1.5 Flashcards
(12 cards)
Proteins
3 points
- Most diverse
- amino acids are monomers of proteins that are folded into 3d shape
- Carries out vital functions
Amino Acids
4 points
20 diff types
8 essential ( must be acquired through diet)
12 non-essential (body can make its own)
differentiated by their r group
Building Protiens
5 points
carboxyl + amino group via dehydration synthesis
Forms peptide bonds
peptide - chains of amino acids
polypeptide - chain with more than 50 polypeptide
Protein is functional after its folding
Protein Structure:
Primary structure
2 points
- linear polypeptide chain
- chain in amino acid can alter/destroy the protein significantly
Secondary structure
4 points
coiling/folding of chains
occurs b/c of hydrogen bonds b/w amino acids
Beta-pleated sheet = zig-zag
Alpha Helix = spiral pattern
Tertiary Structure
4 points
R groups interest, causing 3d shape folding
intermolecular reactions determines shapes
critical for function of proteins and enzymes
Denaturation
Quantinary Structure
2 points
linking polypeptides together
Ex. hemogloblin is made of 4 polypeptides
Protein Prosthetic Group
4 points
PPG - Protein bind with non-proteins in order to function
Ex. O2 is bound to the hemegroups in polypeptides
4 heme group per hemoglobin = 4O2 molecules
Many enzymes reqiure prosthetic groups like metal ions to function
Nucleotides
4 points
Nucleotides are monomers that form nucleic acid
- Nitrogenous bases
- 5-Ring pentose sugar
- phosphate group
Purines
Pyrimidines
A and G
U and T and C
Building Nucleic Acids
3 point
DNA and RNA are joined via phsphodiester bonds
Base pairs are joined via hydrogen bonds
DNA is doubled stranded and runs anti-parallel
DNA and RNA
4 points
DNA:
- Stores herititdy informtion
- responsible for inherited traits
RNA:
- Involves in protein synthesis
- Heritity information for some viruses
