Unit 3 Flashcards
Functional Groups
Group of atoms responsible for chemical characteristics.
- Alcohol (-ol)
- Ether
- Aldehyde
- Ketone
- Carboxylic Acid
- Ester
- Amine
4 Categories of Molecules
- Amino Acids (Proteins)
- Fatty Acids (Lipids)
- Carbohydrates and Alcohols
- Nucleic Acids (DNA/RNA)
DNA
Deoxyribonucleic acid
- Deoxyribose sugar
- Polymer of monomer nucleotides
- Pentose sugar
- Double Helix - ATCG
Stable/stays same/long lifespan
RNA
Ribonucleic acid
- Ribose sugar
- Pentose
- Polymer of monomer nucleotides
- Single strand - AUTG
Dynamic/changeable/short lifespan
Hydrophilic
Structures easily mix with H2O
Monomer
Single subunits or building blocks. Combine through covalent bonds to form polymers. (Dehydration synthesis)
Polymers
Monomers combined
Polypeptides
More than two/Small string of amino acids (polymers)
Dipeptide
Two aminos bonded
Peptidases/Proteases
Enzyme that breaks peptide bonds (hydrolysis)
Proteins
- Carry out cell functions
- Created by amino acid monomers
- 30-100 amino acids
- Synthesized in ribosomes
- Peptidases break down
Ribosome
Cell machine that synthesizes proteins
Dehydration synthesis
Reaction that puts monomers together while losing H2O.
Hydrolysis
Reaction that inserts H2O across the bond and breaks polymers back to monomers
Amino acids
- 2 C and a N form the backbone
- One amino group -NH2
- One carboxyl group -COOH
- 20 common types
- String together to form proteins
Protein structures
Shape is critical to function
- Primary
- Secondary
- Tertiary
- Quaternary
Enzymes
- Catalysts in bio chemical reactions
- Usually complex or conjugated proteins
- Specific for the substrate
- Breakdown, rearrangement, or synthesis reactions.
Hormones
- Chemical signaling molecules
- Usually small proteins or steroids
a-helix
- Secondary structure of protein
- shape together by hydrogen bonds
- spiral shape
B-pleated sheet
- Secondary structure of proteins
- Hydrogen bonds, hold the shape
- Directional arrow together in pleats
- Blunt end -NH2 / Arrow end -COOH
Tertiary structure
- Polypeptide 3 dimensional structure
- Created by interactions among the R- groups.
- Hydrophobic interactions, ionic bonding, hydrogen, bonding, and disulfide linkages.
Quaternary structure
- Several polypeptides or sub units interacting.
Hydrophobic
“Water fearing” or insoluble in water
Lipid characteristics
- Non-polar/Hydrophobic
- Fats, oils, waxes, phospholipids and steroids
- Covalent bonds w/equal sharing
Protein Motif
Commonly seen arrangements of proteins that serve a specific purpose
- Beta Barrel - Large Pore in Membrane
- Helix Turn Helix - binding DNA/turning genes on and off
Properties of Amino Acid R groups
- Negatively Charged (Acids)
- Positively Charged (Bases)
- Non Polar (Hydrophobic)
- Polar uncharged (Hydrophilic)
Amino Acid R group
-Negatively Charged
- Aspartate
- Glutamate (nerve signaling molecule)
Differ by 1 CH2 in the R group
Acids/Proton Donors
Amino Acid R Group
- Positively Charged
- Lysine
- Arginine
- Histidine
Proton acceptors/bases
Interact with -DNA molecules
Amino Acid R Group
- Non-polar
- 10 Amino acids that cannot form hydrogen bonds
- Prefer to be surrounded by lipids or each other
- Hydrophobic
Amino Acid R Group
- Polar Uncharged
- Forms Hydrogen Bonds
- Hydrophilic
- No charge “equal sharing”
- Disulfide bonds (cysteine)