Biomolecules Flashcards
Adhesion
“sticks” to other substances
Cohesion
“sticks” to itself
Surface tension is due to
cohesion of H2O cules to one another and adhesion of H2O to the surface
hydrophobic
repels water
hydrophilic
attracts water
condensation reaction
reaction in which H2O is produced
hydrolysis reaction
reaction in which H2O is consumed (reverse of condensation); this is how we digest food, and also why we need to consume a lot of water.
transpiration
how H2O moves through plants using adhesion to bring the water up the stem and to the top of the plant
Some important properties of H2O
- Less dense as a solid
- Temperature buffer (changes temp slowly and absorbs a lot of nrg)
- can undergo H2O dissociation
H2O dissociation
H2O is pulled apart in the reaction 2H20 -> H3O + OH
This occurs once in every 10^7 cules
functional groups
groups added to carbon-based molecules that give it its special properties
polymer
chain of biomolecules
monomers
one subunit of a polymer
carbohydrate
has the formula (CH2O)n, ends in -ose, found in ring structures in liquids and chains in solids
lipids
mostly C & H, nonpolar
protein
chains of amino acids, has the amine group and is polar (positive at nitrogen end, negative at the opposite end where O is)
peptide
short protein
polypeptide
long protein
nucleic acid
nitrogenous base + carbohydrate + phosphate group
nitrogenous base
monomer of nucleic acid, Adenine, Thymene, Cytosine, and Guanine
polymer of nucleotides
long chain of nucleotides
monosaccharide
one carbohydrate molecule
alpha- monosaccharide
OH group below the plane of the carbons
beta- monosaccharide
OH group above the plane of the carbons
starch
disaccharide formed by two or more alpha-saccharide cules
cellulose
disaccharide formed by two or more beta-saccharide cules
alpha- disaccharide
two monosaccharides joined together by a bond with oxygen below the plane of the carbons
beta- disaccharide
two monosaccharides joined together by a bond with oxygen above the plane of the carbons.
4 types of biomolecules
carbs, lipids, amino acids, nucleic acids
Triglycerides
three fatty acids and a glycerol
These are slower to build up and break down than carbs, they’re useful for long term energy storage, and they’re typically found in fats and oils.
Saturated fatty acid
single bonds between carbons, solid at room temperature, found in animal sources, mostly linear
Unsaturated fatty acid
one or more double bonds, liquid at room temperature, found in plant sources
CIS unsaturated fatty acid
hydrogens are on the same side (looks like a C), appears bent
TRANS unsaturated fatty acid
hydrogens on opposite sides (looks like an S), mostly linear, not naturally occurring, bad for you
Steroids
backbone of four carbon rings, properties are given by attached functional groups (which can be large)
Phospholipids
two fatty acids and a phosphate group attached to glycerol, hydrophobic side, and a hydrophilic side, can assemble into a bubble or a bilayer, has a saturated leg and an unsaturated leg
appearance of a phospholipid
phosphate attached to the top carbon of the glycerol on one side through an oxygen, then two fatty acids connected to the bottom two carbons of the glycerol on the opposite side
protein
covalently bonded amino acids that form a peptide, which bonds and fold to make a polypeptide. carboxyl group on the C connects to the amine group by losing a water molecule.
R groups (proteins)
reactive groups connected to the middle C in the NCC chain, made up of functional groups.
4 levels of structure in proteins
primary, secondary, tertiary, and quaternary
primary protein structure
first level of organization in proteins. occurs when the DNA is synthesized to form amino acids, which connect to one another covalently.
secondary protein structure
the protein begins to have interactions within itself. the carboxyl, hydroxyl, and ketone groups within the amino acids start to interact with one another via H-bonding, causing the structure to curl up in places.
tertiary protein structure
R groups of the protein interact further developing the protein’s folded structure.
quaternary protein structure
R groups of the folded protein interact with the R groups of other folded proteins, creating a ball of proteins.
native (normal) proteins
proteins that folded correctly with little to no abnormalities
nonnative (toxic) proteins
proteins that folded incorrectly, resulting in the wrong shape and function. these proteins can “infect” normal proteins and cause them to become toxic, leading to the buildup of these proteins and therefore disorders and diseases.
diseases caused by toxic proteins
Alzheimer’s (caused by amyloids), Parkinson’s, Huntington’s, diabetes, high cholesterol
amyloids (proteins)
toxic protein with an abnormally large amount of beta-pleated sheets.
beta-pleated sheets (proteins)
places in the proteins where the chain folds/turns rather than curls
functional properties of proteins
storage, transport, enzymes, structure, immune system, motor function, etc
which part of the protein is integral for the protein’s shape?
R-groups, as they determine how the protein folds up
how many common amino acids are used by living things?
20
BMI
weight (kg)/height (m^2)
hydrogenation
artificial addition of double bonds to oils through a process involving pressure, hydrogen gas, and a nickel catalyst
dietary guidelines
avoid trans fats & switch to other fats
strengths of using BMI
simple and inexpensive, non-invasive, gives the doctor an idea of what to check for
limitations of using BMI
measure of excess weight, not fat; doesn’t account for factors like age, sex, ethnicity, height, sexual maturation, and muscle mass; who is BMI based on?
