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Physio Ch. 3

QuestionAnswer
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