Bio: Macromolecules

Carbohydrate

contains carbon, hydrogen, and oxygen; oxygen and carbon number are close

proteins

contains carbon, hydrogen, oxygen, sulfur, and nitrogen

lipids

contains carbon, hydrogen, oxygen, and sometimes a phosphate group; oxygen and carbon number are not close at all

nucleic acids

contain carbon, hudrogen, oxygen, phosphate, and nitrogen

monomer

small, single unit, basic building block

dimer

2 monomers bonded

polymer

many monomers joined together with a covalent bond

different polymers

different sequences of monomers →

anabolic, endergonic reactions

reactions that build up macromolecules

catabolic, exergonic reactions

reactions that break down macromolecules

dehydration synthesis (condensation reaction)

builds molecules up, requires energy. results in the formation of a large molecule out of smaller molecules forming covalent bonds.

water is formed and released each time a covalent bond is formed

hydrolysis reaction

breaks molecules down, releases energy. results in formation of smaller molecules out of a large molecules breaking covalent bonds

water is broken doen and its parts are added to form the products

monosaccharide

monomer of a carbohydrate

1C: 2H: 1O ratio

glucose, fructose, and galactose

6- carbon sugars

C6: H12: O6

ribose and deoxyribose

5- carbon sugars

disaccaharide

dimer of carbohydrates- double sugar

sucrose, maltose, lactose

disaccharides

alpha glucose

1-hydroxyl and 4- hydroxyl on the same side

hydroxyl group below

beta glucose

1 hydroxyl and 4 hydroxyl, on opposite sides

hydroxyl group above

linear

polymers made out of beta glucose

linear polysacchrides

allows for hydrogen bonds creating a strong building material such as cellulose

helical

polymers made out of alpha glucose

alpha glucose (starch and glycogen)

energy storage polysaccharides

beta glucose( cellulose and chitin)

structural polysaccharides

starch

energy storage polysaccharide found in plants (plastids)

glycogen

energy storage polysaccharide found in animals

short term energy storage in liver + muscle

extensively branched

cellulose

structural polysaccharide found in plants, in the cell wall

most abundant on earth

insoluble fiber

chitin

structural polysaccharide found in animals and fungus, makes up exoskeleton in animals

makes up cell wall in fungus and found in exoskeletons

amylose

simple starch, unbranched

amylopectin

complex starch, branched

glycosidic bond

covalent bond; holds monomers together to make polymers in sugars C-O-C

polysaccharide

polymer of carbohydrates

C:H bond

non-polar covalent bond; insoluble in water

hydrocarbon tails

causes lipids to repel water

adipose

long term energy storage, insulation, cushion/ protects organs

2x more than carbs

how much energy does a lipid store

fatty acid and glycerol

what are the two “monomers” of a lipid

fatty acid

carboxyl group bonded to long hydrocarbon chain

glycerol

3-C backbone, sugar alcohol

ester linkage

covalent bond between glycerol and fatty acid; O-C-O

triglyceride (fat molecule)

glycerol + 3 fatty acids

saturated and unsaturated

what are the two types of fatty acids

saturated fatty acid

all single C-C bonds, linear, and maxium hydrogen

packed together tightly and solidify at room temperature

unsaturated fatty acid

contain at least one C-C double bond in the fatty acid; double bong creates a kink in the chain, not max hydrogen

kinks make the fats unable to pack together closely, thus remaining a liquid at room temperature

phospholipid

1 glycerol, 2 fatty acids, and a phosphate group (PO4) that can have other molecules attached to it

head of phospholipid

phosphate group (negative charge) that is hydrophilic (interacts with polar molecules aka water= H-bond with water)

tail of phospholipid

2 fatty acid (hydrocarbon) tails are hydrophobic

protected by the heads in a phospholipid bilayer

steroid

4 fused carbon rings with different functional groups attached giving different properties

cholesterol

the basis for forming all other steroids

found in cell memebranes - fluidity

synthesized by the liver, also obtained in diet

high levels lead to cardiovascular disease

differences in fuction and structure

differences in saturation determine what in a lipid

amino acid

monomer of proteins

20 total, that differ at the R group

carboxyl (COOH) and amino acid (-NH2)

what 2 functional groups are present in an amino acid

dipeptide

dimer of proteins

polypeptide

polymer of proteins

glycoprotein

protein + carbohydrate: found in cell membrane, helps cells with recognition

peptide bond

covalent bond that holds proteins together, C-N

enzymatic, defensive, hormones, transport, receptors, structure, contractile, and storage

what are the 8 functions of proteins

by making sure the amino acid is in the right direction

how do enzymes speed up the reaction in the protein

hydrophobic

carbon + hydrogen

electornegative/ hydrophilic

oxygen + nitrogen

primary structure of proteins

linear chain (a change here will cause a change in all other levels)

secondary structure

polypeptide backbone is folded and stabilized by hydrogen bonds

hydrogen bond formed between oxygen of carboxyl group and hydrogen of amino group

alpha helix

colied regions of a secondary structure amino acid

beta pleated sheet

flat/ folded regions of a secondary structure amino acid

tertiary structure

3d protein shape is stabilized by side chain interactions (R groups)

hydrogen bonds from between polar side chains

disulfide bridges

covalent bonds between sulfhydryl (-SH) groups

quaternary structure

multiple polypeptide chains combine to form one protein

denature

change in protein shape due to breakdown of interactions/ bonding causing it to unravel/ unfold and no longer function

chaperonin

proteins that assit in the process of folding other proteins

large interior spaces that provide the polypeptide chain a “safe place” to fold away from outsid/ environmental influence of the cell

diseases such as alzheimer’s, parkinson’s, and mad cow can be caused

what can happen in a protein misfolds

the specific order of amino acids in a polypeptide

what determines the overall shape and function of the protein

the carboxyl (C) terminus of the growing peptide chain

where do the covalent bonds form in a linear chain of amino acids

nucleotide

the monomer of a nucleic acid

pentose (5C) sugar, Phosphate group (PO4), and a nitogen

what are the 3 parts of a nucleotide

ribose (RNA) or deoxyribose (DNA)

what are the pentose sugars in a nucleotide

gives the backbone a negative charge

what does the phosphate group do in a nucleotide

adenine, guanine, thymine, cytosine, and uracil

what are the 5 nitrogen bases

thymine

what does adenine bond to in DNA

guanine

what does cytosine bond to

uracil

what does adenine bond to in RNA

thymine, uracil, and cytosine

what are the pyrimidines (base with one 6-carbon ring)

adenine and guanine

what are the purines (base with one 6-carbon ring and one 5-carbon ring)

polynucleotide

polymer of nucleic acid

phosphodiester C-O-P

covalent bond holding nucleic acids together

5-C ribose

Adenine nitrogen base

3 phosphate groups

what does ATP contain

5-C ribose

Adenine nitrogen base

2 phosphate groups

what does ADP contain

5-C sugar (ribose or deoxyribose)

Nitrogen base

what does a nucleoside contain

the 3’ end

where are nucleotides added to a growing DNA/RNA strand

5’

phosphate group in DNA/RNA is where

3’

hydroxyl group in DNA/RNA is where

antiparrel 3’-5’ 5-3’

what is the directionality of DNA strands

close evolutionary relationship

similar DNA/proteins→

adenine

what is this nitrogen base

guanine

what is this nitrogen base

cytosine

what is this nitrogen base

thymine

what is this nitrogen base

uracil

what is this nitrogen base

hydrogen bonds

what type of bonds allow for base pairing

3 hydrogen bonds

how many hydrogen bonds do guanine and cytosine have

2 hydrogen bonds

how many hydrogen bonds do adenine and thymine have