Lecture 3 Flashcards

1
Q

What are the amino acids?

A

basic building block of proteins

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2
Q

How many amino acids are there?

A

20 that make up all proteins

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3
Q

What is the R group bound to?

A

a-carbon

aka side chain

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4
Q

What is the Nitrogen tail of an amino acid?

A

the amino group

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5
Q

What is the COH end of an amino acid?

A

the carboxyl group

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6
Q

What are the classes of amino acids?

A

aliphatic
aromatic
sulfur containing
alcohols
bases
acids
amides

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7
Q

What are the four aliphatic amino acids?

A

alanine (A)
valine (V)
leucine (L)
isoleucine (I)

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8
Q

What are the two aliphatic/structural amino acids?

A

proline (P)
glycine (G)

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9
Q

What are the two aromatic amino acids?

A

tryptophan (W)
phenylalanine (F)

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10
Q

What is the aliphatic/sulfur-containing amino acids?

A

methionine (M)

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11
Q

What are the two carboxylic acid amino acids and what are their pKa’s?

A

aspartic acid (D) 4.1
glutamic acid (E) 4.1

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12
Q

What is the aromatic amino acid and what is its pKa?

A

tyrosine (Y) 10.9

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13
Q

What is the thiol/structural amino acid and what is its pKa?

A

cysteine (C) 8.3

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14
Q

What is the amine amino acid and what is its pKa?

A

lysine (K) 10.8

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15
Q

What is the guanidinium amino acid and what is its pKa?

A

arginine (R) 12.5

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16
Q

What is the imidazole amino acid and what is its pKa?

A

histidine (H) 6.0

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17
Q

What are the two alcohol amino acids?

A

serine (S)
threonine (T)

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18
Q

What are the two amide amino acids?

A

asparagine (N)
glutamine (Q)

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19
Q

What are the two transamination amino acids?

A

aspartic acid (D)
asparagine (N)

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20
Q

What are the hydrophobic amino acids?

A

A (alanine)
V (valine)
L (leucine)
I (isoleucine)
M (methionine)
W (tryptophan)
F (phenylalanine)
G (glycine)
P (proline)

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21
Q

What are the acidic amino acids?

A

E (glutamic acid)
D (aspartic acid)
C (cysteine)
Y (tyrosine)

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22
Q

What are the basic amino acids?

A

K (lysine)
R (arginine)
H (histidine)

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23
Q

What are the polar amino acids?

A

S (serine)
T (threonine)
N (asparagine)
Q (glutamine)
D (aspartic acid)

24
Q

What can form disulfide bonds?

A

Cysteine (CYS) (C)

25
Q

What does C, CYS, Cysteine do?

A

plays important functional and structural roles

26
Q

What is C, CYS, Cysteine important for in regards to function and structure?

A

-the catalytic function of many enzymes (the deprotonated -SH group is a good nucleophile)
-it can form disulfide bonds

SH groups must be close in space

27
Q

What is oxidation?

A

loss of e-

28
Q

What is reduction?

A

gain of e-

29
Q

What are reducing conditions in the cell due to?

A

due to Glutathione (GSH)

GSH is a tri-peptide (ECG) with a reducing thiol

30
Q

What can P,PRO, Proline do?

A

can assume both cis and trans conformations

31
Q

In proteins, are peptide bonds generally cis or trans? And what is the exception?

A

trans

proline if it is the aa following the bond

32
Q

What are the four properties of amino acids?

A

1) amino acids are chiral
2) amino acids prefer diff. solvent environments (hydropathy)
3) amino acids are charged
4) amino acids can be Ionized

33
Q

Natural amino acids have what configuration? And what is its enantiomer/mirror image?

A

L, alanine

D and L are enantiomers

34
Q

What is hydropathy?

A

the relative hydrophobicity of each amino acid

(measure of polarity)

35
Q

The amino group and/or carboxyl group will be charged depending on the what?

A

depending on the pH

36
Q

Can the R group be charged?

A

yes it could

37
Q

At neutral pH amino acids are predominantly what?

A

dipolar ions (zwitterions)

38
Q

How many chiral centers and stereoisomers does Isoleucine (ILE) have?

A

2 chiral centers
4 possible stereoisomers

39
Q

What does amino acid ionization state depend on?

A

depends on pH

40
Q

What are the ionizable groups in amino acids?

A

1) carboxyl group
2) amino group
3) some side chains

41
Q

What does each ionizable group have?

A

has a specific pKa

42
Q

For a solution pH BELOW the pKa, the _____ form (__) predominates.

For a solution pH ABOVE the pKa, the _____ (conjugate base) form (__) predominates?

A

For a solution pH BELOW the pKa, the PROTONATED form (AH) predominates.

For a solution pH ABOVE the pKa, the UNPROTONATED (conjugate base) form (A-) predominates?

43
Q

When is pKa the pH?

A

when concentrations of [AH] and [A-] are equal

44
Q

All amino acids have how many charged groups?

A

at least 2 charged groups

45
Q

What is the pKa of Cysteine?

46
Q

What is the pKa of Tyrosine?

47
Q

What is the pKa of Asparagine?

48
Q

What is the pKa of Glutamine?

49
Q

What is the pKa of Aspartic acid?

50
Q

What is the pKa of Glutamic acid?

51
Q

What is the pKa of Lysine?

52
Q

What is the pKa of Arginine?

53
Q

What is the pKa of Histidine?

54
Q

The ratio of unprotonated to protonated R-group changes by an order of magnitude with each what?

A

with each change in pH unit relative to the groups pKa

55
Q

Titration curves are used to determine what?

A

pKa values

56
Q

In a titration curve, what is pI (isoelectric point)?

A

the pH where the net charge is 0 (so in the middle between pK1 and pK 2)

2.4+9.9 / 2 = 6.15

57
Q

What is the net charge of the left side and then the right side? What is the pI of the two?

A

Left side: Net charge +1
Right side: Net charge 0

explanation=, look at all the + and - and cancel them out then see results

pI = 7.65
(6.0 +9.3)/2