Test 1 Flashcards

1
Q

Terminal alpha carbonyl group PKA

A

3.1

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2
Q

Aspartic acid pka

A

Pka 4.1

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3
Q

Glutamic acid pka

A

4.1

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4
Q

Histidine pka

A

6.0

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5
Q

Blood ph

A

7.4

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6
Q

Terminal alpha amino group pka

A

8.0

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7
Q

Cysteine pka

A

8.3

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8
Q

Tyrosine pka

A

10.9 (11)

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9
Q

Lysine Pka

A

10.8 (11)

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10
Q

Arginine pka

A

12.5 (13)

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11
Q

Aliphatic side chain characteristics

A

No hydrogen bonding
No protons dissociate
Hdryocarbon r chain
Relative non polar

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12
Q

What are the 5 aliphatic side chains?

A
Glycine
Alanine
Leucine
Isoleucine
Proline
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13
Q
Amino acid that is :
Non essential
Sweet
ONLY NON CHIRAL AMINO ACID
Hydrogen side chain 
Least polar
A

Glycine, Gly, G

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14
Q
Amino acid that is 
Non essential 
Synthesized from pyruvate
2nd most abundant in proteins
Methyl group side chain
A

ALAnine (ALA, A)

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15
Q
Amino acid:
More non polar
From VALerian plant
Helps you sleep
V side chain
A

VALine
V
Val

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16
Q

Amino acid that is most abundant in proteins
Stimulates muscle protein synthesis
Flavor enhance
Essential amino acid

A

Leucine
LEU
L

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17
Q

Amino acid in egg whites

Essential and antipsychotic

A

Isoleucine
Ile
I

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18
Q
Amino acid that is cyclic
Modified to hydroxyproline in collagen and cell wall
Most abundant protein in collagen
Often found in turns
Non essential
A

Proline (Pro, P

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19
Q

Which amino acids have an OH or S side chain?

A

Serine and Threonine-OH

Cysteine and Methionine-S in side chain

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20
Q

Amino acid that hydrogen bonds
Highly polar first obtained from silk
Non essential
Head group of pohsphotidyl serine

A

Serine
Ser
S

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21
Q

Amino acid that is highly polar
Treatment in multiple sclerosis and indigestion
Essential

A

Threonine
Thr
T

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22
Q

Amino acid that is common in hair
Non essential
Contains sulfhydryl group

A

Cysteine
Cys
C

23
Q

Essential Amino acid
Contains thyoether used in synthesis of cysteine
Start codon for translation
Brazil nuts & cereal grains

A

Methionine
Met
M

24
Q

2 Cysteines can undergo what kind of reaction in presence of strong oxidant to produce ___

A
Undergo oxidation (extra) Ron
To produce cystine
25
Q

Cystine is made from ___ and found in__.

What is rich in cystine?

A

Made from oxidation of 2 cysteine and is found in hair

Alpha keratin is rich in cystine

26
Q

What does a perm do?

A

Smells like sulfer=strong reducing agent
Breaks disulfide bonds
Unfolds alpha keratin and can’t be reshaped
Then strong oxidizing agent is added to reform disulfide bonds

27
Q

At physiological pH, S side chain is mostly?

A

S- however some is still S and can ionize (lose a proton)

28
Q

What are the Aromatic Amino acids

A

Phenylalanine
Tyrosine
Tryptophan

29
Q
Amino acids that is 
High in protein foods
Precursor for tyrosine
Essential 
More non polar
Important precursor for melanin, dopamine, Norepinephrine and epinephrine?
A

Phenylalanine
Phe
F

30
Q
What amino acid has 
PKA of 11 (majority in in OH form)
Polar due to OH
Participates in hydrogen bond
Non essential
A

Tyrosine (Tyr) Y

31
Q
Amino acid with 2 aromatic rings
Polar (NH group)
Hydrogen bond donor
Essential
Makes you sleepy
MELATONIN precursor
A

Tryptophan
Trp
W

32
Q

What are the Basic groups

A

Histidine
Lysine
Arginine

33
Q

What are the acidic groups (COOH)

A

Aspartic Acid

Glutamic Acid

34
Q

What are the Amides of the Acidic Amino acids

A

Asparagine

Glutamine

35
Q

Which Amino acids are phosphorylated
Have 2 negative charges
Have OH groups which accept phosphate group
Interact in electrostatic interactions

A

Serine
Threonine
Tyrosine

36
Q

Amino acid that is
An artificial sweetener
Non essential
Physiological ph =COO-

A
Aspartic Acid (ASP, D)
At physiological pH= ASPARTATE
37
Q

Non essential acidic amino acid
Neurotransmitter
Mostly COO- at physiological pH

A

Glutamic Acid
Glu
E
Glutamate at physiological pH

38
Q

First ever amino acid isolated
NH2 at end of carboxylic acid
Found in asparagus

A

Asparagine
ASN
N
Amide of acidic amino acid

39
Q

Amino acid that participates in
Metabolic processes converted into glucose as energy
Treats patients following abdominal surgery
Amines are “QUTE”

A

GLUTAMINE
GLN
Q
Amide of acidic amino acid

40
Q

Characteristics of Basic side chain groups?

A

Strongly polar because charged & have dissociatable proton
Charged=strongly polar
Normally found on exterior surface
Can be hydrated by surrounding environment

41
Q
Amino acid PKA~6.5
Dissociatable proton
Essential
Half NH+ and Half N (no charge)
Best biological buffer because flat part=small change in pH with high change in base added
Part of hemoglobin
A

Histidine
His
H

42
Q
Amino acid
PKA~10 
Strongly polar
Antibodies involved in inflammation
PH<
A

Lysine

43
Q
Essential amino acid
Wound healing and cell division
STRONGLY POLAR
NH2+=dissociatable proton
Pka ~12
A

Arginine
Arg
R

44
Q

What are the 4 amino acid modifications?

A

Hydroxylated
Acylated
Glycosylated
Phosphorylated

45
Q

Hydroxylated

A

More polar

Adds OH group

46
Q

Acylation

A

Fatty acids esterified to amino acids
Common (16,18, 20 carbons)
More non polar
Acylated=bond between fatty acid and something else

47
Q

Glycosylated

A

Adds sugar group

Increases polarity

48
Q

Phosphorylation

A

Adds phosphate group—>charge at physiological pH

Increases polarity

49
Q

Who is John Crow?

A

-Extending shelf life of platelets to freeze dry them for emergency use
Inject platelets with Trehalose or shrimp brine will extend shelf life
**TREHALOSE

50
Q

Linus Pauling and Robert Corey

A

Determined the repeating structure in proteins
Pauling=2 Nobel prizes
Determinedalpha helix and beta sheet

51
Q

Jane Richardson and Husband David are responsible for?

A

Ribbon diagrams and how proteins in primary structure fold similar to origami (begin flat like paper)

52
Q

Who discovered the 3D structure of Hemoglobin?

A

Max Perutz

53
Q

Who discovered 3D structure of myoglobin?

A

John Kendrew