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