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ap bio unit 1
unit 1 - biochemistry
| Term | Definition |
|---|---|
| starch | carb, monomer:glucose (1000s), storage of energy for plants |
| glycogen | carb, monomer:glucose (1000s), storage of energy in liver/muscles |
| cellulose | carb, monomer:glucose (1000s), cell walls (fiber) |
| insulin (protein) | protein, monomer:amino acid (1000s), lowers blood sugar |
| hemoglobin (protein) | protein, monomer:amino acid (1000s), carry O2 |
| triglyceride (fat) | lipid, 1 glycerol, 3 fatty acids, storage of energy |
| DNA/RNA | nucleic acid, monomer:nucleotide (billions), genetic coding |
| dehydration synthesis | condensation reaction, covalently bonding monomers to form polymers by REMOVING a OH from one monomer and a H from the other |
| hydrolisis | breaking apart polymers into monomers by ADDING H2O (OH to one molecule)(H to the other), what happens when we digest our food |
| carbohydrate structural ratio | CH2O (H-C-OH); glucose=C6H12O6 |
| amino acid structure | one amino group, carbon, one acid (carboxyl) group, R group underneath |
| fatty acid structure | hydrocarbon chain and acid (carboxyl) group |
| nucleotide structure | five-carbon sugar, phosphate group, nitrogenous base |
| protein monomer | amino acid |
| carbohydrate monomer | glucose |
| lipid monomer | fatty acid, glycerol |
| nucleic acid monomer | nucleotide |
| bonds between amino acids | peptide bonds |
| glucose shape | RING (occasionally chain) |
| isomers | same molecular formula, different shape |
| polar bonds | high difference in electronegativity, if O or N is bonded with weak C or H |
| hydrophobic | nonpolar, does not disassociate in water |
| hydrophilic | polar, mixes with water |
| chemical properties of an atom are determined by the | number of valence electrons |
| a nonpolar covalent bond occurs when | a molecule's constituent atoms attract the electrons equally |
| hydrogen bonds are | between MOLECULES not atoms |
| full valence shell= | inert (Ar) |
| atoms with an ALMOST full valence shell | have a high electronegativity |
| atoms that have the same amount of valence electrons | have similar characteristics |
| HONC | 1234 |
| control | what is not changing (usually a specific group, test tube etc) |
| dependent variable | what is measured, what changes uncontrollably |
| independent variable | is changed purposely |
| ions are formed when | a neutral atoms gains or loses an electron |
| bond that requires the most energy to break | covalent bond |
| electron energy levels | 2-->8-->8; when one level is full it goes to the other, electrons do not share orbitals unless they have to, 2 per orbital if needed |
| the number of protons determined the | atomic number |
| in an ionic bond... | there is a mutual attraction between two charged atoms, INVOLVES ELECTRON TRANSFER |
| the cohesiveness (stickiness to itself) among water molecules is directly due to... | hydrogen bonds |
| H--O*--*H | the highlighted bond in water is a polar covalent bond |
| catalysts/enzymes | lower the activation energy NEEDED |
| phospholipids | molecules with hydrophilic and hydrophobic ends |
| adding H to an unsaturated fat will make it more saturated | true |
| chemical reactions that require a net input of free energy to proceed | endergonic reactions |
| glucose+glucose= | maltose |
| carbon atoms can form so many different chemical compounds because | its outer energy level contains four electrons |
| two classes or organic compounds that provide energy for living systems include | fats (lipids), and polysaccharides (carbs) |
| when a protein is denatured the _______ bonds remain intact | peptide |
| C and N in a polypeptide chain... | are bonded linearly to form the backbone |
| competitive inhibitor | compete with substrate molecules for active site and block it |
| noncompetitive inhibitor | bind to a second site on the enzyme and induce a conformational change |
| properties of water | high heat capacity, 3 naturally occurring states, universal solvent, expands as a solid, neutral pH, cohesion, surface tensions, adhesion, capillary action, doesn't evaporate as quickly as a np molecules |
| unstable atoms | have vacancies in their outer energy level; will react with other atoms to achieve stability |
| ionic bond | one or more electrons are completely transferred to another atoms, positive attracts negative (electrostatic attraction) |
| nonpolar covalent bond | electrons are SHARED EQUALLY between atoms |
| polar covalent bond | eletctrons are SHARED UNEQUALLY, closer to 1 atoms than the other because of difference in electronegativity |
| N, O | high electronegativity |
| H, C | weak electronegativity |
| hydrogen bonds | attractions between MOLECULES that have oppositely charged regions due to POLAR COVALENT bonds |
| covalent>ionic>h bonding | strengths of bonds |
| hydrocarbon chains | provide backbone for organic molecules |
| functional groups | responsible for unique chemical properties of organic molecules |
| lipids have _____ energy than carbs and burn _____ | more, slower |
| glycerol | made up of alcohol groups |
| unsaturated fat | Cs are double bonded |
| saturated fat | no double C bonds |
| phospholipids | 1 glycerol, 2 fatty acids, 1 phosphate group; makes membranes |
| protein functions | structural support, enzymes, storage, transport, signaling, movement, defense against germs |
| how many different amino acids are there? | 20 |
| cystine has ____ in ____ | S, R group |
| polypeptide | long strand of amino acids |
| bioenergetics | the flow of energy in living systems |
| free energy (delta G) | energy in an organized state that is capable of doing work |
| 1st law of thermodynamics | energy can be transformed but can neither by created nor destroyed |
| 2nd law of thermodynamics | the energy in the universe is becoming increasingly disorganized (entropy), organized states of matter contain high amounts of free energy but during transformations some free energy is lost |
| exergonic reaction | releases energy, reactants contain more energy than products |
| enzymes | lower activation energy NEEDED, special protein (shape), molecules must be close in proximity and in particular 3D orientation, speed up rate of reaction, does not affect products, can be reused |
| active site | where reactions happen in an enzyme, will only fit certain molecules, determined by R groups, opposites attract, R group folding causes shape |
| extreme heat/pH change will | denature an enzyme's shape |
| substrate | the reactant that will work with the enzyme |
| primary level of complexity | unique sequence of amino acids, determined by DNA |
| second level of complexity | alpha heliz (spiral), beta pleated sheet (zigzag) |
| tertiary level of complexity | 3D globular shape, caused by R groups |
| disulfide bond | S-S, hold 3D shape together |
| quaternary level of complexity | 3D shape of 2 or more polypeptide strands |
Created by:
tpolinsky24
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