Structure and Function -- Macrmolecules (more) Flashcards
What are the macromolecules
carbs lipids nucleic acids proteinP
Macromolecules
super large molecules
Polymers
long molecule that consists of many smaller building blocks linked covalently
Monomers
the things that make up polymers
they can also have their own individual function
Enzyme
macromolecules that speed up chemical reactions
What are the names for the process of how macromolecules are formed/broken respectively
dehydration synthesis and hydrolysis
Hydro
water
Lyse
break apart or split
Hydrolysis aka
digestion
Sugars are made of what macromolecule
carbs
Monosaccharides are made of how many carbons
3-7
What is the shape of glucose when it is in water
ring
What is the shape of 5-6 carbon carbs when they are put in water
ring
Most sugars end in
ose
All carbs have what fxnal groups
carbonyl group and hydroxyl group
Sugars are classified by what
size
3 carbon sugar name
triose
5 carbon sugar name
pentose
6 carbon sugar name
hexose
example of hexoses
fructose and glucose
assymetric carbon
carbon that is attached to 4 different atoms or atom groups
Cellular respiration
cells extract energy from glucose molecules by breaking them down
The carbon skeletons of sugars can be used ot synthesize what other things
other organic molecules or poly or di sacchs
Disaccharide
2 monosaccharides joined by a glycosidic linkage
Glycosidic linkage
covalent bond formed between 2 monosacchardides by dehydration synthesis
Starch
polymer of glucose molecules that is stored in plastids which allows plants to stock a shit ton of glucose which can be hydrolyzed for energy
Plastid
organelles in cells used for storage
What is the shape of starch
helix – branch or unbranched
example of plastid
chloroplast
Glycogen
polysachharide or polymer of glucose where animals store energy and glucose
are carbs long or short term energy
short (usually depleted in 24 hours)
What is the shape of glycogen
helix branched
Where do vertebrates store glycogen
liver and muscle cellsC
Cellulose
structural polysaccharide; polymer of glucose
Shape of cellulose
long structural hydrocarbons that are straight and unbranched
What differentiates cellulose from other common polysaccharides
it has different glycosidic linkages bc the glucoses are upside down alternating unlike how theyre all the same for starch, glycogen, etc.
What is the reason that some organisms can digest glycogen but not cellulose
bc the glycosidic linkages are different so that the hydroxyl group is aternatively on the top or the bottom –> so most organisms dont have the correct enzymes so it js slides into the rest of their shit
Chitin
structural polysaccharide of arthropods that they use ot make exoskeletons –> its soft then its hard ;P so its strong structurally
Why are chitin and cellulose similar
they have the wonky glycosidic linkage different hing
example of an organism that uses chitin and how
fungi in its cell walls
Does fat have monomers
no
What is fat made of
glycerol and fatty acid
Glycerol is what type of molecule
alcohol
Fatty acid
a long carbon chain that is nonpolar and it makes the whole fat molecule hydrophobic
how long is a fatty acid chain
16 - 18 carbons
what fxnal group does fatty acid have
carboxyl acid
Fat aka
triacylglycerol or triglyceride
What bonds the fatty acid to the glycerol in a fat molecule
ester linkage
ester linkage
a bond formed by dehydration synthesis between they oxygen of the hydroxyl group of the glycerol and the carbon of the carboxyl group of the fatty acid
the double bonds in unsaturated fat are cis or trans
cis
Lipids
long term energy storage (better than carbs)
Do lipids have monomers
no
Are lipids molecules
yes they even sometimes form macromolecules
Structure of lipids
hydrocarbon
Lipids polar or nonpolar
nonpolar
Lipids hydrophobic or philic
phobic
How many carbons is usually in lipids
usually 16-18
Hydrogenated
bad, unsaturated fats that have been synthetically converted to saturated fats by adding hydrogen and trans fats
Saturated Fat is bad why
bc it can cause atherosclerosis
Atherosclerosis
clogged arteries
Trans Fat
unsaturated bonds with trans double bonds ( H on opposite sides of the double bond)
What do trans fats do to cholesterol
increase LDL and reduce HDL
HDL
good cholesterol high density lipoprotein
LDL
low density lipoprotein bad cholesterol
Do trans fat occur in nature
yes
Adipose Cells
cells where mammals store long term energy and does the organ cushioning
What organisms have cholesterol in their cell membranes
animal cell membranes
Main purposes of fat
energy
insulation
organ cushioning
Phospholipid
like a fat molecule with only 2 fatty acid groups instead of 3 and the 3rd hydroxyl group is bonded to the phosphate group which is negatively charged
also usually there’s another polar or charged molecule that is linked to the phosphate group
Phospholipid is important for what
cell membrane (phospholipid bilayer and in micelles)
Are the heads of phospholipids hydrophilic or hydrophobic
hydrophilic
Are the tails of phospholipids hydrophilic or hydrophobic
hydrophobic
Why and how is the tail of a phospholipid bent
because there is a double bond so its unsaturated and the tails don’t freeze together
Steroids
lipids that have a carbon skeleton of 4 fused rungs
Examples of steroids
cholesterol and sex hormones
Catalyst
chemical agents that speed up chemical reactions
Amino Acid
organic molecule with amino group, carboxyl group, R group and H that has an assymetric carbon
What makes amino acids different from each other
the r Group
what is the R group aka
side chain
Nonpolar amino acids are
hydrophobic
Polar amino acids are
hydrophilic
Basic amino acids have what
a positive R group
Acidic amino acids have
negative side chain because of carboxyl group in ionized form
Are acidic and basic amino acids hydrophobic or hydrophilic
hydrophylic because they are charged
Peptide bond
covalent bond between the nitrogen of the amino group of one and the carbon of the carboxyl group of another
What are the ends of 2 amino acids bonded together
amino group and a carboxyl group on the other end
Polypeptide backbone
The non-R group of amino acid polymers, consisting literally of -N-C-C-N-C-C-N-
Shape determines
function
Do polypeptides = proteins
no because polypeptides can be proteins (single) but they have to be twisted and folded so polypeptides are just long primary structure
Globular Proteins
proteins that are roughly spherical theyre rough and wide and theyre soluble in water
Fibrous proteins
proteins shaped like long fibers; insoluble in water
All proteins have what levels of structure
1-3
Why do only some proteins have quartenary structure
because not all proteins consist of more than one polypeptide chain
What are the protein structure levels
primary
secondary
tertiary
quaternary
Primary protein structure level
sequence of amino acids which is determine by DNA
If there were 127 amino acids in a chain how many different ways can you make the protein chain and why
20^127 because 20 amino acids exist in nature
Secondary protein structure level
coil/fold due to hydrogen bonds between the H+ of amino group and O- of catboxyl group
What is the coil called in secondary structure in protein structure levels
alpha helix
What is the fold called in secondary structure in protein structure levels
beta pleated sheet
Tertiary protein structure level
overall shape of a polypeptide which results from the interactions between the R-groups
What are some examples of the tertiary bonds wjocj caise overall shapes of polypeptides
hydrophobic interaction
disulfide bridge
Hydrophobic interaction
amino acids (nonpolar) end up in the middle and are held together by Van der Waals forces
also H bonds hold together
also bonds bwteen positive and negative
Disulfide bridge
covalent bond between sulfurs of the sulfhydryl groups of 2 cysteines; super strong
Quaternary
association of 2+ polypeptides
Denaturation
proteins change shape because of wrong conditions because can disrupt bonds that hold it together
What are some of the wrong conditions that can cause denaturation
wrong pH, temp, salt concentration, etc.
Can denaturation be fixed?
yes if you put them back in the right conditions
Chaperonins
proteins that encase other proteins-to-be so they are in the right conditions to fold
Why are chaperonins important
because if proteins fold in the wrong conditions it could lead to fatal diseases such as CF, sickle cell disease, etc.
When proteins-to-be go into chaperoning proteins what level of structure are they in
primary and they leave as secondary
X-Ray Crystallography
shoot X-rays a crystallized and hardened protein and look at defraction patter ti assess design of protein
Gene
a discrete unit of hereditary information consisiting of specific nucleotide sequences in DNA
Gene expression
DNA directs RNA –> protein synthesis (in ribosomes)
Polynucleotides
polymers of nucleic acids
Nucleoside
nucleotide without phosphate
Nucleoside aka
nucleoside monophosphate
Pyrimidine
six carbon ring ( C, U, T)
Purine
six carbon ring fused to a five carbon ring (G,A)
Phosphodiester linkage
the covalent bond between nucleotides between the phosphate group of one and the sugar of another
Where do the phosphodiester linkages appear
on the outside (ribbon part) of the double helix
Where are the hydrogen bonds in DNA
between the bases (in the middle)
Antiparallel
the 2 sugar-phosphate backbones are on the outside of the helix and they run in oppposite directions; one is 5’ -> 3’ and the other one is the other way
RNA has how many strands
one
DNA has how many strands
2 –> double helix
If organisms have similar molecular geanologies…
they are more related
What causes the polar head of a phospholipid
the top is negatively charged because of phosphate and the bottom is positevely charged because instead of a third fatty acid chain (like in a fat molecule) there is a choline which is positively charged
Steriod purpose
chemical messengers/hormones
What is in the backbone that is coiled/foiled in secondary protein structure
everything but the R-group
What are the helix and the beta pleated sheet held together by
hydrogen bonds
