For the AP Exam, students need to be able to identify the structure of an amino acid, and the primary, secondary, tertiary, and quaternary structures of proteins.
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| 7358173848 | *proteins | *a macromolecule made chains of amino acids | 0 | |
| 7397543287 | *Carbon, Hydrogen, Oxygen, Nitrogen (CHON) | *elements that make up a protein | 1 | |
| 7358177816 | categories of proteins | structural proteins, storage proteins, transport proteins, defensive proteins, and enzymes | 2 | |
| 7358467726 | *enzymes | *proteins that speed up chemical reactions (reduce the activation energy required) | 3 | |
| 7358470858 | defensive proteins | proteins that recognize and respond to particles that invade the organism such as antibodies | 4 | |
| 7358478263 | hormonal and regulatory proteins | proteins that control physiological processes such as insulin | 5 | |
| 7358482854 | receptor proteins | proteins that receive and respond to molecular signals from inside and outside the cell | 6 | |
| 7358489181 | storage proteins | proteins that store chemical building blocks for later use | 7 | |
| 7358492221 | structural proteins | proteins that provide physical stability such as collagen | 8 | |
| 7358495085 | transport proteins | proteins that carry substances within the organism, such as hemoglobin | 9 | |
| 7358499681 | genetic regulatory proteins | proteins that regulate how, when, and to what extent a gene is expressed | 10 | |
| 7358202515 | *amino acid | *building block (monomer) of proteins, composed of an amino group and a carboxyl group, a hydrogen atom, and an R-group |  | 11 |
| 7397562072 | *a carboxyl group, an amino group, a central Carbon, a Hydrogen, and an R-group | *structure of an amino acid | 12 | |
| 7358240130 | *20 | *the number of different amino acids that occur extensively in all living organisms | 13 | |
| 7358253032 | glycine | the simplest amino acid, with a Hydrogen atom for the R-group; small enough to fit into tight corners in the interior of a protein molecule |  | 14 |
| 7358526356 | proline | amino acid that lack a hydrogen atom in the amino group resulting in a ring structure; often functions to stabilize bends or loops in proteins |  | 15 |
| 7358538557 | cysteine | amino acid that has a terminal sulfhydrl group, and can react with another cysteine and form a disulfide bridge |  | 16 |
| 7358544511 | disulfide bridge | covalent bond formed between two cysteine amino acids when their SH groups become oxidized; this helps determine how a protein folds |  | 17 |
| 7358235881 | *dehydration synthesis | *process that bond an amino acid to another amino acids (forms peptide bond) | 18 | |
| 7358550897 | oxidization | refers to a molecule that has lost electrons |  | 19 |
| 7358555825 | reduction | refers to a molecule that has gained electrons | | 20 |
| 7358641918 | LEO (the lion) says GER | LEO- loss of electrons is oxidation GER- gain of electrons is reduction | 21 | |
| 7358220046 | *peptide bond | *covalent bond formed between amino acids |  | 22 |
| 7358452786 | *from amino group to carboxyl group (N-C-C+N-C-C) | *order that the amino acids join together | 23 | |
| 7358225084 | *polypeptide chain | *a long line of amino acids bonded together by peptide bonds |  | 24 |
| 7358210096 | *R-group | *stands for the rest of the compound, different for each kind of amino acid, giving the amino acid its properties |  | 25 |
| 7358273491 | *properties the R-group may give the amino acid | *hydrophilic or hydrophobic, polar or nonpolar, acidic or basic | 26 | |
| 7358208510 | side chain | another name for the R-group |  | 27 |
| 7358280558 | four levels of a proteins structure | primary structure, secondary structure, tertiary structure, quaternary structure | 28 | |
| 7358286693 | *primary structure | *the order of amino acids in a peptide chain that makes up a protein |  | 29 |
| 7358309083 | *secondary structure | *three-dimensional shape that occurs from the hydrogen bonding between the amino and carboxyl groups (the backbone) of nearby amino acids; may be shaped as an alpha helix or a beta pleated sheet |  | 30 |
| 7358332399 | alpha helix | secondary structure of an amino acid shaped like a spiral |  | 31 |
| 7358337332 | beta pleated sheet | secondary structure of an amino acid shaped like pleats on a skirt |  | 32 |
| 7358324733 | fibrous proteins | proteins whose shapes are dominated by beta pleated sheet or alpha helix, like collagen |  | 33 |
| 7358346302 | *tertiary structure | *additional three dimensional shaping to a secondary structure due to interactions of the R-groups |  | 34 |
| 7358353981 | globular proteins | proteins whose shape is dominated by the additional three-dimensional shaping of a tertiary structure, like hemoblobin |  | 35 |
| 7358621195 | *denatured | *a change in the shape of a protein due to chemical treatments, temperature, change of pH, or high concentrations of polar or nonpolar substances; may or may not be irreversible |  | 36 |
| 7358374796 | *quaternary structure | *a protein that is assembled from two or more peptide chains; hemoglobin consists of four peptide chains that are held together by hydrogen bonding and interactions among R-groups |  | 37 |
| 7358590304 | *hydrogen bonds | *bond that occurs between R-groups that stabilize folds in proteins | 38 | |
| 7358594983 | *hydrophobic R-groups | *move together to the interior of a protein, away from water | 39 | |
| 7358604523 | van der Waals interactions | bond-like interaction that stabilize nearby hydrophobic R-groups | 40 | |
| 7358608019 | ionic interactions | bond that forms between oppositely charged (positive and negative) R-groups |  | 41 |
| 7358616221 | salt bridge | another name for ionic interactions that occur between oppositely charged (positive and negative) R-groups |  | 42 |
