Macromolcules Flashcards
Carbon Based Molecules
composed with at least one C, they all have similar funtional groups
Polymers
may be homo or hetero depending on whether they are composed the same or different monomers
Monosaccharide
glucose, fructose
Polysaccharide
consists of long chains of monomers
starch, glycogen, cellulose
Condensation
the removal of water to form bonds in biomolecules
Hydrolysis
splits polymers into monomers by adding water
Four classes of biomolecules
Carbs, nucleic acids, proteins, and lipids
Carbohydrates
C,H,O, lots of OH groups
sugars and starches
can be monomers
typically form carbon rings in shape of hexagon or pentagon
glucose is the most common monosaccharide
Nucleic Acids
sequences of nucleotides
DNA, RNA, ATP
Proteins
chain of amino acids, work horses of life
Lipids
- hydrocarbons, hydrophobic
- fatty acids and membrane
- non polar
- many diverse forms
Glucose
alpha glucose which is below the ring
beta glucose which is above the ring
Carbohydrate polymers
small polymers are called oligosaccharides usually between 3-8 monomers
Dehydration Synthesis
reaction between two hydroxyl groups forming an ether
Cellulose
Most abundant macromolecule on earth
comes from orderly alignment of hydrogen to form sheets
Carbohydrate Function
- primary fuel for energy production in cells
- some complex carbs provides structural support
- some combine with other molecules to form receptors
Fatty Acids
saturated, no double bonds
Triglycerides
polymers of fatty acids form ester bonds, fats and oils
Fatty Acids Lipid Function
efficient long term energy storage
adaptive for storage for potential energy
Phospholipid
are modified triglycerides that are amphipathic
have both polar and non polar regions causing self organization
Steroids
complex hyrdocarbon rings
Cholesterol
Parent molecule from which some important hormones are built
* Synthesize in liver of animals (85% in
humans)
– Eating saturated fats can stimulate
production.
* Found in membranes of animals (thickens membrane)
Peptide Bonds
A dehydration
synthesis reaction
between amine (NH2)
and carboxyl (COOH)
of neighboring amino
acids.
* Forms a polypeptide
as more amino acids
are bonded into chains
Protein Fold
Primary: The amino acid sequence of polypeptide
Secondary: Regular coiling of the chain (a helix and b sheet)
– Folding is driven by hydrogen bonding
Tertiary: Complex coiling of the 2° coils
* disulfide bridges (S-S bond b/w
cysteines)
* Alignment of hydrophobic/philic
regions
Quaternary: Two or more polypeptides
together
Chaperones
Some proteins fold spontaneously in a given environment but many proteins require Chaperone proteins, which help proteins fold correctly.
* Prevent newly made polypeptides from clumping
together and speed up folding process
Inducing proteins to change shape
Heat- can cause permanent denaturing.
* Salinity- can influence ionic bonds b/w aa’s
* pH- can influence hydrogen bonds b/w aa’s
* CoFactors- Metals and non-protein molecules that can bind to proteins.
* Substrate molecules bind to enzymatic proteins
to perform reactions.
* Signaling molecules (ligands)- bind to proteins to
induce change.
* Physical stress- sound, light, pressure can
induce changes in some proteins
Glycosides
sugars with other side groups
Nucleic Acids Function
DNA - Genes
* RNA: Manages synthesis of proteins
* ATP is a universal energy molecule of life (akin to a
rechargeable lithium battery).
* NAD+ is a short term electron carrier molecule
* Some are chemical messengers (cAMP)
* Metabolic intermediates in the synthesis of alkoids and
other amines.
* Genetic and cell control
Phenolitics
composed mostly of phenol rings
Amines
ammonia where at least one H is replaced by small carbon groups
Alkaloids
complex amines with cyclic organic structure, usually plant origin
Isoprenoids
technically lipid derivatives
