polymer
long molecule consisting of many similar building blocks linked by covalent bonds
enzymes
specialized macromolecules that speed up chemical reactions
starch
energy storage in plants; loose structure
glycogen
energy storage for animals; found in the liver and muscle cells
cellulose
structure for plants (cell walls) with a tight structure; most abundant organic compound
- parallel molecules are grouped into units called microfibrils
- we can't digest because of beta configuration (upside down)
chitin
structure for insects' exoskeletons; fungi cell walls
- beta links+nitrogen-containing appendage
ester linkage
covalent bonds formed between hydroxyl and carboxyl
saturated fat
saturated by hydrogen; no double bonds between carbons
- solid at room temp due to tight packing
unsaturated fat
double bonds between carbons, causing a kink in chain
- liquid at room temp
cis-fat
naturally occuring unsaturated fat
- hydrogens on the same side of double bond
trans-fat
unnaturally occuring unsaturated fat that is bad
- hydrogens on opposite side of double bond
monosaccharide
simplest carbohydrate with a 1:2:1 ratio (C:H:O)
- examples: glucose, fructose, galactose
- turn into rings in water
- no nitrogen or phosphorus
- oxygen links in rings
- carbon skeleton is 3-7 carbons long
disaccharide
two monosaccharides bonded together by a glycosidic (covalent) bond
-carbohydrate
polysaccharide
multiple polymers linked together
- only uses glucose polymers
- examples: starch, glycogen, cellulose, chitin
- carbohydrate
lipid
contain carbon and hydrogen (+ some oxygen)
triglyceride
a fat
- made up of a glycerol backbone and three fatty acid tails
- carbon at the end of fatty acid tail is part of a carboxyl group that acts as a hook
- hydrophobic because the hydrocarbon chains are nonpolar
- fatty acid tails joined to glycerol by an ester linkage
- dehydration reaction
phospholipid
makes up cell membranes by forming a bilayer in water
- made up of a glycerol backbone, two fatty acid tails, and a phosphate group
- tail is hydrophobic and the head is hydrophilic (due to negative charges of oxygen)
steriod
4 fused rings; lipid
- example: cholesterol - component of animal cell membranes+precursor where other steriods are synthesized (in liver and diet)
protein
made up of 20 different amino acids
- bonds between amino acids are peptide (covalent) bonds
functions of proteins
- speed up chemical reactions (enzymes)
- defense (using antibodies)
- storage
- transport (ex: hemoglobin)
- cellular communication (through hormones)
- movement
- structural support (ex: keratin)
amino acid
an organic molecule with an amino group and carboxyl group with an alpha carbon in the middle
- R group differs
- can be polar or nonpolar (negative from O and positive from NH2)
polypeptide
polymer of many amino acids linked by peptide bonds (between carboxyls and amino groups)
primary protein structure
sequence of amino acids that is determined by genetic code
- held together by peptide bonds
- dictates other levels due to the chemical nature+side chains
secondary protein structure
polypeptide chains coiled or folded in patterns
- hydrogen bonds between the repeating components of polypeptide backbone (between nitrogens and oxygens)
- between non R groups
- alpha helix and beta pleats
alpha helix
delicate coil held by hydrogen bonds between every fourth amino acid
beta pleat
two or more segments of polypeptide chain (beta strands) that are connected by hydrogen bonds
tertiary protein structure
overall shape of a polypeptide resulting from the interactions between the side chains (R groups)
- uses almost all types of bonds
- hydrophobic interaction can occur
- disulfide bridges can occur
Hydrophobic interaction
the nonpolar chains on a protein end up in clusters (due to Van der Waals interactions) at the core of the protein - away from the outside water
disulfide bridge
covalent bond formed between two monomers with sulhydryl groups
- brought together from the protein folding
Quaternary structure
overall protein structure that results from the clumping of polypeptides
- all proteins with multiple polypeptides
flow of a cell
DNA --> RNA --> Protein (polypeptide)
denaturation
happens when a protein unravels+loses shape
- chemical bonds and interactions may be destroyed (breaks shape)
- makes the protein biologically inactive
- caused by changes in pH, salt concentration, temperature, etc.
- can happen if transferred from an aqueous environment to nonpolar solvent
gene expression
the process of DNA and RNA
DNA
genetic material that organisms inherit from their parents
- replicates itself to pass on genes
- double helix and deoxyribose sugar
- sugars and phosphates form a sugar-phosphate backbone when bonded in phosphodiester linkage
DNA nucleotide
contains a deoxyribose sugar, phosphate group, and nitrogenous base (A,T,C,G)
RNA nucleotide
contains ribose sugar, phosphate group, and nitrogenous base (A,U,G,C)
RNA
controls protein synthesis in ribosomes
- single strand and ribose sugar
adenine
2-ringed purine
- pairs with thymine (in DNA) and uracil (in RNA)
- forms two hydrogen bonds
guanine
2-ringed purine
- pairs with cytosine
- forms three hydrogen bonds
cytosine
single-ringed pyrimidine
- pairs with guanine
- forms three hydrogen
thymine
single-ringed pyrimidine
- only found in DNA
- pairs with adenine
- forms two hydrogen bonds
uracil
single-ringed pyrimidine
- only found in RNA
- pairs with adenine
- forms two hydrogen bonds
phosphodiester bond
a covalent bond between the phosphate and sugar
deoxyribose sugar
pentose sugar in DNA, but missing one oxygen in a hydroxyl group
- contains a 5` end and 3`end
ribose sugar
pentose sugar in RNA
- contains a 5` end and 3` end
5` end carbon
the fifth carbon in the pentose sugar that bonds to the phosphate group
- "free fosphate"
3` end carbon
the third carbon in the pentose sugar that is a bonding site for another nucleotide's phosphate group
- "free three"