomer for disaccharides and polysaccharides. Also known as simple sugars, the molecular formulas of monosaccharides are generally some multiple of CH2O. |  | 53 |
| 5137920301 | dissaccharide | A double sugar, consisting of two monosaccharides joined by dehydration synthesis. |  | 54 |
| 5137920302 | Which monosaccharide is a major nutrient, central to cellular metobolism. It is broken down for energy in the process of cellular respiration. The carbon skeleton of this sugar can also be used to build many other organic molecules, including amino acids and fatty acids. | Glucose |  | 55 |
| 5137920303 | hydrocarbon | Compounds composed of only carbon and hydrogen | 56 | |
| 5137920304 | functional groups | A specific configuration of atoms commonly attached to the carbon skeletons of organic molecules and usually involved in chemical reactions. | 57 | |
| 5137920308 | renaturation | a proteins chemical and physical aspects are restored when it is restored to its natural environment | 58 | |
| 5137920309 | structural proteins | Proteins that are important for holding cells and organisms together, such as the proteins that make up the cell membrane, muscles, tendons, and blood. Ex. collagen & keratin | 59 | |
| 5137920310 | storage proteins | storage of amino acids (ex: casein the protein in milk is the major source of amino acids for baby mammals; plants have storage proteins in their seeds; ovalbumin is the protein of egg whites uses as an amino acid source for the developing embryo | 60 | |
| 5137920311 | transport proteins | Proteins that combine with other substances and acts as a mode of transport through the body (e.g. albumin, hemoglobin, transferrin, and vitamin d-binding protein). Also transports substances across the plasma membrane | 61 | |
| 5137920312 | Defensive proteins | antibodies | 62 | |
| 5137920313 | Receptor proteins | Enable a cell to sense its surroundings by binding to certain substances outside the cell. When this happens, it causes changes inside the cell. | 63 | |
| 5137920314 | hormonal proteins | coordination of any organism's activities (ex: insulin, a hormone secreted by the pancreas causes other tissue to take up glucose resulting blood sugar concentration); signals between cells, signal proteins | 64 | |
| 5137920315 | Contractile proteins | Actin and Myosin, generate the force during a contraction | 65 | |
| 5137920316 | Peptide bonds | The bonds connecting amino acids together to form polypeptide chains. | 66 | |
| 5137920317 | Globular proteins | overall spherical shape of the protein | 67 | |
| 5137920318 | Fibrous proteins | Form extended sheets or strands or long fibers. Tough, durable, and generally insoluble in water. Usually play structural roles. | 68 | |
| 5137920319 | Adenine | a double ring purine base found in DNA and RNA. Pairs with Thymine in DNA & Uracil in RNA | 69 | |
| 5137920320 | thymine | A single-ring (pyrimidine) nitrogenous base found in DNA. Pairs with Adenine. | 70 | |
| 5137920321 | Cytosine | A single-ring (pyrimidine) nitrogenous base found in DNA and RNA. Pairs with Guanine | 71 | |
| 5137920322 | Guanine | A double-ring (Purine) nitrogenous base found in DNA and RNA. Pairs with Cytosine | 72 | |
| 5137920323 | Uracil | The RNA version of thymine. Like thymine, this base also pairs with adenine. | 73 | |
| 5137920324 | Monounsaturated fatty acid | A fatty acid whose molecular structure includes only one double carbon bond. | 74 | |
| 5137920325 | Polyunsaturated fatty acid | A fatty acid with two or more double bonds between the carbon atoms of its hydrocarbon chain | 75 | |
| 5137920326 | substrate | - the molecule upon which an enzyme acts | 76 | |
| 5137920327 | Active site | Region of an enzyme into which a particular substrate fits. | 77 | |
| 5137920328 | Induced fit model | Change in the shape of an enzyme's active site that enhances the fit between the active site and its substrate(s) | 78 | |
| 5137920329 | Cofactors | Non protein molecule that assist enzymes | 79 | |
| 5137920330 | Coenzyme | a type of cofactor (not a protein but sometimes a vitamin) essential for the activity of some enzymes | 80 | |
| 5137920331 | inorganic cofactors | often metal ions, like Fe2+ and Mg2+ | 81 | |
| 5137920332 | ATP | (adenosine triphosphate) main energy source that cells use for most of their work | 82 | |
| 5137920335 | allosteric effector | a molecule that binds to an enzyme at a site other than the active site and affects its activity | 83 | |
| 5137920336 | allosteric activator | binds to the enzyme and induces the enzyme's active form | 84 | |
| 5137920337 | allosteric inhibitor | binds to the enzyme and induces the enzyme's inactive form | 85 | |
| 5137920338 | Feedback inhibition | During ____ the end-product of a series of reactions acts as an allosteric inhibitor & shutting down one of the enzymes which was catalyzing the series | 86 | |
| 5137920339 | Competitive inhibition | a substance that mimics the substrate, inhibits an enzyme by occupying the active site. This prevents the enzyme from catalyzing the substrate. | 87 | |
| 5137920340 | noncompetitive inhibition | A substance that reduces the activity of an enzyme by binding to a location other than the active site, changing its conformation (shape) so that it no longer binds to the substrate. Ex: toxins & antibiotics | 88 | |
| 5137920341 | Cooperativity | a shape change in one active sites of a protein caused by substrate binding is transmitted to all the other active sites, facilitating binding of additional substrate molecules to those active sites. | 89 |
