Biochemistry - AP Biology Flashcards
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6680121597 | Polar Molecule | An asymmetrical molecule with a slight charge (dipole); that is hydrophilic (water loving) ex: water | 0 | |
6680121598 | Hydrophilic | Water loving | 1 | |
6680121599 | Nonpolar Molecule | A symmetrical or balanced molecule with no charge; hydrophobic (water fearing) ex: lipid | 2 | |
6680121600 | Hydrophobic | Water fearing | 3 | |
6680121601 | Properties of Water | Ice is less dense than water Very polar Strong H2 attractions High specific heat High heat of vaporization Universal solvent Strong cohesion property | 4 | |
6680121602 | Cohesion | Attraction of water molecules to one another | 5 | |
6680121603 | Adhesion | Attraction of water molecules to other substances | 6 | |
6680121604 | pH | measure of acidity pH < 7 is acidic pH > 7 is basic pH = 7 is neutral acid = [H+] base = [OH-] | 7 | |
6680121605 | Carbohydrates | Consist of carbon, hydrogen, and oxygen in a 1:2:1 ratio Polymers of monosaccharides Function: quick energy Ex: glucose, lactose, sucrose, maltose | ![]() | 8 |
6680121606 | Lipids | Consists of chains of carbon, hydrogen, and oxygen Hydrophobic Function: energy storage, structure, steroids, hormones | ![]() | 9 |
6680121607 | Steroid | Lipid made of 4 carbon rings | ![]() | 10 |
6680121608 | Proteins | Consists of S, P, C, O, H, and N R-group is variable region of amino acid Polymers of amino acids Function: growth and repair | ![]() | 11 |
6680121609 | Protein Structure | Primary structure Secondary structure Tertiary structure Quaternary structure | ![]() | 12 |
6680121610 | Primary Structure (Protein) | Determined by the amino acid sequence of the chain attached by peptide bonds | ![]() | 13 |
6680121611 | Secondary Structure (Protein) | Determined by intermolecular hydrogen bonding within the chain alpha helix and beta pleated sheets | ![]() | 14 |
6680121612 | Tertiary Structure (Protein) | 3-D shape determined by the folding and interactions between amino acids (e.g., nonpolar, polar, disulfide bridges) | ![]() | 15 |
6680121613 | Quaternary Structure (Protein) | Determined by the interactions between 2 or more chains of polypeptides | ![]() | 16 |
6680121614 | Nucleic Acids | RNA, DNA, ATP Polymers of nucleotides Nucleotides consist of sugar, phosphate, and nitrogen base | ![]() | 17 |
6680121615 | Enzyme Characteristics | Organic catalysts that increase the rate of reactions by lowering the activation energy. Function based by induced fit. Denature at specific temperature and pH. | ![]() | 18 |
6680121616 | Activation Energy | Energy required to begin a reaction | ![]() | 19 |
6680121617 | Substrate | The molecule an enzyme works on (A) | ![]() | 20 |
6680121618 | Active Site | Where enzyme and substrate bond (induced fit) | ![]() | 21 |
6680121619 | Induced Fit Model | As a substrate enters the active site of an enzyme, it induces that enzyme to alter its shape slightly so the two bond properly | 22 | |
6680121620 | Competitive Inhibition | Two different substrates resemble each other and compete for the same active site on one enzyme | 23 | |
6680121621 | Noncompetitive Inhibition | The enzyme has more than one active site and the substrates do not resemble each other. When one substrate binds to its active site, the second enzyme cannot bind; thus, no product is formed. | 24 | |
6680121622 | Allosteric Inhibition | Involves an enzyme with two active sites: one for a substrate, one for an inhibitor. The enzyme can alternate between two different confirmations: one active, on inactive. Formation of product is inhibited when the inhibitor binds to the inhibitor site and the enzyme undergoes a conformational change. The active site is altered, and the substrate cannot bind to the enzyme. | ![]() | 25 |
6680136753 | Amino Acid | monomer of proteins 20 total types one end has a carboxyl group one end has an amino group has center carbon with variable R group which determines chemical properties | 26 | |
6680147977 | amphipathic | a molecule having both hydrophilic and hydrophobic parts example: phospholipids with hydrophilic heads and hydrophobic tails | 27 | |
6680156044 | anabolic | chemical reaction that builds molecules such as photosynthesis | 28 | |
6680159982 | catabolic | chemical reaction that breaks down molecules such as respiration | 29 | |
6680166287 | catalyst | a substance that increases the rate of a chemical reaction | 30 | |
6680168220 | coenzyme | An organic molecule that is required for the proper functioning of an enzyme | 31 | |
6680371277 | denaturation | A process in which a protein loses it's shape | 32 | |
6680380507 | disaccharide | two sugars bonded together examples: lactose, sucrose | 33 | |
6680385898 | hydrogen bond | weak attraction between slightly positive hydrogen atoms of a polar covalent bond in one molecules is attracted to the slightly negative atom of a polar covalent bond in another molecule or in another region of the same molecule | 34 | |
6680407704 | macromolecule | a giant molecule formed by joining of smaller molecules, usually by dehydration synthesis | 35 | |
6680413134 | monomer | the subunit that serves as the building block of a polymer | 36 | |
6680449762 | monosaccharide | simple sugar | 37 | |
6680458726 | nucleotide | building block of nucleic acids consisting of a five-carbon sugar, nitrogenous base, and 1-3 phosphate groups | 38 | |
6680520348 | Peptide bond | Covalent bond between the carboxyl group of one amino acid and the amino group | 39 | |
6680537343 | polymer | a long molecule consisting of many similar or identical monomers in a chain | 40 |