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139 Terms
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unsaturated fatty acid
fatty acid w unsaturated carbon chain (double bond between carbons in the chain), usually liquid, plants and fish
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saturated fatty acid
fatty acid w fully saturated carbon chain (no double bonds), solid at room temp, animals
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C3H8O3, lipid monomer that links other lipids, usually fatty acid chains
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protein monomer
amino acids, have amino and carboxyl groups and R functional group (determines function)
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carbohydrate monomer
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nucleic acid monomers
nucleotides, phosphate group, pentose sugar, and nitrogenous base
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lipid functions
barriers (cell membranes), energy storage
carbohydrate basic formula
carbohydrate functions
energy storage, structural support
lipid monomer type, negative charged phosphate head, two nonpolar fatty acid chains, amphipathic (diff spots are polar vs nonpolar)
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polarity of water =
unequal sharing of electrons, resulting in partial pos charge in hydrogens and partial neg in oxygen, hydrogen bonding with other charged molecules
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same types of molecules bind together (usually weaker bonds)
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different types of molecules bind (stick) together (usually weaker bonds)
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surface tension
air is less dense and nonpolar, less binding to water molecules, more binding cohesion, water sticks together and resists force
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capillary action
adhesion to the sides of the container and cohesion to adject water molecules allow water to climb against gravity, thinner tube goes higher (pressure differential encourages climb)
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specific heat
amount of heat that must be absorbed or lost for 1g of the substance to change temp by 1 deg C
specific heat of water is high bc...
hydrogen bonds between molecules take energy to break, in order to heat water (move molecules faster) those bonds need to be broken
bc specific heat of water is ..., it is good for...
high, cooling and regulating internal temps (resists temp change)
breaking hydrogen bonds ... energy
requires/absorbs (endo)
making hydrogen bonds... energy
gives off/releases (exo)
water ... when freezing bc...
expands, molecules orient themselves in matrix position that is more spread out to balance charges
hydration shells
water molecules gathered around a charged particles after dissolving it, all molecules should be oriented specifically
increase H+ or H3O+ (hydronium) concentration
increase OH- concentration (decrease H+)
stabilize pH by minimizing effects of strong acids and bases
standard deviation
how much data points differ from the mean
x bar =
n =
number of data points
higher standard deviation...
lower reliability
standard error
represents uncertainty, sample size and variability (smaller standard error, more likely mean is accurate generalization)
error bars
usually 2SEM, show the standard error, overlap = no statistical significance
OH, polar, makes hydrophilic
-NH2, often in bases, in amino acids with carboxyl
-COOH, carboxylic acid group (dissociates into acid in water), in amino acids with amino
-CH3, nonpolar, binds to cytosine to promote gene expression
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open, methylated DNA
closed, wrapped around histones, unmethylated
-PO4 2-, negative charge = hydrophilic, in phospholipids and nucleotides
-SH, crosslinked molecules, when bound S-S
carbohydrate bond
glycosidic bond
2 bonded monosaccs, maltose, sucrose, lactose
staches, glycogen, cellulose - long term energy storage and structure
plant cell walls
bacterial cell walls
fungal cell walls, arthropod exoskeletons
lipid bond
ester bond
artificially adding hydrogen to carbon chains in fats to saturate them
endomembrane system pathway
synthesize protein in ER, go inside ER, vesicle to golgi, absorbed thru cis face, packaging and tagging, exit thru trans face, vesicle to membrane (fuse w membranes along the way)
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smooth ER
manufactures and replenishes the lipids (phospholipids mostly) consumed in the cell
animal sterol, produced in liver, stabilizes membrane
testosterone and estradiol
hormones (steroids), 4 ring structure
protein based hormones
bind to receptors on cell membrane, don't acc enter, trigger internal signalling
lipid based hormones
because membrane also lipid, can enter the cell itself, trigger signaling once inside of the cell
lipids, alcohol chain and fatty acid chain, insulate from water loss
protein functions
literally everything, cell functions, catalysts (enzymes), cell communication, structure (histones, cytoskeleton?), transport (motor proteins)
protein synthesis location
ribosomes, proteins the will be in the cytosol synthesized in free ribosomes, proteins secreted or in plasma membrane synthesized in bound ribosomes (er)
protein function determined by...
sequence of amino acids and R group interactions (20 diff R groups)
protein bond
peptide bonds
genetic code
triplet code of codons and which amino acids they relate to
primary protein structure
linear, chain of amino acids
secondary protein stucture
hydrogen bonding between near R groups, alpha helices and beta pleated sheets
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tertiary protein structure
3D shape stabilized by R group interactions, hydrophobic, disulfide bridges, ionic bonds, folded into shape, for some proteins final
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quaternary protein structure
association of multiple peptides (multiple subunits), usually weaker bonds, only some proteins
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protein unraveling (degrading) due to change of environment (temp, pH, etc)
2 types of nucleic acids
DNA (deoxy), RNA (ribo)
cytosine, thymine, uracil (t in rna), single rings
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adenine, guanine, double rings, larger
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nucleic acid bonds across the helix
A - T (2 h bonds) G - C (3 h bonds)
nucleotide bonds
phosphodiester bonds
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antiparallel orientation
sides of double helix run in opp directions, count from carbon bound to base clockwise
5 things all cells share
cell membrane, genetic material, ribosomes, cytoskeleton, cytosol
support and mobility, microtubules (thick) microfilaments (thin), cilia and flagella, motor protein highway
golgi apparatus
enter the cis face, out the trans face, transport vesicles and motor proteins carry, golgi gives chemical tags
free ribosome
makes proteins that stay in the cytosol
bound ribosomes
make proteins that go to plasma membrane and outside of cell
lysosomes break down invasive particles, food vacuoles with hydrolytic enzymes
lysosomes break down old parts from the cell itself
have both hydrophobic and hydrophilic regions
functions of membrane proteins
transport, enzymatic activity, signal transduction, cell-cell recognition, intercellular joining, attachment to extracellular matrix
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passive transport
transport across the cell membrane with the concentration gradient, no energy required (diffusion, osmosis, facilitated diffusion)
active transport
transport across the cell membrane against the concentration gradient, requires cell energy as ATP (endocytosis, exocytosis, sodium-potassium pump)
dynamic equilibrium
the state in which a substance is evenly dispersed and movement is uniform
selective permeability in the cell membrane
smaller, nonpolar molecules diffuse through faster than larger, polar molecules; certain molecules can go thru and others can't
facilitated diffusion
passive transport with transport protein channel (bind loosely to molecule, carry it thu) (aquaporins)
sodium potassium pump
inside cell, 3 sodium ions bind to pump, shape change, ATP bind a phosphate (phosphorylation), shape change, sodium out, 2 potassium bind, shape change, dephosphorylation, shape change, potassium release, start over
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membrane potential
difference in electric charge across a membrane (inside usually more negative)
electrochemical gradient
chemical gradient - concentration of molecules, and voltage gradient - pos charged ions outside cells attracted to neg charge inside cell, when cell pos repel
invagination caused by membrane budding off to the inside of cell containing smth (usually large molecules or large numbers of molecules) as a vesicle (ex: phagocytosis, phagosome) - lots of atp (motor proteins)
vesicles from cell merge with membrane and push contents to outside of cell (ex: neurotransmitters into synapse) - lots of atp
technically active transport, 2 molecules have to be present at a transport protein to diffuse thru the protein - active bc another pump moves co-molecule against concentration gradient (usually to outside) to be present at the protein - co-molecule often allows shape change, enables transport
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2 molecules moving in opposite directions thru the same pump
moving in same direction, move together
water potential
takes pressure and solute concentration to predict where water will travel (% = %p + %s)
complete set of organic chemical reactions in the body
catabolism (catabolic reaction)
break down of large into smth smaller (ex: hydrolysis, proteases, nucleases, etc)
anabolism (anabolic reaction)
building large molecules from smaller (ex: kinases, dna polymerase, etc)
exergonic reactions
lower activation energy, high energy reactant w/ low energy products, releases energy into environment (ex: cellular respiration first steps, glucose + oxygen gas high energy -> co2 + H20 low energy, releases energy)
endergonic reactions
higher activation energy. low energy reactant w/ high energy products, need to take in energy for the bonds (ex: photosynthesis, co2 + h20 low energy, need sun to make glucose + o2)
enzymes lower...
activation energy
energy coupling
when the energy released from an exergonic reaction is used as the activation energy to fuel an endergonic reactions (es: breakdown of glucose to fuel atp production)
enzymes function by...
providing specific binding sites to line up where reaction will happen, apply stress/pressure to bonds (then rebond to others), microenvironment, maybe even directly participate
enzymatic pathway
series of multiple enzymes that trigger each other, eventually reach specific function
precursor molecule
molecule that has a similar shape and composition to another molecule, with small change will become that molecule
enzyme activity is affected by...
temperature, pH, concentration (substrate + enzyme)
saturation curve
graph that shows how at a certain substrate concentration all enzyme will constantly be working, so increasing substrate concentration does not increase activity
substance that stops enzyme from functioning properly
competitive inhibitor
molecules that mimic shape of substrate, occupy where substrate wants to go and doesn't let bind (can be outcompeted by substrate)
noncompetitive inhibitor (allosteric)
molecules that bind to a spot on the enzyme (not active site) and changes the enzyme shape, preventing substrate binding (effective even in increasing substrate concentration)
substance that promotes enzyme functioning
allosteric activator
molecules that binds to spot on enzyme (not active) and stabilizes the active enzyme to promote binding of substrates
when substrate binds to active site, stabilizes the enzyme to promote substrate binding
feedback inhibition
when a product of an enzymatic pathway then inhibits an earlier step in the pathway (to turn off), maximizes energy
nonenzyme that binds to enzyme during reaction, essential for reaction (not all reactions)
set of chemical reactions that a cell performs
chemical energy
potential energy available for release thru breaking chemical bonds
2nd law of thermodynamics
energy transfer increases disorder in the universe (higher entropy)
pathways of degradation, break down complex molecules (high potential) and release energy, often exergonic (ex: cellular respiration)
consume energy to build complex molecules from simpler molecules, often endergonic (ex: photosynthesis)
luciferase reaction is exothermic bc...
energy is released in the form of light
energy coupling
when the energy released from an exergonic reaction is used to fuel an endergonic reaction
phosphates for phosphorylation come from..
hydrolysis of ATP (performed by kinase) into ADP or cAMP
ATP structure
similar to nucleotide - ribose (pentose sugar), adenine, chain of 3 phosphate groups
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cellular respiration (basic)
C6H12O6 + 6O2 = 6 H20 + 36 ATP, high pe reactants to low pe products, energy release used to make ATP molecules (high pe)
steps of cell communication
reception, transduction, response
target cell
cell with specific receptor that will bind a signal molecule and have a specific response to it
parasympathetic nervous system
relaxed, rest and digest, less airflow, less atp production + use, peristalsis, etc
sympathetic nervous system
fight or flight, danger, take in more oxygen, release glycogen and break down into glucose, make and use more atp, adrenaline and noradrenaline, etc
scaffolding protein
protein that holds phosphorylation cascade kinases in place to increase speed of reactions
how do signaling pathways begin and terminate
binding of ligand to receptor initiates signaling, activates transduction proteins, when transduction proteins deactivated, turn off
yeast mating factor
yeast cells exchange mating factors (signaling molecules), when mating factors different, will mate - varied genetic material makes more resilient offspring
phosphorylation cascade
series of kinases activating next kinase by phosphorylation
removal of added phosphate group by phosphatase
second messenger
smaller molecule in signaling pathway that diffuses thru cell quicker, allows for quicker signaling
Calcium ion and signaling
cell uses calcium ion pumps to create concentration gradient of Ca2+, when gated ion channel is unlocked by molecule, ions flood into the cell and cause voltage change, which opens voltage-gated pump/channel
local signaling, short distance, secretory vesicle
long distance signaling, in bloodstream, hormones
when 1 molecule in pathway activates many molecules in the next step, makes faster
property of ligands only activating response in certain target cells bc only certain cells express gene to create the receptor for that ligand
neuronal communication (basic)
electric signal sent down