AP Biology Proteins Flashcards
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.
Terms : Hide Images [1]
| 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 |