Lecture 2 Flashcards
Polarity
The unequal distribution of electrons across a covalent bond
Monomer
Single building block of molecules
Polymer
Chain of similar or identical subunits
Synthesis (Condensation) Reaction
Formation of a covalent bond between monomers, energy is required, water is a product
Breakdown (Hydrolysis) Reaction
Breaking of covalent bonds between monomers, energy is released, water is a reactant
Carbohydrates
Responsible for energy storage, cell structure, and cell-cell recognition
Disaccharide
Formed by a covalent bond between monosaccharides
Glycosidic Bond
Covalent bond joining a carbohydrate to another carbohydrate
Polysaccharide
Long chain of repeating units, held together by glycosidic bonds
Starch
Energy storage in plants, nutritional polysaccharide, polymer of alpha glucose, alpha 1-4 glycosidic bonds
Glycogen
Energy storage in animals, nutritional polysaccharide, polymer of alpha glucose, alpha 1-6 glycosidic bonds, highly branched
Cellulose
Structural polysaccharide in plants, polymer of beta glucose, beta 1-4 glycosidic bonds
Chitin
Structural polysaccharide in insects, creates exoskeleton
Lipids
Not true polymers (not made up of a single unit), hydrophobic and non-polar
Fatty Acids
Single hydrocarbon chain, 16-18 carbons long, can esterify to a 3 carbon glycerol backbone
Fats
Energy storage and insulation, formed by 3 fatty acids attached to a 3 carbon glycerol backbone
Saturated Fat
No carbon carbon double bond, solid at room temperature, e.g. animal fat
Unsaturated Fat
Carbon carbon double bond forms ‘kink’ in fatty acid tail, liquid at room temperature, e.g. plant fat
Trans Fat
Carbon carbon double bond present, yet no kink in chain
Phospholipids
Structural component of plasma membrane, 2 fatty acid tails attached to glycerol backbone, but with a phosphate head attached to third carbon
Steroids
Class of lipids based on cholesterol, used for hormones and membrane integrity
Proteins
Polymers of amino acids, held together by peptide bonds
Primary Structure
First degree of protein folding, determined by DNA sequence
Secondary Structure
Second degree of protein folding, driven by R group interactions, stabilized by hydrogen bonds
Tertiary Structure
Third degree of protein folding, driven by hydrophobic R groups, stabilized by R group interactions
Quaternary Structure
Optional, some proteins form multi-subunit complexes (more complex structures), driven by same forces as tertiary structure
Chaperones
Proteins that assist in the folding of other proteins, or that target mis-folded proteins for degradation
Nucleic Acids
Store and transmit hereditary information (RNA/DNA)
DNA
Polymer of deoxyribonucleotides
RNA
Polymer of ribonucleotides
Pyrimidine
Single ring nitrogenous base, e.g. Uracil, Cytosine, Thymine
Purine
Double ring nitrogenous base, e.g. Adenine, Guanine
Phosphodiester Bond
Covalent bonds joining nucleotides
Directionality
End to end chemical orientation, Amino to Carboxylique Terminal in proteins (N to C) or 5 to 3 in DNA (Carbon 5’s phosphate to Carbon 3’s OH)