introduction to bilogical macromolecules Flashcards
what do variations in carbon skeletons allow for?
molecular diversity
carbon can form large molecules known as
macromolecules
polymers
chain like macromolecules of similar or identical repeating units that are covalently bonded together
monomers
the repeating units that make up polymers
dehydration reaction
bonds two monomers with the loss of H2O
the OH of one monomer bonds with the H of another monomer forming H2O, which is released
A+B—>AB+H2O
hydrolysis
breaks the bonds in a polymer by adding H2O
one H of the H2o bonds to one monomer and the remaining OH of the H2O attaches to the other monomer
AB+H2O—>A+B
carbohydrates include blank and blank of sugars
sugars
polymers
what groups do carbohydrates contain?
a carbonyl group and many hydroxyl groups
comprised of C, H, and O
monosaccharides
simple sugars
molecular formulas with multiples of the unit CH2O
most common is glucose
can serve as building blocks for amino acids, or as monomers for di and polysaccharides
disaccharides
two monosaccharides joined together by covalent bonds
most common is sucrose
polysaccharides
polymer with many sugars joined via dehydration reactions
storage polysaccharides
plants store starch (polymer of glucose monomers); allows plants to store excess glucose
animals store glycogen (polymer of glucose); stored in liver and muscle cells
structural polysaccharides
cellulose: tough substance that forms plant cell walls
chitin: forms exoskeleton of arthtropods
formation of a protein
amino acid—>peptide—>polypeptide—>protein
protein
molecule consisting of polypeptides (polymers of amino acids) folded in a 3D shape
comprised of C, H, O, N, and S
shape determines function
amino acids
molecules that have an amino group and a carbonyl group
general structure of protein
amino group, carbonyl group, and variable side chain (R)
unique aspects of the AA are based on what?
the side chain’s physical and chemical properties
side chains can be grouped as
nonpolar (hydrophobic)
polar (hydrophilic)
charged/ionic (hydrophilic)
side chains interact, which determine the blank and blank of the protein
shape
function
to form a peptide bond, the blank group of one AA must be positioned next to the blank group of another AA
carboxyl
amino
polypeptides
many amino acids linked by peptide bonds
each polypeptide has unique sequence of AAs and directionality
each end of a polypeptide is chemically unique
one end is a free amino group (N-terminus)
one end is a free carboxyl group (C-terminus)
the sequence of AAs determines the what?
3D shape
when a polypeptide twists and folds (because of R group interaction), it forms a
protein
functions of proteins
antibody: help protect the body from disease
enzyme: carry out chemical reactions or assist in creating new molecules
messenger: transmit signals (ie hormones)
structural: provide structure and support
transport/storage: bind to and carry small atoms and molecules through the body
primary level of protein structure
linear chain of AA
determined via genes
dictates secondary and tertiary forms
secondary level of protein structure
coils and folds due to hydrogen bonding with the polypeptide backbone
beta pleated sheet: hydrogen bonds between polypeptide chains lying side by side
alpha helix: hydrogen bonding between every fourth AA
tertiary level of protein structure
3D folding due to interactions between the side chains of the AAs
reinforced by hydrophobic interactions and disulfide bridges of the chains
the covalent bonds formed between sulfur atoms and two cysteine monomers
quaternary level of protein structure
association of two or more polypeptides
found in only some proteins
nucleic acids
polymers made of nucleotide monomers
nucleic acids function
store, transmit, and express hereditary info
two forms of nucleic acids
deoxyribonucleic acid (DNA)
ribonucleic acid (RNA)
components of nucleic acids
nucleotides—>polynucleotides—>nucleic acids
three parts of nucleic acids
nitrogenous base
five carbon sugar (pentose)
phosphate group
types of nitrogenous based
pyrimidines and purines
pyrimidines
one ring with 6 atoms
cytosine; thymine (only found in DNA); uracil (only found in RNA)
purines
one ring with 6 atoms bonded to one ring with 5 atoms
adenine; guanine
five carbon sugar
a sugar is bonded to the base
in DNA the sugar is deoxyribose
in RNA the sugar is ribose
a phosphate is added to the 5’ carbon of the sugar to form a what?
nucleotide
what groups link adjacent nucleotides?
phosphate
directionality; 5’ to 3’
the sequence of bases along the DNA or mRNA is blank for each blank
unique
gene
sequence of bases along the DNA or mRNA dictates
primary structure of a protein
3D structure of a protein
DNA
consists of two polynucleotides
forms a double helix
strands are anti parallel
held together by hydrogen bonds between bases
RNA
single stranded polynucleotide
variable in shape
due to base pairing within RNA
lipids
class of molecules that do not include true polymers
generally small in size
often not considered to be a macromolecule
lipids are nonpolar- hydrophobic
types of lipids
fats
phospholipids
steroids
fats are composed of blank and blank
glycerol
fatty acids
glycerol
classified as an alcohol (hydroxyl groups)
fatty acids
ping carbon chains (carboxyl group at one end)
three fatty acids join to a glycerol via blank
ester linkage
ester linkage
bond between a hydroxyl and carboxyl group
saturated fatty acid
no double bonds between carbon sun the carbon chain=more hydrogen (think: saturated with hydrogen)
unsaturated fatty acid
contains one or more double bonds
phospholipids
major component of cell membranes; two fatty acids attached to a glycerol and a phosphate
assemble as a bilayer in H2O; tails are hydrophobic and head is hydrophilic
steroids
lipids that have four fused rings
unique groups attached to the ring determines the type of steroid
