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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glycerol
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
monosaccharide
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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
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carbohydrate basic formula
(CH2O)n
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carbohydrate functions
energy storage, structural support
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phospholipid
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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cohesion
same types of molecules bind together (usually weaker bonds)
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adhesion
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
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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
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bc specific heat of water is ..., it is good for...
high, cooling and regulating internal temps (resists temp change)
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breaking hydrogen bonds ... energy
requires/absorbs (endo)
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making hydrogen bonds... energy
gives off/releases (exo)
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water ... when freezing bc...
expands, molecules orient themselves in matrix position that is more spread out to balance charges
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hydration shells
water molecules gathered around a charged particles after dissolving it, all molecules should be oriented specifically
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acids
increase H+ or H3O+ (hydronium) concentration
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bases
increase OH- concentration (decrease H+)
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bufferes
stabilize pH by minimizing effects of strong acids and bases
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standard deviation
how much data points differ from the mean
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x bar =
mean
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n =
number of data points
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higher standard deviation...
lower reliability
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standard error
represents uncertainty, sample size and variability (smaller standard error, more likely mean is accurate generalization)
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error bars
usually 2SEM, show the standard error, overlap = no statistical significance
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hydroxyl
OH, polar, makes hydrophilic
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amino
-NH2, often in bases, in amino acids with carboxyl
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carboxyl
-COOH, carboxylic acid group (dissociates into acid in water), in amino acids with amino
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methyl
-CH3, nonpolar, binds to cytosine to promote gene expression
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euchromatin
open, methylated DNA
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heterochromatin
closed, wrapped around histones, unmethylated
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phosphate
-PO4 2-, negative charge = hydrophilic, in phospholipids and nucleotides
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sulfhydryl
-SH, crosslinked molecules, when bound S-S
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carbohydrate bond
glycosidic bond
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disaccharides
2 bonded monosaccs, maltose, sucrose, lactose
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polysaccharides
staches, glycogen, cellulose - long term energy storage and structure
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cellulose
plant cell walls
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peptidoglycan
bacterial cell walls
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chitin
fungal cell walls, arthropod exoskeletons
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lipid bond
ester bond
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hydrogenation
artificially adding hydrogen to carbon chains in fats to saturate them
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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
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cholesterol
animal sterol, produced in liver, stabilizes membrane
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testosterone and estradiol
hormones (steroids), 4 ring structure
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protein based hormones
bind to receptors on cell membrane, don't acc enter, trigger internal signalling
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lipid based hormones
because membrane also lipid, can enter the cell itself, trigger signaling once inside of the cell
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waxes
lipids, alcohol chain and fatty acid chain, insulate from water loss
ribosomes, proteins the will be in the cytosol synthesized in free ribosomes, proteins secreted or in plasma membrane synthesized in bound ribosomes (er)
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protein function determined by...
sequence of amino acids and R group interactions (20 diff R groups)
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protein bond
peptide bonds
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genetic code
triplet code of codons and which amino acids they relate to
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primary protein structure
linear, chain of amino acids
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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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denaturation
protein unraveling (degrading) due to change of environment (temp, pH, etc)
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2 types of nucleic acids
DNA (deoxy), RNA (ribo)
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pyrimidines
cytosine, thymine, uracil (t in rna), single rings
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purines
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)
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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
support and mobility, microtubules (thick) microfilaments (thin), cilia and flagella, motor protein highway
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golgi apparatus
enter the cis face, out the trans face, transport vesicles and motor proteins carry, golgi gives chemical tags
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free ribosome
makes proteins that stay in the cytosol
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bound ribosomes
make proteins that go to plasma membrane and outside of cell
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phagocytosis
lysosomes break down invasive particles, food vacuoles with hydrolytic enzymes
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autophagy
lysosomes break down old parts from the cell itself
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amphipathic
have both hydrophobic and hydrophilic regions
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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)
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active transport
transport across the cell membrane against the concentration gradient, requires cell energy as ATP (endocytosis, exocytosis, sodium-potassium pump)
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dynamic equilibrium
the state in which a substance is evenly dispersed and movement is uniform
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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
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facilitated diffusion
passive transport with transport protein channel (bind loosely to molecule, carry it thu) (aquaporins)
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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)
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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
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endocytosis
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)
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exocytosis
vesicles from cell merge with membrane and push contents to outside of cell (ex: neurotransmitters into synapse) - lots of atp
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cotransport
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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antiport
2 molecules moving in opposite directions thru the same pump
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symport
moving in same direction, move together
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water potential
takes pressure and solute concentration to predict where water will travel (% = %p + %s)
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metabolism
complete set of organic chemical reactions in the body
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catabolism (catabolic reaction)
break down of large into smth smaller (ex: hydrolysis, proteases, nucleases, etc)
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anabolism (anabolic reaction)
building large molecules from smaller (ex: kinases, dna polymerase, etc)
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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)
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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)
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enzymes lower...
activation energy
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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)