The flashcards below were created by user
adriana321
on FreezingBlue Flashcards.
-
Uses
growth, repair,support, movement, transport, immunity, and coordination
-
Examples
collagen, keratin, hemoglobin, antibodies, enzymes, hormones
-
-
Amino Acids
- monomers
- 20 total
- amine + carboxyl+ hydrogen + R(rest)
- ONLY thing that changes from one amino acid to the next is R
-
Linking Amino Acids
- condensation- links amino acids together
- peptide bondaa+aa= dipeptideaa x 36= polypeptide
- order determines shape, shape determines protein(function)
-
20 Amino Acids
- 8- essential to diet (body can't make)
- 12- non essential to diet (body can make)
-
Transamanation
body can rearrange to make certain amino acids
-
Structure
- random genetic mutations
- environmental conditions (pollutants)
-
Fibrous/Globular Proteins
- Fibrous- insoluble, long coiled (keratin,collagen,elastin)
- Globular- soluble, rounded structure, compact (hormones, antibodies,enzymes)
-
Enzymes
- proteins that act as biological catalysts; control rate of reaction
- weaken bonds/ lower the amount of activation energy
-
Globular
- active site: where they connect
- enzyme + substrate( whatever you are trying to build up/break down)
- arrangement determines what it can connect with "-ase"
-
Lock and Key Model
every enzyme has a matching substrate
-
Induced Fit Model
if enzyme and substrate are close enough, it will work
-
Catabolic Reaction
1 sub → 2 products
-
Anabolic Reaction
2 sub → 1 product
-
Denaturating Proteins
cannot work due to change in temperature; pH can unfold a protein
-
Remember
enzymes are very specific
-
Primary Structures
straight
-
Secondary Structures
helix (coil) or pleated sheet (fold)
-
Tertiary Structures
- Polypeptide= pleated + helix working together
- > 2/3 of either pleated or helix
-
Quaternary Structures
globular
|
|