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Macromolecules

Organic Molecules

  • What is an organic molecule

  • Process that builds polymers- Dehydration synthesis

  • Process that breaks down monomers- Hydrolysis

Carbohydrates

  • C,H, O (in a 1:2:1 ratio)

  • Structure/Function: provides both energy and structure to many organisms

  • Monosaccharides (Glucose, Fructose, Galactose)

  • Disaccharides (Sucrose, Lactose, Maltose)

  • Polysaccharides (Starch, Cellulose, Glycogen)

Lipids

  • Made of: glycerol backbone, 2 fatty acid tails (hydrophobic), and a phosphate group (hydrophilic).

  • C,H,O(No ratio)

  • Phospholipid

  • Triglycerides

  • Steroids

Proteins

Structure of amino acids :

An R-Group is a side chain attached to the α-carbon of all amino acids. It decides the chemical versatility of the amino acid. For example, some R-Groups carry a charge, creating a polar molecule. Some R-groups are hydrophobic or hydrophillic.

Peptide Bond:

Protein Folding

Primary, Secondary, Tertiary, Quaternary Structure:

Denaturation happens when there is a change in pH and temperature. Denaturation is the unfolding or breaking up of a protein, modifying its standard three-dimensional structure.

Enzymatics

Substrate**:** a molecule that an enzyme reacts with.

Active Site**:** the part of an enzyme to which substrates bind.

Enzyme**:** proteins that help speed up metabolism.

Enyme-Substrate Complex**:** a temporary molecule formed when an enzyme comes into perfect contact with its substrate.

Nucleic Acids

Structure/Function

Building blocks

DNA vs. RNA

Base pairing

Organic Molecules

  • What is an organic molecule

  • Process that builds polymers- Dehydration synthesis

  • Process that breaks down monomers- Hydrolysis

Carbohydrates

  • C,H, O (in a 1:2:1 ratio)

  • Structure/Function: provides both energy and structure to many organisms

  • Monosaccharides (Glucose, Fructose, Galactose)

  • Disaccharides (Sucrose, Lactose, Maltose)

  • Polysaccharides (Starch, Cellulose, Glycogen)

Lipids

  • Made of: glycerol backbone, 2 fatty acid tails (hydrophobic), and a phosphate group (hydrophilic).

  • C,H,O(No ratio)

  • Phospholipid

  • Triglycerides

  • Steroids

Proteins

Structure of amino acids :

An R-Group is a side chain attached to the α-carbon of all amino acids. It decides the chemical versatility of the amino acid. For example, some R-Groups carry a charge, creating a polar molecule. Some R-groups are hydrophobic or hydrophillic.

Peptide Bond:

Protein Folding

Primary, Secondary, Tertiary, Quaternary Structure:

Denaturation happens when there is a change in pH and temperature. Denaturation is the unfolding or breaking up of a protein, modifying its standard three-dimensional structure.

Enzymatics

Substrate**:** a molecule that an enzyme reacts with.

Active Site**:** the part of an enzyme to which substrates bind.

Enzyme**:** proteins that help speed up metabolism.

Enyme-Substrate Complex**:** a temporary molecule formed when an enzyme comes into perfect contact with its substrate.

Nucleic Acids

Structure/Function

Building blocks

DNA vs. RNA

Base pairing