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Physio Ch. 3
| Question | Answer |
|---|---|
| eukaryotic cells have a | cell membrane, nucleus and cytoplasm |
| the cell membrane determines | regulation |
| cell membrane is made of a...and contains a... | phospholipid bilayer...protein mosaic |
| the protein mosaic has two types of proteins | integral (transmembrane) and peripheral |
| integral proteins are actually part of...and are... | the cell membrane...amphipathic |
| peripheral proteins perform | regulatory action |
| nucleus contains | DNA, RNA, and proteins |
| the proteins in the nucleus help with the...and the... | structure of chromosomes...functioning of DNA and RNA |
| the cytoplasm contains | cytosol and organelles |
| proteins are the..of the cell | work horses |
| protein synthesis has two steps | transcription and translation |
| the purpose of synthesis is | to code and decode genetic information to create new sets of amino acids |
| transcription | DNA coding into mRNA code |
| transcription occurs in the | nucleus |
| translation occurs in the | cytoplasm, more specifically a ribosome |
| translation | mRNA code to make amino acids (aka nucleic language to protein language) |
| transcription uses...and they are... | complementary base pairing...T=A, A=U, G=C, C=G |
| a codon is a | coding unit |
| 3 codons is an | amino acid instruction |
| Only one side of...is used in translation | DNA helix |
| translation leaves the...and finds... | nucleus...ribosome to do translation |
| mRNA | triplet codons |
| tRNA | anticodons which carry amino acids |
| anticodons determine | what amino acid is built |
| anticodons are the | tRNA base pair of mRNA |
| rRNA and associated proteins | polypeptide construction |
| key to protein structure | is its shape |
| start/stop codon | polypeptide chain |
| mutation is a | change in the DNA |
| mutations can have 2 affects | no effect or an altered protein function |
| no effect means there was a | base substitution and degenerate code which means the same amino acid was produced from a different sequence of amino acids (20 amino acids but 64 possible codons) |
| altered protein function can either be a | minor or major effect or it can lead to cell death |
| mino effect means there was no | change in protein binding site |
| major effect means there was | a change in biding site |
| cell death means | nonfunctional essential protein |
| protein degredation regulates the | amount of protein present in cells |
| ubiquitin is a..that binds to.. | peptide (small chain of amino acids)...proteins |
| ubiquitin is a marker for...and for...to bind to it | cell to be destroyed...a proteasome |
| proteasome are vesicles with | enzymes for protein digestion |
| proteasomes contain a | protein complex that denatures and hydrolyzes protein |
| proteins without a signal sequence(...) attached are in the... | ubiquitin...cytosol |
| protein with signal sequence gets sent to the...then the...where it is packagedinto... | RER...golgi...secretory vesicles for exocytosis or lysosome for internal storage |
| ligands area also called...and they... | substrate..bind to protein |
| binding site is where the...binds to the.. | ligand...protein |
| binding site bonds are usually | weak |
| the binding site depends largly upon the | shape |
| active or functional site is where | the ligand and protein actually pair up |
| regulatory site is used for...which ... | modulation...modifies how protein functions |
| chemical specificity | only some proteins can work with some ligands |
| affinity | how well does a bind form (strength) |
| affinity is the strength of | ligand-protein bond |
| saturation is the % | of protein bound with a ligand |
| saturation depends on two things | ligand concentration and affinity |
| competition means that...ligands can... | alternate....use same binding site on protein |
| protein regulation is done via | allosteric modulation or covalent modulation |
| protein regulation is very important for | cells to be on time and in the right anount |
| allosteric modulation is when a...binds in orderr to... | modulator molecule...alter shape of protein to alter its function |
| allosteric modulation is done via | noncovalent bonding with a modulator molecule |
| allosteric modulation can alter the function of the protein by | turning on or off the function through a changed shape |
| covalent modulation has a..iinstead of a... | phosphate group...modulator molecule |
| covalent modulation is built via | covalent bondsand phosphate groups |
| enzyes =...but...do not=... | proteins...proteins...enzymes |
| enzymes are organic....meaning they... | catalysts...make reaction happen faster |
| enzymes can't cause | an impossible reaction to happen |
| enzyme + substrate ->...-> | E- S complex...enzyme + product |
| example of enzymes would be maltose -> | glucose + glucose |
| maltASE is the | enzyme that breaks down maltose |
| maltase tells the name of the | ligand |
| carbonic acid (H2CO3) -> | CO2 + H20 |
| what tells the name of the reaction? | carbonic anahydrase |
| cofactors can either be | allosteric modulators or coenzyme |
| allosteric modulators change the... | shape so enzyme does or doesn't work (enzyme conformation) |
| cofactors promote | enzyme activity |
| coenzymes are...that act as a... | organic molecule...substrate |
| coenzymes are...meaning they are part of the reaction but... | recycled...never used up (same as enzyme) |
| regulation of enzyme mediated reactions depend on what 3 things | enzyme concentration, affinity, allosteric or covalent modulation |
| enzyme concentration is...v...and the... | high...low enzyme concentration...rate of reaction |
| affinity is ...v...and the... | high...low enzyme affinity...rate of reaction |
| allosteric or covalent modulation | activation & inhibition and rate of reaction |
| endproducts of reaction are used to | regulate |
| multienzyme mediated reactions depend on | metabolic pathways, rate-limiting reaction and product inhibition |
| product inhibition is a form of | negative feedback |
| metabolic pathways include | cellular respiration and anabolism |
| cellular respiration is what keeps us....and is a form of... | alive...catabolism |
| cellular respiration usually starts with...and goes to(->).... | glucose + water +oxygen...carbon dioxide +water +atp |
| variations of cellular respiration | glycogen, fats and proteins |
| cellular respiration is partly | reversible through anabolism |
| big pictures is | glycolysis (aerobic or fermentation if its anaerobic) |
| glycolysis starts with...and -> | glucose...2 pyruvate |
| glycolysis' enzymes are in the | cytosol |
| glycolysis produces | 2 ATP and 2 NADH |
| NADH is an | intermediate form of energy |
| fermentation starts with...->... | 2 pyruvate...2 lactate |
| fermentation occurs inthe...and is... | cytosol...anaerobic |
| fermentation uses 2...from...and produces... | NADH...glycolysis...2 atp |
| oxdation of pyruvate starts with..->... | 2 pyruvate...2 acetyl coA + 2 CO2 |
| oxdation of pyruvate removes...then converts... | energy sources...pyruvate into another molecule that can go on and be used in next step of cellular respiration |
| ox of py occurs in the...and is...and produces... | mitochondrion...aerobic...2 NADH |
| what comes after ox of py | krebs or citric acid cycle |
| citric acid cycle starts with...-> | 2 acetyl CoA...4 CO2 |
| krebs occurs in the...is...and produces... | mitochondrion...aerobic...2 atp, 6 nadh, 2 fadh |
| krebs cycle finishes | breaking down original glucose molecule |
| oxidative phosphorylation is when...is produced | atp |
| ox phosph occurs in the..and is... | mito...aerobic |
| ox phosph uses 10...-> | NADH...10 NAD + 28 ATP |
| ox phosph also uses 2 FADH-> | 2 FAD + 4 ATP |
| 1 nadh =...so the problem is... | 3 atp...some atp is used going from cytosol to mito |
| cellular respiration all together produces | 34-38 ATP |
| aerobic respiration produces | higher amounts of atp than anaerobic |
| the body utilizes other substances such as...by incorporating them along.. | carbos, triglycerides and proteins...the path of cellular respiration |
| other carbohydrates- most get converted to...for... | glucose...breakdown |
| glycogenolysis | breaks down glycogen |
| glycogenolysis: glycogen->...-> | glucose 6 phosphate....pyruvate |
| glycogenolysis occurs mainly in the | liver and skeletal muscles where its stored |
| triglycerides use..for... | glycerol...glycolysis |
| triglycerides: fatty acids ->...via the... | smaller fatty acids + acetyl coA...krebs cycle |
| proteolysis of proteins: proteins -> | amino acids |
| deamination of amino acids occurs in the...and means you take off a... | liver...nitrogen |
| deamination of amino acids: amino acid ->...to..or.. | keto acid + ammonia... pyruvate...krebs cycle |
| transamination of amino acids means that some amino acids MUST | come from diet |
| transamination of amino acids: produce | a different amino acid |
| the body makes organic molecules via | anabolism |
| glucose -> | fatty acids |
| glycerol <->...to resupply... | glucose...liver and muscles |
| fatty acids <->...through the.. | amino acids ...krebs cycle |
| amino acids <->...via... | glucose...pyruvate |
| carbos convert | glucose to other carbos |
| carbos also convert glucose to...for.. | glycogen..storage |
| carbos convert other carbos to...from.. | glucose...glycogen that is in storage in liver and skeletal muscles |
| gluconeogensis comes from a | non carbo source |
| gluconeogensis starts with...->...-> | pyruvate...glucose 6 phosphate...glucose |
| gluconeogensis occurs in the | liver and kidneys |
| fatty acids are used in the...order...and occur in the... | reverse...of the catabolic pathway...cytosol |
| amino acids & proteins convert glucose -> | keto acids |
| transamination of keto acids makes | new amino acids |
| ...essential amino acids from diet | 9 |
| essential nutrients can't | be produced by the body |
| essential nutrients are...but can't be... | necessary...manufactured (if you can make them you can't make them in big enough amounts) |
Created by:
handrzej
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