Lecture 3: Biomolecules Flashcards
Organic molecules
molecules containing carbon
Carbon
can form 4 covalent bonds
allows creation of large complex molecules
can also form ultra-stable double covalent bonds (CO2)
Hydrocarbons
store a great amount of energy
molecules that consist of only carbon and hydrogen
functional groups
groups of atoms that give molecules their different properties
ex: estrogen and testosterone
Endergonic
reaction that builds bonds and require energy
exergonic
reaction that breaks bonds and releases energy
ATP
energy molecule used to build bonds
temporarily store energy by building new bonds
large molecules
made up of smaller molecules
monomer
single unit
polymer
a bunch of monomers put together
how do you build a polymer from monomers
use a dehydration reaction aka take the water out and build a new bond
aka an ENDERGONIC REACTION
how do you break down a polymer
hydrolysis reaction in which water is added to split the molecule in two
aka EXERGONIC
biomolecules
organic molecules associated with organisms
carbohydrates
most abundant
polar
monomer of carbohydrate
monosaccharide
2 monosaccharides joined by a glycosidic bond
disaccharides aka sucrose
polymer of carbohydrate
polysaccharide
what do carbohydrates end in?
-ose ie sucrose lactose glucose
carbohydrate polymers
sucrose (glucose and fructose) lactose (glucose and galactose) cellulose (fiber) glycogen starch
Glucose
easiest energy source for bodies
starts cellular respiration
easiest energy source for bodies
brain cannot use anything but glucose to survive
if you don’t eat enough of it, body can convert other biomolecules into glucose
2 forms of glycosidic bonds
alpha and beta
how do you breakdown a glycosidic bond
enzymes are needed
specific enzymes are for each bond
humans make mostly enzymes for alpha glycosidic bonds
beta bonds
not many enzymes for beta bonds and if you eat something with beta bonds, you can’t digest it
cellulose
found on outer part of plant cells
give plants rigidity and structure in because they have no backbone
starches
large carbohydrate molecules where lots of organisms store excess energy
in humans, what is the form that excess glucose is stored in?
glycogen, a type of starch
monomers of carbohydrates
glucose and fructose
glycogen
stored in the liver and muscles and used when we need energy but aren’t eating
what happens when you reach your glycogen set point
the rest is stored as fat
lipids
nonpolar fatty acid
source of energy storage
most common form of lipids
triglycerides which are 3 fatty acids bound to a glycerol
saturated fats
every carbon is bound to as many hydrogens as possible “saturated with hydrogens”
can be packed together tightly –>can create a solid structure at room temp
straight
unsaturated fats
carbon molecules are not bound to as many hydrogens as possible
kinks in the chain can form double bonds
cannot be packed together tightly
cannot create a solid structure at room temp; liquid at room temp
fats
type of lipid
long term energy storage and insulation
sterols
cholesterol
can do many things in the body
form the basis for hormones
regulate growth and development
form the basis of a bunch of different molecules
phospholipids
similar to triglycerides
two tails
phosphate group
form the basis for all biological membranes
polar heads
nonpolar fatty acid tails
proteins
most versatile of biomolecules
ALL CONTAIN NITROGEN
polar
monomer of protein
amino acid
amino acid
20 types
all have a carboxyl group and an amine group
different R or functional group; determines amino acid
tells us a lot on how our protein is shaped
polymer of protein
polypeptides
amino acids are classified as
polar (charged
polar(uncharged)
nonpolar
determine protein shape
what bonds are formed in amino acids when they are added to polypeptide
peptide bonds through dehydration reactions
primary structure
linear string of amino acids
where do building polypeptides take place?
in an aqueous environment
what happens when a primary structure grows longer
it may begin to fold
properties of amino acids dictate
the bonds among them
factors that influence proteins
hydrogen bonds btw polar amino acids
ionic bonds between charged amino acids
hydrophobic effect
van der waal forces (weak attractions)
disulfide bridges
secondary structure
sequences of amino acids form hydrogen bonds, causing protein to fold into a spiral (a helix or b pleated sheet)
tertiary structure
secondary structure folds into a 3D shape
quaternary structure
two or more polypeptides may bind to each other to form a functional protein
antibodies
help fight against cerain bacteria
denaturation
protein returns to its primary structure
temp and ph affect this
some proteins can renature
every protein is specific for its
ligand
enzymes usually end in
-ase
many proteins bind other ligands in order to
transport or store them within cells or the blood
ie hemoglobin and oxygen
one type of protein (enzymes) will always change its ligand (substrate)
enzyme lactase breaks down its substrate lactose
most of the protein we eat is
used to make new proteins for our bodies
to use protein for energy we need to
remove the nitrogen found in the amine group
nitrogen then becomes urea, the main component of urine
monomer of nucleic acids
nucleotides
polymers of nucleic acids
nucleic acids DNA and RNA
a single nucleotide is made up of
phosphate group
5 carbon sugar
3 carbon-nitrogen ring structure called a nitrogenous base
difference btw DNA and RNA
ribose (w an oxygen) or deoxyribose (w/out an oxygen)
5 nitrogenous bases
adenine guanine cytosine thymine uracil
what bonds are btw the bases
hydrogen bonds
DNA
double helix consisting of two lines of phosphate and sugar groups
genetic material of the cell
can produce every protein of our bodies based on the DNA that codes for that protein
located in the nucleus
can DNA leave the nucleus
no,
will make a single stranded copy of our gene into RNA so it can leave the nucleus and make the protein
every 3 bases on the RNA copy will code for a single amino acid
RNA structure
single stranded molecule
steps to code RNA for a single amino acid
1) synthesis of mRNA
2) movement of mRNA into cytoplasm
3) synthesis of protein
