living chemistry

biological molecules primary consist of

carbon bonds or carbon bonded to other molecules

polymerization

the process of linking monomers (small molecules) to form a polymer (large molecules), typically through chemical reactions.

dehydration synthesis

a macromolecule

a large molecule (essentially a a bunch of polymers)

the 4 macromolecules

Carbohydrates, proteins, lipids, and nucleic acids.

dehydration synthesis

This is the chemical process of combining monomers by removing water

hydrolysis

the chemical process of polymers becoming monomers by adding water

the monomer of carbohydrates

monosaccharides

the monomer for proteins

Amino acids

Lipids do not have a true monomer because they are not true polymers

monomer for lipids

building blocks of fats

fats are made from glycerol + fatty acids when people say (monomer) they mean this

monomer of nucleic acids

nucleotide

poly

many

-mer

unit

mono

one

Carbon

biological molecules consist of this element either bonded together or bonded to other molecules

how many bonds can carbon form

4 covalent bonds

it maybe be bonded to functional groups with specific properties

depolymerization

breaks down larger molecules into smaller monomers

hydrolysis

A.K.A protein

polypeptides

R-group

This helps determine protein function

they are at the ends of each amino acids. example in picture

function of proteins

enzymes: speed up chemical reaction

structure: support cells and tissue

transport: move substances, like oxygen

movement: helps muscles contract

defense: antibodies protect the body

primary protein structure

this is the first level of protein structure (its unique for every protein)

tertiary protein structure

three- dimensional folding pattern of protein due to side chain

r- groups interacting with each other

secondary protein structure

this is the folding or coiling stage of amino acid chain interaction

quaternary protein structure

protein consisting of more than one amino acid chain (formed when two or more polypeptide chains (subunits) come together and function as one protein complex)

peptide bonds (covalent)

between amino acids

stabilizes the primary structure

hydrogen bonds

between backbone atoms (no r-groups involved)

stabilizes secondary structure

creates a helices and b plated sheets

this level is stabilized by multiple bonds

hydrogen bond (between r-groups)

ionic bonds (between charged r-group)

hydrophobic interactions (nonpolar r-groups cluster inwards)

disulfide bridges (strong covalent bonds between cysteines)

this gives the protein its 3D shape

This level is the subunit interaction

hydrogen bonds

ionic bonds

hydrophobic interaction

sometimes disulfide bridges

Nitrogenous base - adenine, guanine, cytosine, thymine, or uracile

sugar- ribose in RNA, or deoxyribose in DNA

and a phosphate group

nucleotide is made of this