Exam 1 Flashcards

(42 cards)

1
Q

What is the only aa that has buffering properties

A

Histidine, sits at ph 6-7

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

Tryptophan is a precursor to what molecule

A

Serotonin

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

What molecule is a major player in tryptophan being able to cross the blood brain barrier

A

Insulin, generally from response to high carb diet

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

What is the primary excitatory neurotransmitter of the CNS

A

Glutamate

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

What functions is glutamate a key player in

A

Pain sensation
Neuronal plasticity
Central sensitization

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

What does the primary structure of a protein determine

A

Shape AND function

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

What is the importance of substance p

A

It is a neuropeptide that is co- released with glutamate to create a greater sense of pain and injury in the system.

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

What number of aa corresponds with a polypeptide

A

10-20 aa

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

What number of aa corresponds to proteins

A

> 20 aa

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

What are the functional classes of proteins

A
Enzymes
Transport
Mechanical support
Contractile
Control and signaling
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What is the cause of sicke cell anemia

A

A non conservative change of a Hb protein of glutamate, for valine

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

What aa h-bond together in an alpha helix

A

1st and 5th

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

What is average distance between turns when h-bonding occurs in an alpha helix

A

3.6aa/ turn

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

Why is the anti parallel nature of beta sheets stronger than a parallel structure

A

The h bonds are closer together in a anti parallel structure, while there is a slightly larger distance between the bonds in a parallel structure, thus making the bonds weaker

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

Where is beta sheeting often found

A

Inside the cell, and often pulls proteins together

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

Which secondary structure makes up half of the globular proteins

A

Beta sheeting

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What is the predominant aa in the collagen triple helix

A

Glycine- approx every 3rd aa in the chain

18
Q

What is the basic unit of collagen

A

Tropocollagen

19
Q

What is the basic structure of tropocollagen

A

3 separate peptide chains held together by interchain h bonds

20
Q

A polyproline strand will form what structure

A

A TRIPLE helix

21
Q

What factor is required for proper collagen formation

A

Vitamin c, lack of will lead to scurvy

22
Q

What causes cross linking in collagen

A

Losing residues
Larger amounts cause aging
Lack of cross linking causes stretchy skin

23
Q

What is the specific structure of protein due to

A

Hydrophobic bonding

Specific side chain interactions

24
Q

What is the strongest 3* structure interactions

A

Disulfide bridges

25
What is the weakest 3* interaction
Van der waals forces
26
How does urea denature a protein
Out-competes for h bonding of protein structures at all levels
27
How many bonds are needed for a biuret reaction to occur
At least 2 peptide bonds
28
What does hydrolysis and proteases do to protein
Denatures by breaking peptide bonds
29
How can you separate out individual proteins
Gel electrophoresis
30
What molecule musts specifically be present for o2 to bind a Hb
Fe2+ | Must be present in the heme group of Hb
31
Why doesn't met Hb bind O2
Because it contains Fe3+
32
What is the better O2 carrier in the body
Mb because it only has one heme group to bond it's able to deliver O2 faster ( creates a left shifted curve)
33
How does CO2 affect the function of Hb
Lowers the affinity for O2 but does not directly bind the heme group. ( binds the nh3 end)
34
How does CO affect O2 transport
Directly competes for the heme group and binds to fe2+ | Able to displace o2 at low concentrations
35
What is the Bohr effect
Higher h+ levels causes decree in o2 affinity for the heme group allowing more o2 to be released into the body. Important when metabolically active and body creates slight acidic environment
36
What is the affect of BPG
Binds two subunits of Hb causing lowered affinity of o2 and a right shift on the graph
37
What are the affects of fetal Hb
Does not bind BPG, so you get a left shifted graph
38
What is HbA1c used for
Long term view of blood glucose levels
39
What are the types of chains making up the shape of the antibodies
2 heavy chains | 2 light chains
40
What is the predominant structure of the antibody
Beta sheeting domains
41
How is the antibody held together
Disulfide bridges
42
Where are the binding sites for antigens located on the antibody
On the variable region at two identical sites