CHAPTER 8 - Protein functions and structure. Flashcards

1
Q

What are the 6 roles that proteins play in living cells?

A
  1. Enzymes
  2. Movement
  3. Transport
  4. Signalling
  5. Defense
  6. Structure
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What role do protiens play in enzymes?

A

Enzymes catalyze chemical reactions.

1) Enzymes can be secreted by cells (e.g. chief cells add pepsin into your stomach)
2) attached to a plasma membrane (e.g. lactase on your small intestine microvilli cells),
3) floating inside the cytosol (e.g. hexokinase for step 1 of glycolysis),
4) held within a lysosome (many digestive enzymes), etc.

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

What role do protiens play in Movement?

A

Movement: motor proteins use energy (e.g. from ATP) to produce movement
1) kinesin and dynein drag vesicles along microtubules in opposite directions
2) myosin produces muscle contraction by pulling along actin filaments

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

TRUE OR FALSE
a single missense mutation (single amino acid change) can make kinesin move vesicles in the wrong direction.

A

TRUE

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

What role do protiens play in Transport?

A

Transport: e.g. membrane channels & transport proteins/pumps for facilitated diffusion and active transport.

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

What role do protiens play in Signalling?

A

Signalling: e.g. between cells via direct contact or signalling molecules

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

What role do protiens play in Defence?

A

Defence:
- receptors and antibodies that recognize and bind to foreign molecules and cells to inactivate and/or destroy them as part of our body’s immune response.

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

What role do protiens play in Structure?

A

Structure:
- The microtubules (e.g. spindle fibres) & microfilaments of a cell’s internal cytoskeleton, the proteins in the complex extra-cellular matrix found outside the cell, and the membrane-bound proteins that these fibres are anchored to.

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

Describe at least one way in which carbohydrates, nucleic acids, and lipids are each necessary for making this cell recognition possible.

A

Carbohydrates:
-The red blood cell’s glycoproteins include oligosaccharides (polymers of a few sugars) that are important markers recognized by the WBC’s receptor protein. OR
-Glucose provides energy for synthesizing the receptor protein.

Nucleic acids:
-DNA holds the genetic info. Needed for synthesizing the receptor protein. OR
-mRNA must be translated to synthesize the receptor protein.

Lipids:
-The phospholipids bilayer of the rough ER is needed for these transmembrane proteins to fold correctly.
-Without phospholipids to make membranes, there would be no Golgi apparatus to join sugars and proteins to make a glycoprotein.

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

What are 3 components that Amino acids are comprised of.

A

-It has carbon in the middle, called ⍺ carbon.
-It has an Amine group (NH2) at its N-terminus end.
-It has a carboxyl group (COOH) at its C-terminus end.

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

What is the real name for Amino Acids?

A

⍺-amino carboxylic acid,

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

What makes each of the amino acids?

A

Different unique side chains or R groups which are attached to the side of the alpha carbon.

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

Do polypeptides have directionality?

A

Yes, they are always synthesized from the N-terminus to
the C-terminus (i.e. new amino acids are always added to the C-terminus)

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

During what does each amino acid get added to a growing polypeptide chain?

A

During translation, each amino acid is added to the growing polypeptide chain with a peptide bond (a covalent bond between amino acids), forming a repeating backbone of N-C-C-N-C-C-…, with the specific R groups sticking out the sides of the backbone.

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

What are the 4 types of amino acids?

A

1) NON-POLAR
2) POLAR
3) (+) CHARGE
4) (-) CHARGE

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

How many structures do protiens have?

A

4

17
Q

What is Primary structure?

A

Primary structure = the sequence of amino acids in a chain formed by covalent bonds
This sequence of amino acids eventually determines the final shape of the protein, since it determines how different parts of this chain will interact with each other
(via different bonds and interactions) and their external environments.

18
Q

What is Secondary structure?

A

Secondary structure = localized 3-D structures stabilized
by hydrogen bonds between the backbone atoms of the
polypeptide (e.g. alpha helices & pleated sheets)

19
Q

What is Tertiary structure?

A

Tertiary structure = Overall 3D structure of the entire protein (or polypeptide, if it’s part of a protein that is made up of multiple polypeptide subunits)
-Notice: You can find alpha helices and pleated sheets within this final tertiary shape.
-This structure is stabilized by many different bonds & interactions (e.g. H-bonds, disulphide bridges, ionic bonds, van der Waals interactions, etc.),
between side chains and backbone atoms.

20
Q

What is a Quaternary structure?

A

Quaternary structure = the precise interlocking of more than one polypeptide subunit to form the final, completed protein.
-Note: Proteins that consist of just one polypeptide do NOT have a quaternary structure
-The same variety of bonds stabilizes quaternary structure as tertiary structure.