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[Midterm] BIOCHEM > AMINO ACIDS > Flashcards

AMINO ACIDS Flashcards

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1
Q

The following are the function of what?

  • It has a variety of roles in metabolism.
  • It is the building blocks of protein.
  • Forming parts of Coenzymes.
  • As Precursors for the biosynthesis of molecules such as Heme (blood).
A

Amino acids

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2
Q

________ pertains to protein.

These are organic compounds / molecules that combines together to form proteins.

A

Amino Acids

Note: Always keep in mind that amino acid is always related to protein.

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3
Q

Amino Acids forms as parts of COENZYMES

TRUE OR FALSE

A

TRUE

Note: When we lack an enzyme inside our body, amino acids acts as a substitute for the enzyme. However, it only plays a “part” of the function.

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4
Q

Anything that is lacking among the 20 amino acids can result to a ____________.

A

Medical condition

Note: We can’t get amino acids through food, there are some instances that it is normally produced by our body. If we have medical conditions, then our body cannot produce enough amino acid that can biosynthesize the molecule to produce normal amount of blood, normal color of the blood, and normal shape of the blood.

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5
Q

More than 300 different amino acids have been described in nature.

TRUE OR FALSE

A

TRUE

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6
Q

Only ___ are commonly found as constituents (essential) of Proteins.

A

20

Note: This is the STANDARD α - AMINO ACIDS. The other 280 are just the combination of these 20.

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7
Q

FAMILIARIZE ONLY!

What are the common Medical conditions caused by lacking of one of the essential amino acids?

A
  • Different types of anemia (Sickle cell anemia, aplastic anemia)
  • Edema (pamamanas)
  • Insomnia
  • Diarrhea
  • Depression
  • Lower blood sugar (hypoglycemia)
  • Loss of appetite
  • Fat deposition in the liver
  • Skin and hair related conditions (integumentary)
  • On and off headache
  • Body weakness
  • Irritability
  • Easy fatigue
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8
Q

__________ AMINO ACIDS:

  • Amino acid derivatives found in protein.
  • Non-protein amino acid

A. STANDARD
B. NONSTANDARD

A

B. NONSTANDARD

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9
Q

Why are amino acids uniquely suited to their role as the building blocks of proteins?

A

Amino Acids are fundamental building blocks of protein and it acts as a backbone of compounds such as being a neurotransmitter and hormones.

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10
Q

GENERAL STRUCTURE OF α - AMINO ACIDS

  • H₃N⁺
A

Amino group

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11
Q

GENERAL STRUCTURE OF α - AMINO ACIDS

  • COO⁻
A

Carboxyl Group

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12
Q

GENERAL STRUCTURE OF α - AMINO ACIDS

  • R

R group, R=”Reminder of the molecule”

A

Side chain

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13
Q

In all common amino acids, the α-carbon (alpha carbon) is bonded to four different groups, making it a chiral center.

“Which common amino acid is the only one that does not have a chiral α-carbon due to having two hydrogen atoms attached to it?”

A

Glycine

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14
Q

The α-carbon atom is a _________.

A

chiral center

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15
Q

It comes from a Greek word cheir, meaning “Hand”.

An object or a system that cannot be superimposed on its mirror image is called what?

A

Chiral

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16
Q

_______ objects are nonsuperimposable on their mirror images.

This “handedness” means that they have a distinct left- and right-handed version, known as enantiomers in chemistry.

A. Chiral
B. Nonchiral

A

A. Chiral

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17
Q

_________ objects are superimposable on their mirror images.

They do not have “handedness,” so their mirror image is identical to the original.

A. Chiral
B. Nonchiral

A

B. Nonchiral

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18
Q

If a molecule has an atom bonded to ____ different groups, it can be chiral.

A

Four

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19
Q

A chiral molecule, has left and right-handed isomers called ______.

A

Enantiomers

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20
Q

The Two Enantiomers of each amino acid are designated by what system according to the D - and L - Glyceraldehyde.

A

D,L System

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21
Q

“D” molecule rotates plane-polarized light clockwise or to the right.

What does D means?

A

Dextrorotation

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22
Q

“L” molecule rotates plane-polarized light counterclockwise or to the left.

What does L means?

A

Levorotation

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23
Q

Only the L-amino acids have been found in proteins.

TRUE OR FALSE

A

TRUE

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24
Q

___-isomers have been found only in small peptides of bacteria cell walls or in some peptide antibiotics.

A. D
B. L

A

A. D

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25
All the Amino Acids (AAs) were given a **trivial (common) name**. * Glutamate from _______.
Wheat Gluten
26
All the Amino Acids (AAs) were given a **trivial (common) name**. * Tyrosine from ______.
Cheese ("Tyros" in Greek)
27
Each AA is given how many letter abbreviation and symbol? Note: There are two answers.
* **Three (3)** Letter Abbreviation * **One (1)** Letter Symbol
28
Amino Acids often have the First 3 Letter and the the First Letter. When there is a confusion, _______ is used. A. a standard B. an alternative
B. an alternative
29
What are the **20 Common Amino Acid**?
* Alanine * Arginine * Asparagine * Aspartic Acid * Cysteine * Glutamic acid * Glutamine * Glycine * Histidine * Isoleucine * Leucine * Lysine * Methionine * Phenylalanine * Proline * Serine * Threonine * Trytophan * Tyrosine * Valine
30
Three-Letter Abbreviation of Alanine
Ala
31
Three-Letter Abbreviation of Arginine
Arg
32
Three-Letter Abbreviation of Asparagine
Asn
33
Three-Letter Abbreviation of Aspartic Acid
Asp
34
Three-Letter Abbreviation of Cysteine
Cys
35
Three-Letter Abbreviation of Glutamic Acid
Glu
36
Three-Letter Abbreviation of Glutamine
Gln
37
Three-Letter Abbreviation of Glycine
Gly
38
Three-Letter Abbreviation of Histidine
His
39
Three-Letter Abbreviation of Isoleucine
Ile
40
Three-Letter Abbreviation of Leucine
Leu
41
Three-Letter Abbreviation of Lysine
Lys
42
Three-Letter Abbreviation of Methionine
Met
43
Three-Letter Abbreviation of Phenylalanine
Phe
44
Three-Letter Abbreviation of Proline
Pro
45
Three-Letter Abbreviation of Serine
Ser
46
Three-Letter Abbreviation of Threonine
Thr
47
Three-Letter Abbreviation of Tryptophan
Trp
48
Three-Letter Abbreviation of Tyrosine
Tyr
49
Three-Letter Abbreviation of Valine
Val
50
One-Letter Abbreviation of Alanine
A
51
One-Letter Abbreviation of Arginine
R
52
One-Letter Abbreviation of Asparagine
N
53
One-Letter Abbreviation of Aspartic Acid
D
54
One-Letter Abbreviation of Cysteine
C
55
One-Letter Abbreviation of Glutamic Acid
E
56
One-Letter Abbreviation of Glutamine
Q
57
One-Letter Abbreviation of Glycine
G
58
One-Letter Abbreviation of Histidine
H
59
One-Letter Abbreviation of Isoleucine
I
60
One-Letter Abbreviation of Leucine
L
61
One-Letter Abbreviation of Lysine
K
62
One-Letter Abbreviation of Methionine
M
63
One-Letter Abbreviation of Phenylalanine
F
64
One-Letter Abbreviation of Proline
P
65
One-Letter Abbreviation of Serine
S
66
One-Letter Abbreviation of Threonine
T
67
One-Letter Abbreviation of Tryptophan
W
68
One-Letter Abbreviation of Tyrosine
Y
69
One-Letter Abbreviation of Valine
V
70
What are the (5) Classification of Amino Acids based on **Polarity**?
* Nonpolar, Aliphatic Amino Acids * Polar, Uncharged Amino Acids * Aromatic Amino Acids * Acidic Amino Acids * Basic Amino Acids
71
What are (7) Nonpolar, Aliphatic amino acids?
* **G**lycine (Gly) * **A**lanine (Ala) * **P**roline (Pro) * **V**aline (Val) * **L**eucine (Leu) * **I**soleucine (Ile) * **M**ethionine (Met) *REMEMBER THE ACRONYM **GAP-V-LIM***
72
What amino acid is this? * R group: Hydrogen * Symmetric, not chiral
Glycine (Gly)
73
What amino acid is this? * Imino acid * Five-membered ring structure, rigid in conformation
Proline (Pro)
74
What amino acid is this? * Hydrocarbon R groups, often involved in hydrophobic interactions for stabilizing protein structure.
* Alanine (Ala) * Valine (Val) * Leucine (Leu) * Isoleucine (Ile)
75
What are (5) Polar, Uncharged amino acids?
* Serine (Ser) * Threonine (Thr) * Cysteine (Cys) * Asparagine (Asn) * Glutamine (Gln)
76
What are the (3) Functional groups, **R group that is Hydrophilic**?
* Hydroxyl groups * Sulfur atoms * Amide groups
77
-SH group of two Cys in proteins can be oxidized to form a _________.
Covalent disulfide bond
78
It play a special role in the structures of many proteins by forming covalent links.
Disulfide bonds
79
What are the (3) Aromatic Amino Acids?
* Phenylalanine (Phe) * Tyrosine (Tyr) * Tryptophan (Trp)
80
Phenelalanine (Phe) and Tyrosine (Tyr) has a six-membered carbon ring with alternating double bonds, which creates a conjugated system. What do you call this ring?
Benzene rings
81
Tryptophan is consists of a benzene ring fused to a five-membered nitrogen-containing pyrrole ring. What do you call this ring?
Indole ring
82
The _____ group in tyrosine (Tyr) is an important functional group in proteins because it can form hydrogen bonds, participate in phosphorylation, and stabilize local structure
-OH
83
The aromatic amino acids tyrosine (Tyr) and tryptophan (Trp), with a minor contribution from phenylalanine (Phe) are jointly responsible for the light absorption of proteins at _________.
280 nm
84
Proteins in solution absorb UV light with absorbance _______ at 280 nanometer (nm). A. minimum B. maximum
B. maximum
85
You can measure protein content by what?
Photo spectrometry
86
What are the (2) Acidic Amino Acids? Acidic is negatively charged
Aspartate (Asp) and Glutamate (Glu)
87
Aspartate (Asp) and Glutamate (Glu) have ____ in their R Groups.
Carboxyl
88
What are the (3) Basic Amino Acids? Basic is positively charged
* Lysine (Lys) * Arginine (Arg) * Histidine (His)
89
What are the 3 Functional Groups Contributing to Positive Charge in R Groups?
* **Amino** - Lysine * **Guanidino** - Arginine * **Imidazole** - Histidine
90
Some amino acids have positively charged R groups at a physiological pH of _____.
7.0
91
All 20 common amino acids found in proteins are A. α-amino acids B. β-amino acids
A. α-amino acids
92
In **19 of the 20 common amino acids**, the **α-amino group** is primary, meaning it consists of a nitrogen atom bonded to two hydrogen atoms (-NH₂) attached to the α-carbon. TRUE OR FALSE
**TRUE** **Proline** is unique among these amino acids because it has a **secondary amino group (often called an imino group).**
93
Out of 20 amino acids, The α-carbon for 19 of them are asymmetric or chiral. What is the amino acid where the α-carbon is not chiral?
Glycine
94
Many additional nonstandard amino acids are found in cells and in proteins. TRUE OR FALSE
**FALSE** Note: Nonstandard amino acids are found in cells, but not in proteins
95
IN NONSTANDARD AMINO ACIDS Amino acid derivatives found in proteins * 4 - Hydrocyproline and 5 - hydroxylamine in ______. A. collagen B. myosin
A. collagen
96
IN NONSTANDARD AMINO ACIDS Amino acid derivatives found in proteins * 6-*N*-Methyllysine in _____. A. collagen B. myosin
B. myosin
97
What are the 2 amino acids that play key roles as **intermediates in amino acid metabolism**, specifically in the urea cycle?
Ornithine and citrulline
98
It cannot be synthesized by the humans, must be supplied in the diet. Examples: * Phenylalanine (Phe) * Valine (Val) * Threonine (Thr) * Tryptophan (Trp) * Isoleucine (Ile) * Methionine (Met) * Leucine (Leu) * Lysine (Lys)
Essential Amino Acids
99
Essential Amino Acids is also called as
Indispensable Amino Acids
100
It is required by infants and growing children. Examples: * Histidine (His) * Arginine (Arg)
Semi-Essential Amino Acids
101
ACID / BASE PROPERTIES OF AMINO ACIDS (AAS) * Amino Acid has both of this group. What are these?
**Basic Amine Group** and **Acidic Carboxylic Acid Group**
102
ACID / BASE PROPERTIES OF AMINO ACIDS (AAS) * In Neutral solution (pH 7.0), the amino acid contains a **negative charge** and a **positive charge**. It is called a?
**Zwitterion** (German for **"Hybrid Ion"**)
103
Amino Acids (AAs) ionize to various states depending on _____.
**pH values** Note: Amino acids (AAs) can exist in different ionization states depending on the pH of the surrounding environment. This is because they contain functional groups, like the amino group (–NH 3 + 3 + ​ ) and carboxyl group (–COO – –), which can gain or lose protons (H + + ) depending on the pH.
104
It is the specific pH at which the amino acid has no net charge. At this pH, the positive and negative charges on the molecule balance each other out. AA has equal positive and negative charge (no net electric charge).
The **isoelectric point** or **pI**
105
Low pH (Acidic Environment) * **pH < pI** Charge: + * **A+**
Cation
106
Isoelectric Point (pI) * **pH = pI** Charge: 0 (neutral) * **A⁰**
Zwitterion
107
High pH (Basic Environment) * **pH > pI** Charge: – * **A⁻**
Anion
108
The special name given to the amide bond between the carboxyl group of one amino acid and the -amino group of another.
Peptide bond
109
These are chains of amino acids linked together by peptide bonds.
Polypeptides
110
CHARACTERISTICS OF THE PEPTIDE BOND * The peptide bond have partial ______ bond feature. A. Single B. Double
B. Double
111
CHARACTERISTICS OF THE PEPTIDE BOND * The C–N bond in the peptide bond has a bond length of approximately _________ A. 0.142 nm B. 0.132 nm
**B. 0.132 nm** Note: This length is intermediate between: * A typical C–N single bond (0.149 nm), which is longer. * A typical C=N double bond (0.127 nm), which is shorter.
112
CHARACTERISTICS OF THE PEPTIDE BOND * Rigid and unable to rotate freely. TRUE OR FALSE
TRUE
113
CHARACTERISTICS OF THE PEPTIDE BOND * The peptide bond is non-planar, in cis-configuration, and charged. TRUE OR FALSE
**FALSE** The peptide bond is planar, trans-configuration and uncharged.
114
In Peptide _______: the six atoms attached to the peptide bond are coplanar. A. line B. plane
B. plane
115
CHARACTERISTICS OF THE PEPTIDE BOND * The carbonyl oxygen and the amide hydrogen are in ____ positions.
trans
116
The peptide chain is ______. A. directional B. non-directional
A. directional
117
The end having a free a-amino group.
**Amino-terminal** or **N-terminal**
118
The end having a free a-carboxyl group.
**Carboxyl-terminal** or **C-terminal**
119
By convention, the N-terminal is taken as the ____ of the peptide chain, and put at the left (C-terminal at the right). A. beginning B. end
A. beginning Note: * In a written peptide sequence, the N-terminal is always placed at the left and the C-terminal at the right. * This convention reflects the directionality of the peptide chain, similar to reading from left to right.
120
________ can be classified according to how many amino acids they contain. Examples: Dipeptide. Tripeptide, Oligopeptide, Polypeptide
Peptides
121
POLYMERS OF AMINO ACIDS * 2 amino acid residues
Dipeptide
122
POLYMERS OF AMINO ACIDS * 3 residues, and so on.
Tripeptide
123
POLYMERS OF AMINO ACIDS * 12 - 20 residues.
Oligopeptide
124
POLYMERS OF AMINO ACIDS * Many residues.
Polypeptide
125
It is a **biologically important peptide** that plays a vital role in various biological processes, particularly in maintaining cellular health and preventing damage from oxidative stress.
Glutathione (GSH)
126
Glutathione is a tripeptide, meaning it is composed of three amino acids. What are these?
* Glutamic acid * Cysteine * Glycine The sequence of these amino acids is: Glutamic acid – Cysteine – Glycine
127
In function of Glutathione (GSH), It is important in biological ________ reactions, has reduced an oxidized form.
oxidation-reduction
128
It is the most important molecule you need to stay healthy and prevent disease.
Glutathione (GSH)
129
What amino acid can be found in milk? This is an essential amino acid. However, it is not allowed because of some medical conditions.
**Phenylalanine**

[Midterm] BIOCHEM (3 decks)

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