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BIO 120 Exam 1
| Term | Definition |
|---|---|
| How many bonds can carbon atoms make? | 4 |
| How and what is attached to the carbon molecule determines... | functionality |
| Isomers | molecules that have the same molecular formula, but different structures |
| Structural Isomers | same molecular formula, but the structure is different |
| Cis isomers | two x's on the same side of a double bond |
| Trans isomers | the two x's are on opposite sides of a double bond |
| Enatiomers | mirror images of each other; often differ in biological activity |
| Functional Groups | a specific configuration of atoms commonly attached to the carbon skeletons of organic molecules and involved in chemical reactions |
| elements | one type of atom |
| Elements of life | carbon, hydrogen, oxygen, nitrogen |
| Molecules(compounds) | 2 or more elements bonded together determined by electrons |
| atom is an | element |
| nucleus | contains protons and neutrons |
| electron shells (cloud) | contains electrons, the more shells, the more unstable |
| neutrons | neutral charge |
| protons | positive charge |
| electrons | negative charge |
| atomic number | number of protons and electrons in an atom |
| atomic mass/mass number | number of protons and neutrons |
| Find the number of neutrons | subtract the mass number from the atomic number |
| how many electrons in the first shell | 2 |
| how many electrons in the second shell? | 8 |
| why does bonding happen? | to fill orbital shells, which makes the atom stable |
| what is needed to be a stable element? | 8 electrons in the valence shell |
| valence shell | outer shell |
| ionic bonding | donation of an electron by one element and the acception of that electron by another element |
| in ionic bonding, what happens to the charge of the atom that donates the electron? | it becomes more positively charged |
| in ionic bonding, what happens to the charge of the atom that receives the electron? | it becomes more negatively charged |
| polarity | A lack of symmetry; structural differences in opposite ends of an organism or structure |
| covalent bonding | sharing of electrons between atoms |
| two ways of covalent bonding | equally/symmetrical- no charge, unequally/asymmetrical- charge (one side is positive, one side is negative) |
| electronegativity | the attraction of a given atom for the electrons of a covalent bond |
| chemical reactions are | reversible |
| why does water behave differently? | the electronegativity of oxygen |
| properties of water | polar covalent bonds, hydrogen bonds, ability to moderate temperature, expansion upon freezing, cohesive behavior, adhesive behavior, and universal solvent |
| hydrogen bonds | weak bonds between molecules when they are oppositely charged (polarity) |
| specific heat | the amount of energy required to raise the temperature of 1 gram of a substance by 1 degree Celsius |
| why does water have a high specific heat? | hydrogen bonding |
| why does water expand when frozen? | hydrogen bonds between water molecules hold them together, and when frozen, the bonds stabilize and expand |
| adhesion | attraction between molecules of different substances |
| cohesion | attraction between molecules of the same substance |
| solution | a homogeneous mixture of two or more substances |
| solvent | the dissolving agent of a solution |
| solute | substance that is dissolved in a solution |
| the solute needs to be able to... | disrupt the bonds in water to dissolve |
| hydrophobic | nonpolar covalent bond that is unable to disrupt hydrogen bonds between water |
| hydrophilic | solutes that have a charge (ionic bond or polar covalent bond) and are able to disrupt hydrogen bonds between water |
| amphiphilic | both hydrophobic and hydrophilic |
| basic solution | less hydrogen, more OH- |
| acidic solution | more hydrogen, less OH- |
| neutral pH | normal |
| Properties of elements depend on | its structure |
| Polar Covalent Bond | A covalent bond between atoms that differ in electronegativity. The shared electrons are pulled closer to the more electronegative atom, making it slightly negative and the other atom slightly positive |
| Nonpolar Covalent Bond | A type of covalent bond in which electrons are shared equally between two atoms of similar electronegativity |
| Variations in the reactive properties of different organic molecules are most closely associated with... | the presence or absence of functional groups |
| What characteristic is responsible for the complexity and variety of organic molecules? | the chemical versatility of carbon atoms |
| Monomers | small unit that can join together to form polymers |
| Polymer | A long molecule consisting of many similar or identical monomers linked together |
| Macromolecules | carbohydrates, proteins, and nucleic acids |
| Macromolecules do not include | lipids |
| 4 major types of biological molecules | carbohydrates, lipids, proteins, nucleic acids |
| Polymers are typically the same thing as | macromolecules |
| Dehydration reaction | connects a monomer to another monomer or a polymer through covalent bonding of a hydroxyl group and a hydrogen resulting in the loss of a water molecule |
| Organic Chemistry | the study of carbon compounds |
| Hydrolysis | A water molecule is used up in the breaking of a bond between two monomers. An H is added to one monomer, and an OH is added to the other |
| Functions of carbohydrates | Source and storage of energy, source of carbon, and structural roles |
| Monomer name for carbohydrates | monosaccharide |
| Polymer name for carbohydrates | polysaccharide |
| Disaccharide | a sugar composed of two monosaccharides |
| Glycosidic Linkage | a covalent bond formed between two monosaccharides by a dehydration reaction (growing chain) |
| The shape and linkage of polysaccharides changes... | functionality |
| Hydrocarbons | long chains of carbon and hydrogen (hydrophobic, nonpolar) |
| What type of bond do lipids have? | Covalent nonpolar bonds |
| Unifying feature of lipids | having little or no affinity for water |
| Functions of lipids | long term energy storage, protective molecules, structural components of membranes, and hormones |
| Triglyceride | lipid made of three fatty acid chains and a polar glycerol molecule that provides fat storage |
| Ester Linkage | when a hydroxyl from glycerol and carbon from a hydrocarbon have a dehydration reaction (lipid) |
| Saturated Fat | lipid where every carbon is saturated with fat, solid at room temps (mostly animal fats) |
| Unsaturated Fat | lipid where not every carbon is bonded with a hydrogen some are double bonded carbon molecules (cis double bonds), liquid at room temp (plant-based) |
| Phospholipids | make up cell membranes; has a glycerol and phosphate group head (hydrophilic and polar) with two fatty acid chain tails (hydrophobic and nonpolar) |
| Sterols | a type of lipid with four carbon rings that are communicators (hormones); no ester linkage |
| Function of proteins | Keep you alive, regulate chemical processes, help you defend against invaders, and help you feel emotions |
| Monomer name of proteins | amino acids |
| Polymer name of proteins | polypeptide |
| Linkage bond of proteins | peptide bond |
| Functional groups involved in proteins | carboxyl, amino |
| Functional groups involved in lipids | carboxyl, hydroxyl |
| Functional groups involved with nucleic acids | phosphate |
| Function of nucleic acids | store, transmit, and help express hereditary information |
| Monomer name of nucleic acids | nucleotides |
| Polymer name of nucleic acids | nucleic acids (DNA and RNA) |
| What is the functional group difference between DNA and RNA? | RNA has a hydroxyl group |
| Enzymes | one type of protein |
| Side chain/ R group | a chemical group that is attached to a core part of the molecule called the "main chain" or backbone |
| Nonpolar side chains are | hydrophobic (no charge) |
| Polar side chains are | hydrophilic (positive or negative charge) |
| Peptide bond | dehydration reaction bond between a carboxyl and an amino group (protein) |
| A proteins structure correlates with its... | function |
| Primary structure | the sequence of amino acids in a protein |
| Secondary structure | hydrogen bonds between the backbone of the polypeptide forming coils/sheets |
| Tertiary structure | global arrangement of secondary structure; R groups/side chains interact |
| Quaternary structure | the arrangement of multiple protein molecules in a complex; two or more polypeptide chains form one macromolecule |
| Denaturation | loss of shape and function of protein |
| DNA | double-stranded helix, only in nucleus, thymine (base), deoxyribose (sugar), stable molecule |
| RNA | single-stranded, can leave nucleus in cytoplasm, uracil (base), ribose (sugar), less stable |
Created by:
kkade
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