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Polymer
long chain of similar repeating sub units joined together by similar bond types
carbs
hexagon structure, cellulose (wood)
protein
polymers of amino acids
amino acid structure: carbon bonded to nitrogen, phosphate group, R group
peptide bond
join amino acids together
primary structure
from first amino acid to the last
proteins have only one
linear chain
secondary structure
proteins have many
3D helix of stable parts of the protein
stabilized by polar interactions b/n protein backbone
tertiary structure
overall 3D shape of protein
stabilized by interaction of -R group
easily influenced by external environment
Quaternary structure
functional protein: groups separate subunit protein structures
nucleic acids
polymers made of nucleotides
info and data storage transmission
DNA and RNA
RNA has OH
purines A, G; pyrimidines C, T (or U in RNA)
base pairing
A = T/U
G = C
Phosphodiester bond
lipids
not polymers; fats, oils (nonpolar)
glycerides: made of a glycerol backbone bonded to fatty acid(s)
phospholipids
amphipathic
P head, NP tail
shunned by water → minimize interactions with NP, maximize with P (surrounds)
micelles
spherical clusters of amphipathic molecules
dissolve in water, spontaneously forms
steroids
found in our body
are many hormones
3 hexagons, 1 pentagon
plants
sugar / starch / carb
less energy per gram
easier to make and access
animals
lipids / fats
more energy per gram
lighter, takes less energy to move around
harder to access
cell theory
all living organisms made of cells
cells divide from preexisting cells
cells can be cultures to produce more cells
plasma membrane
regulates what enters and leaves the cell
cytoplasm
gelatinous liquid that fills the inside of a cell
DNA
molecule that contains genetic instructions
blueprint for proteins
naked DNA: not enclosed in nucleus, easily accessible
Ribosomes
organelle that makes proteins
free ribosomes are in cytoplasm
bound ribosomes are attached to rough ER, temporarily
cytoskeleton
found in eukaryotic cells
tubes composed of proteins
provide structural support for compression and expansion
protein filaments
microfilaments
frequently interacts with myosin to do movement
protects cell from being stretched/tensed
microtubules
tracks for kinesin to transport proteins and vesicles
uses energy (ATP)
3 types of cells
bacteria and archaean’s : prokaryotes
eukaryotes
prokaryotic cells
naked DNA
no organelles
smaller size
bacteria, archaean’s
produce through binary fission
smaller ribosomes
simpler organization
parts
cell wall
capsule
pill
flagella
nucleoid
plasmids
eukaryotic cells
DNA arranged as chromosomes and stores in nucleus
many organelles
larger size
plants, animals, fungi, protists
produce through mitosis
larger ribosomes
more complex and organized
parts
nucleus
mitochondria
Endopasmic reticulum
golgi apparatus
lysosomes
chloroplasts
vacuoles
cytoskeleton
nucleus
DNA (how to make proteins) is protected but less accessible
only in eukaryotic cells
nuclear localization signal (NLS)
molecular tag on proteins so they can get in and out of the nucleus
process
protein with NLS in cytoplasm
binds to importin
goes to nucleus
pulse-chase experiment
use labeled compounds (dyed proteins) to follow dynamics of cellular processes and pathways
endomembrane system
make and distribute proteins, secretion
parts
Endoplasmic reticulum: surrounds nucleus, network folds of membranes
rough ER
protein synthesis
mRNA copies info from DNA → cytoplasm → binds to free ribosomes and gives info to make protein
if protein needs to go to other parts of endomembrane system or secreted → binds to ribosome → signal sequence → binds SRP → binds receptor → protein made (“pooped”) into ER
bind to vesicle → transported
if protein needed in cytoplasm or nucleus → don’t have signal sequence → remains free ribosome
smooth ER
lipid synthesis
similar parts in eukaryotic and prokaryotic cells
ribosomes
DNA
cytoplasm
plasma membrane
golgi apparatus
part of endomembrane system in eukaryotic cells
distribution center of proteins from endoplasmic reticulum
transports to other parts of endomembrane system
secretion out of cell
lysosomes
recycling center
breaks down molecules
endosymbiotic theory of origin of mitochondria and chloroplast
similar in size to prokaryotes
photosynthetic bacteria and oxygen breathing bacteria eaten
symbiotic relationship
larger bacteria → more glucose and energy
smaller bacteria → protected
oxygen breathing → mitochondria
oxygen breathing AND photosynthetic → mitochondria AND chloroplast
cell wall
structural support
in plant cells, highly porous → doesn’t regulate
energy and enzymes
energy of reaction doesn’t change because of enzyme
enzyme speeds up reaction
ATP
found in DNA and RNA
3 phosphate groups connected in a sequence
RNA has OH
energy coupling
use of exergonic progress to drive endergonic process
enzyme regulation
enzymes can be turned off and on
prevent unnecessary reactions
competitive inhibition
competition for binding space on active site
prevents regulatory molecule from binding to enzyme active site
lowers enzyme activity
allosteric regulation
2nd binding site: allosteric site
molecules binding to allosteric site change shape of enzyme
allosteric activation; on
allosteric inhibition; off
feedback inhibition
product of pathway acts as inhibit of pathway
prevents too much buildup of a product
self-regulating system
if product level gets too low in concentration, there isn’t enough product to bind to enzymes, thus the enzymes will start producing more product
enzyme and environment
proteins, especially enzymes, easily affected by environment
temperature
temperature optimum
when above, enzyme activity crashes
when below, enzyme activity unaffected
pH
pH optimum
too high/low will denature enzyme
temperature optimum
temperature where enzyme operates at peak efficiency
pH optimum
usually around the pH of the environment found, the pH where the enzyme operates at peak efficiency