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Flashcards in Exam 1 Deck (42)
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1
Q

What is the only aa that has buffering properties

A

Histidine, sits at ph 6-7

2
Q

Tryptophan is a precursor to what molecule

A

Serotonin

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

4
Q

What is the primary excitatory neurotransmitter of the CNS

A

Glutamate

5
Q

What functions is glutamate a key player in

A

Pain sensation
Neuronal plasticity
Central sensitization

6
Q

What does the primary structure of a protein determine

A

Shape AND function

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.

8
Q

What number of aa corresponds with a polypeptide

A

10-20 aa

9
Q

What number of aa corresponds to proteins

A

> 20 aa

10
Q

What are the functional classes of proteins

A
Enzymes
Transport
Mechanical support
Contractile
Control and signaling
11
Q

What is the cause of sicke cell anemia

A

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

12
Q

What aa h-bond together in an alpha helix

A

1st and 5th

13
Q

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

A

3.6aa/ turn

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

15
Q

Where is beta sheeting often found

A

Inside the cell, and often pulls proteins together

16
Q

Which secondary structure makes up half of the globular proteins

A

Beta sheeting

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
Q

What is the weakest 3* interaction

A

Van der waals forces

26
Q

How does urea denature a protein

A

Out-competes for h bonding of protein structures at all levels

27
Q

How many bonds are needed for a biuret reaction to occur

A

At least 2 peptide bonds

28
Q

What does hydrolysis and proteases do to protein

A

Denatures by breaking peptide bonds

29
Q

How can you separate out individual proteins

A

Gel electrophoresis

30
Q

What molecule musts specifically be present for o2 to bind a Hb

A

Fe2+

Must be present in the heme group of Hb

31
Q

Why doesn’t met Hb bind O2

A

Because it contains Fe3+

32
Q

What is the better O2 carrier in the body

A

Mb because it only has one heme group to bond it’s able to deliver O2 faster ( creates a left shifted curve)

33
Q

How does CO2 affect the function of Hb

A

Lowers the affinity for O2 but does not directly bind the heme group. ( binds the nh3 end)

34
Q

How does CO affect O2 transport

A

Directly competes for the heme group and binds to fe2+

Able to displace o2 at low concentrations

35
Q

What is the Bohr effect

A

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
Q

What is the affect of BPG

A

Binds two subunits of Hb causing lowered affinity of o2 and a right shift on the graph

37
Q

What are the affects of fetal Hb

A

Does not bind BPG, so you get a left shifted graph

38
Q

What is HbA1c used for

A

Long term view of blood glucose levels

39
Q

What are the types of chains making up the shape of the antibodies

A

2 heavy chains

2 light chains

40
Q

What is the predominant structure of the antibody

A

Beta sheeting domains

41
Q

How is the antibody held together

A

Disulfide bridges

42
Q

Where are the binding sites for antigens located on the antibody

A

On the variable region at two identical sites