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BIOL1024 > Lecture 4 > Flashcards

Lecture 4 Flashcards

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1
Q

What are the main types of proteins?

A
  • Receptors and channels
  • Structural
  • Storage
  • Enzymes
  • Transport
  • Protection
  • Hormonal
  • Contractile
  • Catalyst
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2
Q

What are the levels of protein structure?

A
  • Primary
  • Secondary
  • Tertiary
  • Quaternary
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3
Q

What is the composition of amino acids?

A

Amino acids consist of an amine group, a carboxylic acid group, a variable R group, and a central (α) carbon.

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4
Q

Define fibrous proteins.

A

Fibrous proteins are insoluble and used structurally to give strength or make a protective layer.

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5
Q

Define globular proteins.

A

Globular proteins are soluble and usually offer dynamic functions, with their exact 3D shape critical for their function.

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6
Q

What is the zwitterionic form of amino acids?

A

In physiological solution (~pH 7.35), amino acids exhibit a zwitterionic form with both positive and negative charges.

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7
Q

What is the CORN rule in amino acids?

A

The CORN rule helps determine the chirality of amino acids by reading clockwise or anticlockwise from the α-carbon.

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8
Q

What are the simplest non-polar amino acids?

A
  • Alanine (A)
  • Glycine (G)
  • Methionine (M)
  • Cysteine (C)
  • Phenylalanine (F)
  • Tryptophan (W)
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9
Q

What are the characteristics of acidic polar R-groups?

A

Acidic polar R-groups include aspartic acid (D) and glutamic acid (E), which contain a carboxylate group that provides a negative charge.

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10
Q

What are the basic polar R-groups?

A
  • Lysine (K)
  • Arginine (R)
  • Histidine (H)
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11
Q

Fill in the blank: The bond formed between amino acids is called a _______.

A

[peptide bond]

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12
Q

What is the significance of the peptide bond?

A

The peptide bond is rigid and planar, restricting the conformations of polypeptides.

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13
Q

What are neurotransmitters derived from amino acids?

A
  • Glutamate (Glu, E)
  • Aspartate (Asp, D)
  • Glycine (Gly, G)
  • Tryptophan (Trp, W)
  • Tyrosine (Tyr, Y)
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14
Q

True or False: All amino acids can be synthesized in the human body.

A

False

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15
Q

What is selenomethionine?

A

Selenomethionine (SeMet) is a naturally occurring amino acid that can be incorporated into proteins in place of methionine.

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16
Q

What is the role of glutathione?

A

Glutathione is an important antioxidant made from cysteine, glycine, and glutamate.

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17
Q

What happens during a condensation reaction between amino acids?

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A

A condensation reaction joins the carboxyl group of one amino acid to the amino group of another, forming a peptide bond.

18
Q

Estimate the molecular mass of a protein with 400 amino acid residues.

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A

Approximately 44,000 Da (44 kDa)

19
Q

What is the unique feature of the peptide bond?

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A

The peptide bond has partial double bond character, making it rigid and planar.

20
Q

What are the unusual amino acids mentioned?

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A
  • Selenomethionine (SeMet)
  • Selenocysteine
  • Pyrrolysine (Ply or O)
21
Q

How do non-polar amino acids behave in an aqueous environment?

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A

Non-polar amino acids tend to cluster together to avoid water due to their inability to form hydrogen bonds.

22
Q

What are the functions of amino acids outside of protein synthesis?

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A

Some amino acids act as neurotransmitters or precursors for hormones and antioxidants.

23
Q

What amino acid is often used as a preservative in bread products?

24
Q

Fill in the blank: The sequence of amino acids in polypeptides is described from _______ to _______.

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A

[N-terminal, C-terminal]

25
What are the common methods to remember amino acid codes?
Mnemonics and flashcards are commonly used for memorizing amino acid codes.
26
What is a meteorite that fell known to contain?
Many organic compounds, including a novel amino acid similar to mammal neurotransmitters ## Footnote This highlights the potential for extraterrestrial sources of biological molecules.
27
What happens to venom from snakes and spiders if orally consumed?
It will be digested normally as they are only amino acids (protein) ## Footnote This indicates the nature of venom and its composition.
28
What is L-Cysteine commonly derived from?
Human hair, collected in hair salons ## Footnote This amino acid is used as a preservative in many bread products.
29
Does taking amino acids without exercising increase muscle?
No ## Footnote This emphasizes the importance of exercise in conjunction with amino acid intake for muscle growth.
30
What two amino acids are combined to produce aspartame?
Phenylalanine and aspartic acid ## Footnote Aspartame is a widely used low-calorie sweetener.
31
How much sweeter is aspartame compared to sucrose?
Roughly 200 times as sweet ## Footnote This makes it a popular choice for low-calorie soft drinks.
32
How many kinds of amino acids are used in protein synthesis?
20 kinds ## Footnote These amino acids play crucial roles in various biological processes.
33
Amino acids are precursors to what?
Other useful molecules ## Footnote This includes neurotransmitters, hormones, and other essential compounds.
34
What is the stereoisomer form of amino acids always used in proteins?
L-stereoisomer (except Glycine) ## Footnote This is important for the structural integrity of proteins.
35
How are amino acids classified?
According to their R-group ## Footnote This classification includes non-polar vs polar (acidic, basic, uncharged).
36
What do amino acids join together to form?
Polypeptide chains via peptide bonds ## Footnote Peptide bonds are crucial for protein structure.
37
What type of reaction is peptide bond formation?
A condensation reaction ## Footnote This process results in the release of a water molecule.
38
What is the primary structure of a protein?
The linear sequence of the protein, read from N– to C-terminal ## Footnote This sequence determines the protein's function.
39
What are the four levels of protein structure?
Primary, Secondary, Tertiary, Quaternary ## Footnote Each level represents a different aspect of protein structure.
40
What is the secondary structure of a protein?
Local folding patterns (e.g., alpha helices and beta sheets) ## Footnote This structure is stabilized by hydrogen bonds.
41
What is the tertiary structure of a protein?
The whole protein's 3D shape ## Footnote This is crucial for the protein's functionality.
42
What is the quaternary structure of a protein?
Different proteins interacting together ## Footnote This structure is significant in multi-subunit proteins.

BIOL1024 (3 decks)

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