Carbon Linkage and Polymers Flashcards
What are two types of carbon linkage? +examples
- Linked in linear molecule (octane)
- Linked in a ring (glucose)
6 functional groups commonly attached to carbon
- Hydroxyl (Alcohols)
- Phosphates
- Sulfhydryl (Thiolds)
- Amino (amines)
- Carbonyl (aldehydes and Ketones)
- Carboxyl (carboxylic acids)
(SHAPCC)
How do compounds react to alcohols? (hydroxyl) Why? Is it an acid or a base?
Alcohols are highly polar so they make compounds more soluble.
Acts as a weak acid.
What is the advantage of biochemical unity?
We can obtain energy from eating and digesting other organisms
What are the two common chemicals reactions in metabolism? How do they work?
- Condensation: monomer in, water out; anabolic (requires energy) ex: DNA replication, protein synthesis, making of starch…
- Hydrolysis: water in, monomer out; catabolic (releases energy) - essentially the breaking down of a polymer into its constituent monomers. ex: digestion of food molecules for energy generation
What is at start and end of polypeptide chain?
Every polypeptide chain starts with an amino group and ends with a carboxyl group
How does protein folding happen?
- Protein folding happens when hydrogen bonds form between peptide chains (between H and O)
- Side chains aren’t involved
What are the two structures of protein from hydrogen bonding?
- Alpha helix
- B pleated sheet
3 characteristics of alpha helix
- Very stable
- H bond every 3.6 a.a.
- Side chains point out
3 characteristics of B-pleated sheet(what does it end with)
- Side chains point up and down (interact with environment)
- Ends in NH2
- Hydrogen bonds form within the plane of the sheet, generating a stable sheet.
How is proline a unique amino acid?
- Fits neither in alpha helix nor B pleated sheet
- There is not space in ring to hydrogen bond, and no rotation about the bonds in the ring
- Still used because not ALL proteins structures are a-helix or B-psheet
How do side-chain interactions determine what? What is an example?
- Tertiary structure
Folding of polypeptide
- hydrogen bond between two side chains,
- hydrophobic interactions
ex: perms break disulfide bondWhat is the coiled coil?
Two alpha-helices wrapped around each other.
- 2 hydrophobic amino acids at every 4th position
- Gives strength to tendons, hairs, and feathers,
- When both alphahelices are same polypeptide, it is tertiary structure
- When both a-helices are different polypeptide, it is quartenary
Primary structure __________ energy while
Secondary/Tertiary folding ______ energy meaning its occurs _______
Primary structure REQUIRES energy while
Secondary/Tertiary folding RELEASES energy meaning its occurs AUTOMATICALLY
Protein becomes functional once it is in what structure?
Quarternary structure
