Lecture 7: Proteins Flashcards

1
Q

what is a zwitterion

A

is a neutral ion with charged portions

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1
Q

What does the pKA tell you about the amino acid

A

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

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2
Q

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

A

PI isoelectric point

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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

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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

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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

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6
Q

What are the aromatic compounds

A

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

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7
Q

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

A

Phenylketonuria

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8
Q

Tyrosine is a precursor for ___________

A

catecholamine

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9
Q

Tryptophan is a _________________

A

serotonin

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10
Q

What are the sulfur containing amino acids

A

Methionine and cystine

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11
Q

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

A

Cystinuria

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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

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13
Q

What are the polar amino acids
*hydrophilic

A

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

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14
Q

What are the Charged amino acids

A

Negative:
Aspartate
glutamate

Positive
Arginine
Lysine
Histidine

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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

A

Arginine

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
Q

In terms of B sheet what determines if it is Parallel or antiparallel

A

the folding of the sheet

25
Q

If regular patterns are alpha helix and beta pleasted sheet, what are some non normal patterns

A

Bends loops turns

26
Q

What is tertiary structure

A

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
Q

G actin and B adregeric receptors are example of ________ structure

A

tertiary structure

28
Q

What is quaternary structure

A

the association of individual polypeptide chains subunits in a geometrically and stoichiometrically specific manner

Ex: hemoglobin, insulin, immunoglobulin

29
Q

____________ is the destruction of a proteins quaternary, tertiary, or secondary structure

A

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