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Proteins > Proteins And Amino Acids > Flashcards

Proteins And Amino Acids Flashcards

1
Q

What are amino acids?

A

Amino acids are nutritional elements needed by the body, forming basic structural units of peptides and proteins.

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2
Q

What functions do amino acids serve in the body?

A

They are involved in the synthesis of body protein, non-protein nitrogen-containing compounds, and provide 12 to 20% of total daily body energy needs.

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3
Q

How are amino acids synthesized?

A

Many amino acids are derived from the diet, while others are synthesized in the body through metabolic processes.

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4
Q

What is the chemical structure of amino acids?

A

Amino acids have an amino group and a carboxyl group, with their behavior changing based on pH levels.

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5
Q

What happens to amino acids at neutral pH?

A

At neutral pH, amino acids exist as zwitterions with zero net charge.

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6
Q

What is the charge of amino acids at low pH?

A

At low pH, amino acids have a net positive charge, with both amino and carboxyl groups protonated.

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7
Q

What is the charge of amino acids at high pH?

A

At high pH, amino acids have a net negative charge, with both amino and carboxyl groups deprotonated.

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8
Q

What is the significance of the R group in amino acids?

A

The R group confers high variability in structure and physical properties, influencing hydrophobicity and solubility.

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9
Q

What are the classifications of amino acids based on the carbon atom?

A

Amino acids can be classified as α-amino acids, β-amino acids, and γ-amino acids based on the position of the amino group.

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10
Q

What are proteinogenic amino acids?

A

Proteinogenic amino acids include essential and non-essential amino acids.

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11
Q

What are some examples of essential amino acids?

A

Essential amino acids include histidine, leucine, isoleucine, lysine, methionine, valine, phenylalanine, threonine, and tryptophan.

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12
Q

What are some examples of non-essential amino acids?

A

Non-essential amino acids include alanine, cysteine, glycine, proline, serine, tyrosine, aspartate/asparagine, and glutamate/glutamine.

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13
Q

What is the simplest amino acid?

A

Glycine is the simplest amino acid and acts as an inhibitory neurotransmitter.

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14
Q

What is the most abundant amino acid?

A

Glutamine is the most abundant amino acid, comprising 61% of skeletal muscle.

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15
Q

What are branched-chain amino acids (BCAA)?

A

Branched-chain amino acids include leucine, isoleucine, and valine, which are important for skeletal muscle.

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16
Q

What is the isoelectric point of an amino acid?

A

The isoelectric point (pI) is the pH at which an amino acid bears no net charge.

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17
Q

How is the genetic code related to amino acids?

A

The genetic code consists of codons that correspond to specific amino acids, defining how DNA is translated into proteins.

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18
Q

Who first described the concept of codons?

A

The concept of codons was first described by Francis Crick and his colleagues in 1961.

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19
Q

What did Nirenberg and Matthaei discover about the genetic code?

A

They showed that the RNA sequence UUU specifically coded for the amino acid phenylalanine.

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20
Q

What percentage of body mass do proteins constitute in an adult?

A

15% of body mass.

21
Q

What is the role of proteins as biological catalysts?

A

Proteins act as enzymes.

22
Q

What is the transport and storage function of proteins?

A

Haemoglobin is responsible for transport and storage.

23
Q

How do proteins contribute to defense in the body?

A

Proteins function as antibodies.

24
Q

What role do proteins play in regulation and homeostasis?

A

Proteins act as hormones.

25
Q

What are some structural components made of proteins?

A

Muscle (actin and myosin), hair, nails, and skin.

26
Q

What is the primary structure of proteins?

A

The sequence of amino acids on a peptide chain.

27
Q

What does the primary structure of proteins include?

A

It includes the determination of the number of amino acids in a peptide chain.

28
Q

How is the primary structure of proteins typically written?

A

From the amino end to the carboxyl end (N – C).

29
Q

What are the classifications of peptide bonds in a primary structure?

A

Peptides: fewer than 50 amino acids; Dipeptides: 2 amino acids; Tripeptides: 3 amino acids; Polypeptides: more than 10 amino acids; Proteins: more than 50 amino acids.

30
Q

What is the secondary structure of proteins?

A

Folding of the polypeptide chain into specific coiled structures held together by hydrogen bonds.

31
Q

What are the types of secondary structures in proteins?

A
  1. Alpha Helix 2. Beta pleated sheet 3. Loop or coiled conformation 4. Super secondary motif.
32
Q

What is the shape of an alpha helix?

A

A clockwise rodlike spiral shape.

33
Q

How is the alpha helix formed?

A

By intrachain hydrogen bonding between C=O group of each amino acid and NH2 group present 4 residues ahead.

34
Q

What are the properties of proteins with an alpha helix structure?

A

They have great strength and elasticity and can be easily stretched due to tight coiling.

35
Q

What characterizes a beta pleated sheet?

A

5 to 10 amino acids line up side by side, forming a structure that is fully expanded and inelastic.

36
Q

What is the loop or coil conformation in proteins?

A

Present mainly in globular proteins, connecting two alpha helices or beta sheets.

37
Q

What are super secondary motifs?

A

Structures formed when two beta pleated sheets are connected by an alpha helix.

38
Q

What does the tertiary structure of proteins refer to?

A

The overall conformation of a polypeptide.

39
Q

What is the shape of myoglobin when fully extended?

A

Its length is 20 times its width.

40
Q

What does the quaternary structure of proteins involve?

A

Proteins with more than one peptide chain subunit.

41
Q

What is an example of a protein with a quaternary structure?

A

Hemoglobin.

42
Q

What are globular proteins?

A

Spherical or oval-shaped proteins, subdivided into albumin and globulins.

43
Q

What are fibrous proteins?

A

Long threadlike fibers that are usually insoluble in water, constituting structural proteins.

44
Q

What are examples of fibrous proteins?

A

Collagen, elastin, keratin.

45
Q

How are proteins classified based on function?

A
  1. Structural proteins 2. Transport proteins 3. Regulatory proteins 4. Catalytic proteins 5. Contractile proteins 6. Protective proteins 7. Storage proteins.
46
Q

What are some clinical correlates related to proteins?

A

Nutrition, antioxidants, hormones and enzymes, genetic disorders, laboratory tests.

47
Q

What are disorders of protein misfolding called?

A

Proteopathies.

48
Q

What are some examples of diseases related to protein misfolding?

A

Creutzfeldt–Jakob disease, Alzheimer’s disease, Parkinson’s disease, amyloidosis, Gaucher’s disease.

Proteins (2 decks)

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