Unit 2: Chemistry and Cellular Functions Flashcards
Biological molecules of life.
Four types of biological molecules
Carbohydrates, Proteins, Lipids, and Nucleic Acids
Carbohydrates
- Most abundant of biological molecules (sugar)
- Consists of Monosaccharides, Oligosaccharides, and Polysaccharides
- Quick Energy
Monosaccarides
Monomer. Basic unit of carbohydrates. C6 H12 O6
Ex. Glucose & Ribulose
Oligosaccharides
Covalently linked monosaccharide units. (part of carbohydrates)
Associated with proteins (glycoproteins) and lipids (glycolipids)
Polysaccharides
Large monosaccharide units. (part of carbohydrates)
ex. Starch & Glycogen
Lipids
- Organic compounds that are insoluble in water (i.e. hydrophobic
- Fats, phospholipids, cholesterol and steroids
- Consists of monomers called “fatty acids)
Proteins
- Monomers are amino acids
- Synthesized from the same 20 amino acids.
- Form peptide bonds, compose dipeptides, tripeptides, oligopeptides, and polypeptides.
Nucleic Acids
- Large biomolecules that plays essential roles in cells and viruses; carries genetic information
- Two types: Deoxyribonucleic Acid (DNA) & Ribonucleic Acid (RNA)
- Made of monomers called nucleotides (each nucleic acid made from 8 nucleotides)
Structure of Carbohydrates
- Consists of long carbon chains attached to hydroxyl and carbonyl groups.
- Empirical Formula: Cn H2 O (always 2x many H than O)
Structure of Lipids
Saturated compounds (long organic molecules without pi bonds).
General Structure: Glycerol backbone, 2 fatty acid tails (long carbon chains; 16-18 carbons), and a phosphate group.
Structure of Proteins
Have a primary amino group, carboxylic acid group substituent, and a centered carbon atom (except proline).
Also forms peptide bonds. (e.g. dipeptides, tripeptides, oligopeptides, and polypeptides).
Proteins
- Complex unbranched macromolecules
- Involved in Growth and Repair, Regulation, and Enzyme Activity
- Dietary Sources: Fish, poultry meat, beans, peanuts
Structure of Proteins
- Consists of elements S, P, C, O, H, N
- Each has a conformation unique shape (primary, secondary [hydrogen bonding alpha helix, beta pleated sheet], tertiary, and quarternary).
Amino Acids
- Make up proteins
- Functional groups: amino group and carboxyl group.
- Linked by together via peptide bonds
Primary Structure of Proteins
- Amino Acid sequence in a polypeptide chain (if less than 20, they are oligopeptides, e.g. hormones)
- Peptide bonds formed by condensation reaction, between amino group of the first AA and the carboxyl group the 2nd AA.
Secondary Structure of Proteins
- Forms hydrogen bonding within the polypeptide module
- Folds into alpha helix (RH) or a beta pleated sheet (N-H and C=O bond)
Tertiary Structure of Proteins
- 3-D shape, determines protein’s specificity
- Hydrogen bonding and Ionic Bonding between R groups of amino acids
- Hydrophobic Interactions (Methyl-based groups)
- Disulfide bonds between cysteine amino acids
Quarternary Structure of Proteins
- Proteins with more than one polypeptide chain
- Hydrophobic interactions, hydrogen bonds, and ionic interactions hold subunits together
Chaperone Proteins
Assist with protein folding
Prions
Misfolded proteins
Denaturation
Loss of protein shape and function. Goes from most complex (e.g. Quarternary or Tertiary) to least complex (Primary).
Disaccharides
Formed by two monosaccharides, C12 H22 O11
Saturated Lipids
Structure consists only of single (sigma) bonds
Unsaturated Lipids
Structure consists of at least one alkene (carbon-carbon double bond)
Steroids
Lipids that do not have the same general structure as other lipids
Phospholipids
- Major component of the cell membrane, boundary between inside and outside of cell.
- 22 fatty acids attached to the glycerol backbone and form 2 hydrophobic tails
- Third hydroxyl glycerol group head attacks water and self assemble into double layer
Nucleic Acid
- Hereditary information encoded in ribonucleic acid (RNA) and deoxyribonucleic acid (DNA)
- Made up of nucleotide subunits
- Carbon atoms of deoxyribose sugar numbered 1 to 5.
