Module 3: Proteins Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

Space filling diagram

A

Shows actual relative size and location of each atom, represents different atoms with different colours

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Ribbon diagram

A

Lines represent backbone of protein polymer
Broader line rep organized reiterated structure (alpha helix)
Thinner line rep less ordered loop

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Nucleus

A

Double membrane bound domain that contains chromosomes which pack and control DNA molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Ribosomes

A

Involved in synthesis of protein

Made in nucleolus

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Free ribosomes

A

Remain soluble in cytoplasm

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Bound ribosomes

A

Free ribosomes can attach to endoplasmic reticulum to become bound

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Amino acid

A

Central carbon bound to amino group, carboxyl group, hydrogen atom and variable side chain (R)
Side chain determines properties of protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Polypeptide

A

Strand of amino acids that covalently bound to one another through condensation reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Condensation

A

Polymerize amino acids releasing water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Hydrolysis

A

Break polymer apart by adding water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Primary structure

A

Sequence info

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Secondary structure

A

Alpha hélix -spiral by formation of hydrogen bonds

Beta pleated -made by parallel protein strands w HBs formed between carboxyl and amino group of adjacent strands

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Tertiary structure

A

3-D shape that determines function

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Quaternary structure

A

Association of different polypeptide subunits to form fully functional proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Molecular chaperones

A

Bind hydrophobic regions of nascent polypeptides and prevent incorrect folding

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Chaperonins

A

Large molecular complexes that form isolation chambers
Inside chamber, single nascent proteins sequestered away from other proteins so it can fold without interference and incorrect bonds

17
Q

Endomembrane system

A

Allows for cell to compartmentalize different areas to serve different functions

18
Q

Vesicles

A

Small membrane-bound compartments in cell that bud off ER

19
Q

Glycosylation

A

Occurs on most secreted and membrane-bound proteins

Help contribute to proteins stability, folding, cell to cell recognition

20
Q

Cytoskeleton

A

Dense network of fibres that maintains and change cell shape

21
Q

Microtubules

A

Protein polymers that form long fibres which stretch through cell
Cellular roadways that allow vesicles to be transported

22
Q

Kinesin and dynein (motor proteins)

A

Attached to transport vesicle and walk along microtubules using ATP

23
Q

Aquaporins

A

Embedded in plasma membrane and allow for movement of water across a membrane
Has hydrophobic exterior -allows for embedding in membrane-and hydrophilic core-Allows for passage of water

24
Q

Cystic fibrosis

A

Genetic disease which causes accumulation of mucus in organs specifically the accumulation of thickness mucus in the lungs