Macromolecules

Julia Castellani
Mind Map by Julia Castellani, updated more than 1 year ago
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Description

Macromolecules

Resource summary

Macromolecules
1 Carbohydrates (major energy source)
1.1 Monomers (Simple)
1.1.1 Monosaccharides (C6H12O6)

Annotations:

  • -5 (pentose) or 6 (hexose) carbons
1.1.1.1 Glucose
1.1.1.2 Fructose

Annotations:

  • 2 of carbons are outside of ring
1.1.1.3 Galactose
1.1.2 Disaccharides (double sugars)

Annotations:

  • molecules joined by condensation reactions (a water molecule is lost)
1.1.2.1 Maltose (glucose + glucose)

Annotations:

  • -alpha 1-4 linkages -formed by a condensation reaction (lose a water molecule)
1.1.2.2 Sucrose (glucose + fructose)

Annotations:

  • -a.k.a table sugar -most comes from beets
1.1.2.3 Lactose (galactose + glucose)

Annotations:

  • -milk sugar
1.2 Polysaccharides (Complex)

Annotations:

  • multiple mono/disaccharides join
1.2.1 Storage Polysaccharides
1.2.1.1 Starch (plants)

Annotations:

  • -Insoluble -alpha 1-4 linkages
1.2.1.1.1 Amylose (unbranched)
1.2.1.1.2 Amylopectin (branched)
1.2.1.2 Glycogen (animals)

Annotations:

  • -insoluble; more branches than amylopectin -stored in liver and muscle tissue (skeletal) -alpha 1-4 + 1-6 linkages
1.2.2 Structural Polysaccharides
1.2.2.1 Cellulose (fibre)

Annotations:

  • -linear, unbranched -forms fibrils which reinforce plant cell walls -cannot be digested by animals
1.2.2.2 Chitin

Annotations:

  • -polymer of an amino sugar -makes up exoskeletons -chitin + calcium = hard -semi conductor under certain conditions
2 Proteins (Polypeptides)

Annotations:

  • -50% of dry weight of cells -"molecular tools" -NATIVE CONFORMATION is the shape in which a protein functions best    -assisted by chaperone proteins -proteins can be DENATURED (unfold and become non-functional) by changes in temp, pH, or salt concentration 
2.1 Primary Structure (DNA blueprint)

Annotations:

  • -sequence of amino acids -determined by a single gene -peptide bonds
2.2 Secondary Structure (regular, repeated backbone folding)
2.2.1 Alpha Helix (H-bonds b/w every 4th peptide bond)
2.2.2 Beta Pleated Sheet (H-bonds b/w polypeptide chains)
2.3 Tertiary Structure (irregular folding of a polypeptide via R-group interactions)

Annotations:

  • -R-group (side chain) interactions -"Globular proteins" b/c chape is irregular and globular
2.3.1 H-bonds
2.3.2 Ionic bonds
2.3.3 disulfide bridge (covalent)
2.3.4 Hydrophobic
2.4 Quaternary Structure (multiple polypeptides)

Annotations:

  • -weak interactions/disulfide bridges (eg -s-s-) -each polypeptide chain is a SUBUNIT of the protein
3 Enzymes (catalysts)

Annotations:

  • -reduce activation energy required for a reaction to occur
3.1 Thermodynamic Laws

Annotations:

  • 1. total amt of energy in the universe is constant 2. Disorder (entropy) in the universe is always increasing
3.2 Activation Energy

Annotations:

  • amount of energy required to start a reaction
3.3 Lock and Key Theory

Annotations:

  • -one enzyme (loc) has a specific shape for one set of substrates (key)
3.4 Induced-Fit Theory

Annotations:

  • -shape of the active site changes somewhat after substrate(s) bind to it
3.5 Competitive Inhibition

Annotations:

  • -"look-alike" molecule binds to active site -enzyme unable to bind with substrate -enzymes inactivated
3.5.1 Penicillin

Annotations:

  • kills succeptible bacteria by inhibiting the enzyme that catalyzes the final step in cell wall biosynthesis
3.5.2 ACE Inhibitors

Annotations:

  • Inhibit enzymes that make angiotensin II hormone (constricts blood vessels)
3.5.3 Ethanol

Annotations:

  • antidote for methanol poisoning
3.5.4 Grapefruit

Annotations:

  • Inhibit a drug-metabolizing enzyme in the small intestine
3.6 Non-Competitive Inhibition

Annotations:

  • Molecules bind to a site adjacent to active cite and change the shape of the active site
3.6.1 Eg) Heavy metals
3.7 Allosteric Regulation

Annotations:

  • Molecules bind to a site AWAY from active site
3.7.1 Allosteric activation
3.7.2 Allosteric deactivation
3.7.3 Co-enzyme (vitamin aiding enzyme's action)
3.7.4 Co-factor (mineral aiding enzyme's action
4 Lipids (Energy and Structure)

Annotations:

  • -C, O, H (no ratio) -hydrophobic
4.1 Fats and Oils

Annotations:

  • *Glycerol + 3 Fatty Acid chains *joined by ester linkages
4.1.1 Saturated Fatty Acids

Annotations:

  • -solid at room temp *Every carbon bond holds a Hydrogen -eg) animal fats
4.1.2 Unsaturated Fatty Acids

Annotations:

  • -liquid at room temp *Some double bonds (more double bonds = healthier)
4.1.2.1 Monounsaturated (1 double bond)
4.1.2.2 Polyunsaturated (more than 1 double bond)
4.1.2.3 Cis isomer (H's on same side)
4.1.2.4 Trans isomer (H's on opposite side)
4.2 Phospholipids

Annotations:

  • -fat derivitives -important in cell membranes *AMPHIPATHIC (hydrophobic + hydrophillic regions)
4.2.1 Hydrophilic head
4.2.2 Hydrophobic tails

Annotations:

  • -2 fatty acid chains
4.3 Sterols

Annotations:

  • -flat ring structure of carbons
4.3.1 Cholesterol (most common)

Annotations:

  • -found in cell membranes -makes membranes less permeable
4.3.1.1 High-density Lipoprotein (good)
4.3.1.2 Low-Density Lipoprotein (bad)
5 Nucleic Acids / Polynucleotides (Structure, Functional)

Annotations:

  • -in nucleus and mitochondria -polymers of nucleotides
5.1 Nucleotides
5.1.1 Consists of:
5.1.1.1 a nitrogen base
5.1.1.1.1 Pyrimidines (single ring)
5.1.1.1.1.1 Thymine (DNA) / Uracil (RNA)
5.1.1.1.1.2 Cytosine (DNA & RNA)
5.1.1.1.2 Purines (double ring)
5.1.1.1.2.1 Adenine (DNA & RNA)
5.1.1.1.2.2 Guanine (DNA & RNA)
5.1.1.2 a 5-carbon sugar
5.1.1.2.1 Deoxyribose (DNA)
5.1.1.2.2 Ribose (RNA)
5.1.1.3 a phosphate group
5.1.2 2 types
5.1.2.1 Deoxyribonucleic Acid

Annotations:

  • -Chemical basis for the gene -found in nuclei of cells
5.1.2.2 Ribonucleic Acid

Annotations:

  • -close copies of genes -found in cytoplasm
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