BIOFOUND 2.1 Biological Molecules pt 1

carbohydrates, lipids, nucleic acids, and proteins

four types of biological molecules

polymers

a chain of small repeating molecules that are held together by covalent bond

monomer

a molecule that can be bonded to other identical molecules

dehydration synthesis

process used to make new polymers from smaller building blocks, forms a covalent bond between two molecules by REMOVING two hydrogen atoms and an oxygen atom

hydrolysis

process used to break apart large polymers into their building blocks, breaks a covalent bond between two molecules by ADDING two hydrogen atoms and one oxygen atom

amino acids

what is a monomer in a protein sequence?

protein sequence

the order of amino acids in a protein

peptide bond

a special kind of covalent bond used to connect the amino acids in a polymer

alpha carbon, amino group, carboxyl group, side chain

what are the four main parts of an amino acid?

alpha carbon, amino group, carboxyl group

what three parts of the amino acid make up the “back bone”?

alpha carbon

single carbon atom which all other parts of the amino acid are connected to

amino group (NH₃⁺)

nitrogen base connected to the alpha carbon

carboxyl group (COOH)

a biological acid that is used to form peptide bonds

side chain

a unique feature in Amino acids, this differs for every amino acid while the backbone stays consistent

negatively charged group of amino acids

this group of amino acids have side chains that are acidic which release a hydrogen ion into the water that leaves behind a negatively charged side chain

positively charged group of amino acid

this group of amino acids have nitrogen based side chains that act like bases (absorb hydrogen ions), when basic side chains absorb hydrogen ions they become positively charged

uncharged polar group of amino acids

this group of amino acids have polar side chains that are hydrophilic and uncharged, side chains on these amino acids will easily and often participate in chemical reactions that modify protein structure and function

non polar group of amino acids

this group of amino acids are hydrophobic, the more hydrocarbons they have the more strongly hydrophobic they are this helps to maintain protein structure using the hydrophobic affect

formation of a peptide bond

when forming a protein, the amino group of one amino acid chemically bonds to the carboxyl group of the next

protein folding

in order to be fully functional, proteins must do this action which must stay in a 3D shape to stay functioning properly

primary structure

in this stage the order of the amino acids are as they are unfolded. each protein has a unique version of this

secondary structure

in this stage the backbone of the protein folds into simple shapes by forming hydrogen bonds with itself

alpha helix

a spiral shaped structure found during the second stage of protein structure

beta sheet

a flat sheet structure found during the second stage of protein structure

tertiary structure

the third level in protein folding, side chains begin to interact with each other which causes the simple shapes to fold on top of each other and forms three dimensional shapes (for many but not all proteins, folding stops here)

quaternary structure

the fourth level in protein folding, some proteins must interact with two or more other proteins to become functional: these interactions are usually temporary and held together by hydrogen bonds and electrical attractions