Help
Options
Didn't know it?
click below
click below
Knew it?
click below
click below
Don't Know
Remaining cards (0)
Know
retry
shuffle
restart
0:00
Embed Code - If you would like this activity on your web page, copy the script below and paste it into your web page.
Normal Size Small Size show me how
Normal Size Small Size show me how
Intro to Cell Bio.
Final exam study guide with terms about DNA replication, transcription and trans
| Term | Definition |
|---|---|
| ATP | holds potential energy. Cells break its phosphoanhydride bonds to release energy |
| Phosphoanhydride bond | bonds phosphate groups in ATP |
| exergonic reaction | a spontaneous reaction, releases energy |
| endergonic reaction | non-spontaneous reaction, usually takes in energy |
| entropy (S) | the measure of disorder in a system |
| enthalpy (H) | amount of potential energy in a system |
| Gibbs Free Energy (G) | the measure of free energy in a system |
| LEO | Loss of Electrons Oxidation |
| GER | Gain of Electrons Reduction |
| Glycolysis | a 10 step process that changes glucose into pyruvate |
| hydrophillic molecules | molecules that are polar and will dissolve in water |
| hydrophobic molecules | molecules that are non-polar and will not dissolve in water |
| water is held together by... | hydrogen bonds |
| the functional group -OH | hydroxyl- |
| functional group -COOH/-COO- | Carboxyl-/ Carboxylate |
| functional group -C=O | carbonyl- |
| functional group PO3^(2-) | Phosphate |
| functional group C-NH2/ C-NH3 | amino |
| Though one hydrogen bond is weak, many hydrogen bonds together are... | strong |
| pH | -log[H3O+] |
| acid | donates protons in solution |
| base | accepts protons in solution |
| atomic weight | # of protons plus neutrons the atom or molecule contains |
| atomic number | # of protons |
| Buffers | weak bases or acids that control the pH in cells |
| types of non-covalent bonds | hydrophobic interactions, electrostatic attractions (ionic bonds, hydrogen bonds, and van der waals attractions) |
| Lipids | composed of fatty acids (steroids, triacylglycerols, cholesterol) |
| saturated fats | fats that have no double bonds and abundant in hydrogen |
| unsaturated fats | fats that have double bonded carbons |
| amphipathic | has both polar and non-polar regions |
| amino acids | monomers of proteins |
| amino acid | made up of an amino group, a carboxylic acid group, an R group, and an alpha carbon |
| residue | a specific amino acid within a protein |
| peptide bond | bonds that link amino acid residues, they are polar covalent bonds |
| methionine | amino acid that is the beginning of all proteins and is found at the N-terminus |
| tertiary structure | the final 3-D shape/ conformation of a protein |
| prion | proteins that, if misfolded, cause cascade of protein misfolding. they are proteinaceous infectious particles |
| quaternary structure | describes the structure when several proteins come together to perform a function |
| secondary structure | describes the structure of a protein when it has an alpha helix or a beta sheet |
| molecular chaperones | assist proteins to fold correctly |
| alpha helical shape formed when... | every 4 alpha carbons the carboxyl group's C=O bonds with N-H (*ONLY peptide atoms involved, never side chains) |
| protein domains | portions of proteins that can independently fold into compact 3-D shapes |
| protein families | proteins that have similar primary and tertiary structures and thus similar functions. (*NOT always similar primary structures) |
| homodimer | two of the same protein that form quaternary structure |
| electron microscopy | useful to see structure of large subunits in proteins |
| ligand | any molecule that binds to a protein |
| binding site | A cavity on a protein where a molecule can bind. mediated by either charge or hydrophillicity |
| Ka | Eq. ass. constant. describes the strength of non-covalent, ***NON-ENZYMATIC** association (no chemical rxn) |
| equilibrium | when there is no net change in G and molecules are in constant motion, coming together and breaking apart at the same rate |
| Kd | 1/Ka |
| allosteric regulator | molecules that bind to proteins (outside of their active site) and change the shape of the protein to regulate function |
| enzyme | molecules that lower the activation energy to reach transition state |
| nuclease | hydrolyses nucleic acids |
| protease | breaks down proteins |
| isomerase | makes an isomer |
| synthase | builds a molecule |
| hydrolase | add water to break apart a molecule |
| Km | concentration of substrate that produces 1/2 rxn rate of Vmax |
| change in enzyme structure | provides most rapid cellular response |
| covalent modifications of proteins | phosphorylation, lipid addition, ubiquitination |
| regulatory protein code | how protein is modified and controlled (stability, activity, binding, or location) |
| feedback inhibition | molecule produced inhibits protein earlier in the metabolic pathway. |
| gamma phosphate of ATP | The most readily available phosphate of ATP |
| Keq | [product]/[reactant] |
Created by:
kimmandigo
Popular Biology sets