Asparric Acid and Glumatic Acid

Question 1

the side chains are negatively charged at neutral pH

Answer 1

aspartic acid and glumatic acid

Question 2

The side of _____ and ____ are positively charged at or near neutral pH

Answer 2

lysine and arginine

Question 3

the side chain amino group is attached to an aliphatic hydrocarbon tail

Answer 3

Lysine

Question 4

the side-chain basic group, the guanidino group, is more complex in structure than the amino group, but it is also bonded to an aliphatic hydrocarbon tail .

Answer 4

Arginine

Question 5

free histidine, the pKa of the side-chain imidazole group is ___, which is not far from physiological pH.

Answer 5

6.0

Question 6

found in the protonated or unprotonated forms in proteins

Answer 6

Histidine

Question 7

properties of many proteins depend on whether individual histidine residues are ____ or not

Answer 7

changed

Question 8

charged amino acids are often found in the ____ site of enzymes.

Answer 8

active

Question 9

have aromatic rings in their side chains

Answer 9

Phenylalanine, tryptophan, and tyrosine

Question 10

Phenylalanine, tryptophan, and tyrosine

allow us to locate and measure proteins ➡️ _____________

Answer 10

the aromatic rings absorb strongly at 280 mn and can be detected using a spectrophotometer

Question 11

Phenylalanine, tryptophan, and tyrosine

Very important physiologically➡️ ______________

Answer 11

are both key precursors to neutrotransmitters

Question 12

tryptophan is converted to ______ (5-HT) - - has calming effect

Answer 12

serotonin

Question 13

very low level of serotonin= _______

Answer 13

associated with depression

Question 14

extremely high levels =__________

Answer 14

produce a manic state

Question 15

Manic-depressive schizophrenia (bipolar disorder) can be managed by controlling the levels of _______ and it’s further metabolites

Answer 15

serotonin

Question 16

derived from phenylalanine

Answer 16

Tyrosine

Question 17

converted to catecholamines

Answer 17

epinephrine (adrenaline)

Question 18

L-Dihydroxyphenylalanine (L-dopa)

Answer 18

is an intermediate in the conversion of tyrosine.

•lower than normal levels of L-dopa are involved in Parkinson’s disease.

Question 19

Tyrosine and phenylalanine

Answer 19

precursor to norepinephrine and epinephrine- stimulatory

Question 20

Epinephrine

Answer 20

“flight or fight” hormone

Question 21

It causes the release of glucose and other nutrients into the blood and stimulates brain function

Question 22

some effects:

Answer 22

•phe-headaches (aspartame)
• try- morning lift
• tyrp- sleep

Question 23

produced by modification of the parent amino acid after the protein is synthesized by the organism (post-translational modification)

example: hydroxyproline and hydroxylysine ➡️ found only in a few connective tissue proteins (collagen)

Answer 23

Uncommon aa

Question 24

differs from tyrosine ➡️ extra iodine-containing aromatic group on the side chain

Answer 24

Thyroxine

Question 25

Thyroxine is found only in the _____ gland

Answer 25

thyroid

Question 26

Thyroxine is formed by ______ modification of tyrosine residues-thyroglobulin

Answer 26

post-translational

Question 27

Thyroxine is released as a hormone by ________ of thyroglobulin

Answer 27

proteolysis