Lecture 7: Proteins Flashcards

1
Q

what is a zwitterion

A

is a neutral ion with charged portions

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

What does the pKA tell you about the amino acid

A

pKa= -log (Ka) characteristic of the strength of an acids

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

___________ The Ph at which the overall net charge of the molecule is 0

A

PI isoelectric point

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

What are the Non polar amino acids

A

A Giraffe Licks Icy Puddles, Vigorously”

-Alanine A
-Glycine G
-Leucine L
-Isolucine I
-Proline P
-Valine V

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

In myoglobin the polypeptide sequence ala-leu-val is most likely in which part of the molecule?

A

The inside because it is non polar

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

___________________:
‣ Defective breakdown of BCAA
‣ Distinctive sweet odor of urine
‣ Toxic build-up of BCAA and
respective metabolites
‣ Neurotoxicity if not treated
‣ Treatment - special diet

A

Maple syrup urine disease

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

What are the aromatic compounds

A

Phenylalanine (non polar)
Tyrosine (polar)
Tryophan (polar)

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

____________ is caused by a build up of phenylalanine in the body

A

Phenylketonuria

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

Tyrosine is a precursor for ___________

A

catecholamine

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

Tryptophan is a _________________

A

serotonin

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

What are the sulfur containing amino acids

A

Methionine and cystine

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

_______________ is a disorder of the proximal tubule reabsorption of the fuiltereced cystine and dibasic amino acids (ornithine, arginine, lysine)

A

Cystinuria

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

What does cystunuria

A

The inability to reabsorb cystine leads to accumulation and subsequent precipitation of stone of cystine in the urinary tract

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

What are the polar amino acids
*hydrophilic

A

Serine (S)
Threonine (T)
Asparagine (N)
Glutamine (Q)

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

What are the Charged amino acids

A

Negative:
Aspartate
glutamate

Positive
Arginine
Lysine
Histidine

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

What are the properties of charged amino acids

A

Basic or acidic
‣ Highly hydrophilic
‣ Participate in ionic interactions
‣ More complicated titration curve

16
Q

What amino acids can be synthesized in a biochemical pathway in humans

A

Leucine and Lysine

17
Q

What amino acids are not essential in normal conditions but can become so to meet demands

A

Tyrosine
Isoleucine
Phenyulalnine
Tryptophan

18
Q

What amino acid is essential in trauma patients

A

glutamine and arginine

19
Q

What amino acid is essential during childhood growth

20
Q

What are the 9 essential amino acids

A

“Pretty Vagina takes turns in Make Happy Lovers Laugh”
Phenylalanine
Valine
Threonine
Tryptophan
Isoleucine
Methionine
Histidine
Leucine
Lysine

21
Q

What is primary structure

A

The unique sequence of amino acids arrange to form a polypeptide

22
Q

__________ patients with a mutation in the hemoglobin polypeptide chain results in the substitute of glutamic acid for valine

A

sickle cell disease

23
Q

What is secondary structure

A

Alpha helix or beta sheet

Maintained by hydrogen bonds formed between carboxyl oxygen and amine hydrogen in polypeptide backbone

24
In terms of B sheet what determines if it is Parallel or antiparallel
the folding of the sheet
25
If regular patterns are alpha helix and beta pleasted sheet, what are some non normal patterns
Bends loops turns
26
What is tertiary structure
The pattern of secondary structure elements folding into unique #D conformations. Maintained by the interaction of side chains EX: disulfide bridges and ionic interactions
27
G actin and B adregeric receptors are example of ________ structure
tertiary structure
28
What is quaternary structure
the association of individual polypeptide chains subunits in a geometrically and stoichiometrically specific manner Ex: hemoglobin, insulin, immunoglobulin
29
____________ is the destruction of a proteins quaternary, tertiary, or secondary structure
protein denaturation ✓ Nonenzymatic modifications: ‣glycosylation ‣oxydation ‣nitrosylation etc. ✓ High temperature: ‣fever above 40 C is a medical emergency ✓ Very low or very high pH: ‣stomach juice - pH 4.5 ‣metabolic conditions - lactic acidosis, ketoacidois, alkalosis etc