Structures and Functions of Proteins: Amino acids Flashcards
Proline
Why is it unique?
-Has a secondary amino acid group, side chain forms rigid ring structure
-INTERRUPT THE ALPHA-HELICAL STRUCTURE (breaks it)
(glycine can also do so)
Nonpolar amino acids
1) glycine
2) valine
3) alanine
4) Leucine
5) Isoleucine
6) Proline
7) Methionine
Aromatic (nonpolar):
1) Phenylalanine
2) Tryptophan
3) Tyrosine
Uncharged, Polar amino acids
1) Cysteine
2) Asparagine
3) Glutamine
4) Serine
5) Threonine
Positive Charge (Basic) amino acids
1) Arginine
2) Lysine
3) Histidine
Negative Charged amino acids
1) Aspartate
2) Glutamate
What amino acid synthesizes serotonin
Tryptophan
How are catecholamines synthesized
Catecholamines:
1) Dopamine
2) Norepinephrine
3) Epinephrine
Formed from TYROSINE
How are peptide hormones formed
-Cleavage from larger precursor protein
How can Alpha-helix be interrupted?
1) Electrostatic repulsion or attraction between amino acids
2) Steric hinderance
3) Bulky side chains
Quaternary Structure of Hemoglobin (Hb)
- Only in RBC
- Alpha beta dimers
- Hydrophobic interactions
- Weak ionic and hydrogen bonds
Functions of Hsp 70 and Hsp 60
Hsp 70
-Prevents premature folding of protein
Hsp 60
- Corrects folding of cellular proteins
- Refolds
- Needs ATP
Ubiquitin-Proteasome Complex
- Misfolded/defective proteins tagged by ubiquitin (Needs ATP)
- Degraded in ubiquitin-proteasome system
- Ubiquitin proteins degraded, ubiquitin recycled
- Proteasome unfolds and cuts the target protein into fragments
Prions Disease
- Nature of disease
- Transmission
- Usually founds in brain
- More B-sheets (PrPsc)