Macromolecules Flashcards
Organic macromolecules
Large organic (carbon based) molecules that are made of monomers
Monomer
Single subunit that makes up a polymer
Polymer
Large molecule made of identical or similar repeating monomers
Dehydration reaction (condensation)
Formation of covalent bond between monomer of macromolecules with a loss of water; requires energy and enzymes
Hydrolysis
Splitting or breaking of a covalent bond between monomers of macromolecules given the addition of water
Carbohydrate function
Energy storage and structure
Carbohydrate monomer
Monosaccharides
Carbohydrate polymer
Polysaccharides
Bond formation in carbohydrates
Glycosidic linkage
Starch function
Energy storage in plants
Starch structure
Alpha glucose monomers that form a helix or branch
Cellulose function
Structural macromolecule in plants
Cellulose structure
Beta glucose monomers form straight chains
Cellulose molecules form microfibrils when held together by hydrogen bonds
Glycogen function
Energy storage in animals
Glycogen structure
Alpha glucose monomers; form bonds 1-4 and 1-6; highly branched allows the molecule to be less ridged as opposed to starch
Chitin function
Structural macromolecule in animals
In exoskeletons and fungal cell walls
Chitin structure
Beta glucose structure with an amino functional group on carbon 2
Lipid functions
Energy storage, membranes, insulation, shock absorbance, and steroids/hormones
Bond formation in fats
Ester linkage; dehydration bond between glycerol backbone and carboxyl group of fatty acids
Structure of fats
Glycerol backbone + 3 fatty acids
Saturated fatty acids
Saturated with hydrogen, no double bonds, straight chained, solid at room temperature
Unsaturated fatty acids
Not every carbon has maximum hydrogens due to the presence of double bonds, branched and thus liquid at room temperature
Hydrogenation
The forceable addition of hydrogen to unsaturated fatty acids which causes the formation of trans-fats
Phospholipid structure
Phosphate group (-) + glycerol + 2 fatty acids
Amphipathic molecule
Molecule composed of both hydrophobic and hydrophilic parts
Hydrophobic end of phospholipid
Fatty acid tails
Hydrophilic end of phospholipid
Phosphate heads
Steroid structure
4 interlocking rings, with identifying side chains
Steroid function
Many are hormones
Cholesterol regulates the fluidity of the cell membrane ensuring resistance to temperature changes
Nucleic acid function
Make up genes, involved in protein synthesis and gene regulation
Nucleic acid monomers
Nucleotides
Nucleic acid polymers
DNA and RNA
Nucleotide structure
Pentose sugar (ribose or deoxyribose) + phosphate group + nitrogenous base
How do nucleotides bond
Phosphate group to pentose sugar
Hydrogen bonds between the nitrogenous bases
Pyrimidines
6 member ring; Thymine, Uracil, Cytosine
Purines
6 member ring joined to 5 member ring; Adenine and Guanine
Dinucleotides
NADH, FADH2, NADPH
Protein
One or more polypeptide chains folded or coiled into a specific conformation
Protein bond between the carboxyl and amino groups
Peptide bond
Protein monomer
Amino acids
Protein polymer
Polypeptide
Protein functions
Catalysis
Cell support
Cell movement
Cell to cell communication
Cell division
Cell receptors
Passive transport
Active transport
Hormones
Neurotransmitters
Immune defense
Organism protection, support, and movement
Native conformation
The usual shape necessary for a protein to function normally
Denaturing
Breaking bonds of a protein to change it’s structure thus effecting function
Caused by heat, pH, ionic concentration, or agitation
Renaturing
The reformation of proteins to their native conformations; possible if no covalent bonds have been broken
Primary structure
Single amino acid chain (polypeptide)
Secondary Structure
Alpha helix or beta pleated sheet held by H bonds
Tertiary Structure
Three dimensional folded structure cause by side chain interactions; disulfide bridges (strong bond), ionic bonds (R groups), H bonds, Van Der Waals forces, hydrophobic interactions
Quaternary Structure
Multiple polypeptide chains folded together, same bonding as tertiary structure
Chaperonins
Enzyme that assists with some complex protein folding; protein enters enzyme chamber with a specific environment that is needed for protein folding
Intrinsically disordered proteins
Proteins that do not have a native conformation (distinct 3-D structure) until they interact with a target molecule or protein
