bio unit 1 12U

how many bonds can carbon form

4

what atoms make up the base of every organic molecule

carbon atoms

hydrocarbon consist of

carbon atoms bonded to hydrogen atoms

shapes of carbon skeleton

linear, branched, or closed ring shape

Carbon Structure: linear

fats

Carbon Structure: ring

carbohydrate

organic

found in living things

Macro

Large/big

organic molecules

large molecules that are found mainly in living things

all organic molecules are composed of mainly

carbon, hydrogen and oxygen

monomer

(simplest unit) a molecule that may react chemically to another molecule of the same type to form a larger molecule

polymers

large molecules that are formed when monomers link together chemically in a chain

monosaccharide → polymer name

polysaccharides (carbohydrate)

fatty acids → polymer name

lipids

amino acids → polymer name

protein

nucleotide → polymer name

nucleic acid

amount of bonds that carbon can do

3 different ways producing 3 different shaped bond

functional groups

“additives” that

hydroxyl group increases

polarity

carboxyl groups increase

acidity and polarity of a molecule

amino and sulfhydryl groups are found

primarily in proteins and DNA/RNA

anything that is polar

can dissolve in water

carbohydrates classifications

monosaccharides, disaccharides and polysaccharides

carbohydrates purposes

source of energy, “identification flags” on cells and molecules, structural building blocks (ie. cellulose in cell walls of plants)

monosaccharide

simple sugar

composed of C - H - O

a 1:2:1 ratio

anything that ends in “ose”

a sugar

dehydration

anabolic reactions: take water to build bonds

hydrolysis

catabolic reactions: adding water to break bonds

glycosidic bond

only carbohydrates have this bond (creating a disaccharide)

carbohydrates have 2 functional groups

hydroxyl (OH) & carbonyl (carbon double bonded to an oxygen)

monosaccharides & disaccharides polarity

polar, hydrophilic, soluble

sucrose

disaccharide: glucose + fructose

lactose

disaccharide: galactose + glucose

maltose

disaccharide: glucose + glucose

polysaccharide monosaccharide amount

hundreds to thousands linked by glycosidic

polysaccharide polarity

polar, hydrophilic, non-soluble(b/c large size)

cellulose

polysaccharide

glycogen

polysaccharide: energy storage for animals

starch

polysaccharide: energy source for plants

sucrose: alpha glycosidic bond (straight across)

lactose: beta glycosidic bond (slanted)

cellulose bonds

has both alpha and beta glycosidic bonds

maltose bond

alpha glycosidic bond

hydrolysis word meaning

hydro = water, lysis = split

which linkage tends to be tougher

beta linkages

triglyceride composition

3 carbon glycerol molecule attached to 3 long chained fatty acids

all fatty acids have this functional group

carboxyl

ester linkage

when a fat creates a bond

functional group that glycerol has

hydroxyl

lipids (in animals)

main energy stores

animal lipids state

solid at room temp

plant oils state

liquid at room temp

structure of animal fats

single bonds and max amount of hydrogens

structure of plant fats

at least one double or triple bond (can have more) and less hydrogens

saturated fats

animal fats, solid at room temp, long fatty acid tail and single bonds

unsaturated fats

plant fats, liquid at room te mp, shorter fatty acid chains and double or triple bonds “have bends to it”

steroids

special lipids with carbon rings inside of them that are large and heavy, easier to transport through the bloodstream, can pass through fatty portion of CM as well become part of CM

wax

found in plants and some parts of animals, solid at room temp and can soften with increased temp

DNA

deoxyribonucleic acid

RNA

ribonucleic acid

nucleotide composition

phosphate, pentosugar and nitrogen base

DNA vs RNA

DNA has one less oxygen, one less hydroxyl group

RNA has one more oxygen, one more hydroxyl group

DNA is double stranded

RNA is single stranded

DNA has G, A, C, T

RNA has G, A, C, U

DNA is found in the nucleus and mitochondria

RNA is found attached to rough ER, cytoplasm, and nucleus

DNA is self-replicating

RNA is synthesized utilizing DNA

bond between nitrogenous bases

hydrogen bonds

pyrimidines

single ring (C, T, U)

purines

two rings (A, G)

A & T hydrogen # of bonds

2

C & G hydrogen # of bonds

3

phosphodiester linkage

bond found in nucleic acids, occurs at carbon 3

5 prime nucleotide

has phosphate group

3 prime nucleotide

does not have phosphate group

proteins

form necessary structures for all types of tissues, serve as chemical signallers, subunits are amino acids

amino acid composition

a central carbon, an amino functional group, a hydrogen, a carboxyl functional group, and an R-group that varies

peptide bond

formed between the amino group & carboxyl group of two amino acids

N terminus

first amino acid

C terminus

last amino acid, can only add amino acids through this end

polypeptide

several (50+ usually) amino acids strung together by peptide bonds

dipeptide

2 amino acids with a peptide bond

4 levels of protein organization

primary, secondary, tertiary, and quaternary structure

primary structure

a unique linear sequence of amino acids, 50 or more a.a. strung together by peptide bonds, known as a polypeptide

2 forms of secondary structure

Beta pleated sheet: forms a side-by-side alignment

or

A helix: hydrogen bonds between every 4th amino acid

how secondary structures are created

created as the protein begins to fold in on itself - atoms on the protein molecule begin interacting with other parts of the chain to create 3D shapes

tertiary structure creation

created by the side chains (R-group to R-group interactions) interacting with each other. This creates further folding → functional 3D structure, one can see multiple secondary structures within

quaternary structure creation

created when multiple tertiary structures come together to form a protein

primary structure

secondary structure

tertiary structure

quaternary structure

hydrophobic interactions (protein bonds)

amino acids orient themselves towards the centre of the polypeptide to avoid the water

disulphide bridge (protein bonds)

amino acid cysteine forms a bond with another cysteine forms a bond with another cysteine through its R group

hydrogen bonds (protein bonds)

Polar “R” groups on the amino acids form bonds with other Polar “R” groups

hydrophilic interactions (protein bonds)

these amino acids orient themselves outward to be close to the water

ionic bonds (protein bonds)

positively charged R group

codon

a structure that has 3 nitrogenous bases that codes for one amino acid

start codon

A U G and it’s methionine

stop codons

UAA, UAG, UGA

DNA and RNA process

DNA replication → RNA transcription → RNA processing → mRNA transport → protein translation