Day 10, Lecture 1: Proteins I: Protein structure-Function Flashcards
1
Q
A
2
Q
Amino acids with special features?
A
- Glycine
- A hydrogen side chain
- small, thus no steric hindrance
- can pack tightly
- Disulfide link
- Crosslink two cysteine (C) groups to join polypeptides together
- Proline
- A secondary amine with a ring; kinks polypeptide chain
3
Q
A
4
Q
The formation of the amide or peptide bond occurs in the
A
ribosome
5
Q
The peptide bond can _____ with other peptide bonds and groups
A
Hydrogen bond
6
Q
In a polypeptide chain, the only rotation is around the _____. Due to
A
- Alpha-carbon
- due to steric hindrance and/or interactions between R-groups, only certain favorable angles are allowed between any two residues
7
Q
A
8
Q
A
9
Q
Isoforms/isozymes
A
proteins with distinct sequences that perform the same general function. Optimize performance for functions in other tissues or developmental stages
10
Q
all peptide bonds are ____ bonding in alpha helix and beta sheets
A
hydrogen bonding
11
Q
common amino residues in turns
A
- glycine, good since no side group
- proline, starts a kink for a tight turn
12
Q
Motifs
A
combinations of helix, sheet, etc structures
13
Q
Denaturing proteins using
A
- Heat
- pH changes
- Solvent change (turn protein hydrophobic core inside out)
- Toxic ligans (heavy metals can disrupt disulfide links)
14
Q
Osteogenesis imperfecta
A
- In some cases, results from a point mutation that changes glycine ot a bulky amino acid that impairs triple helix formation. Strong collagen fibers do not form resulting in “brittle bone disease)
15
Q
Conformational change of protein can result in change of function such as
A
- Control activity
- protein off or on depending on a phosphorylation event that changes tertiary structure
- Fine-tune function
- Accommodate several types of molecules
- enzyme can accept a substrate and release a product
- Convey information
- hormone in blood binds to a cell surface receptor that starts a signaling cascade in the cell cytoplasm