Proteins Flashcards

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1
Q

What are proteins comprised of?

A

Proteins are comprised of long chains of recurring monomers called amino acids

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2
Q

What is the cause for amino acid diversity?

A

The R-group of amino acids is variable, causing 20 different natural variations within amino acids.

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3
Q

What are polypeptides?

A

Polypeptides are chains of amino acids that are made by linking together amino acids by condensation reactions

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4
Q

What are peptide bonds?

A

The bond formed between the amino group of one amino acid and the carboxyl group of the adjacent is a peptide bond.

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5
Q

What is the cause for polypeptide diversity?

A

Amino acids can be linked together in any sequence giving a huge range of possible polypeptides.

  • If we consider a polypeptide with 100 amino acids, the number of possible sequence is 20^100
  • However, only particular sequences are made in very large quantities because they have useful properties
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6
Q

What is the significance of genes in the formation of polypeptides?

A
  • The amino acid sequence of a polypeptide is coded for by a gene
  • The sequence of bases in the DNA of the gene determines the sequence of amino acids in the polypeptide
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7
Q

What is the primary structure of amino acids?

A

The linear sequence of amino acids. Formed through peptide bonds.

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8
Q

What is the secondary structure of amino acids?

A

The stable configuration of amino acid sequences. Caused by hydrogen bonds between O and H in the peptide bond.
Two types:
1. Alpha helicles (spiral in shape) - most common
2. Beta-pleated sheets (directionally-oriented)

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9
Q

What is the tertiary structure of amino acids?

A

The overall three-dimensional configuration of the protein. Will have bonds such as disulphide bonds, ionic interactions, polar associations.

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10
Q

What is the quaternary structure of amino acids?

A

The quaternary structure describes the way in which the different subunits are packed together to form the overall structure of the protein

Example:

  • Lysosome consists of 1 polypeptide
  • Integrin consists of 2 polypeptides
  • Collagen consists of 3 polypeptides
  • Haemoglobin consists of 4 Polypeptides
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11
Q

What are the 7 main functions of proteins (with examples)?

A
  1. Enzymes
    • Rubsico catalyses the reaction that fixes CO2 from
      the atmosphere
  2. Antibodies & Clotting Factor
    • Immunoglobulins are antibodies
    • Immune system produces a variety of
      immunoglobulins, each with a different binding site
    • Plasma proteins act as clotting factors
  3. Hormones
    • Insulin, Glucagon, LH, FSH
  4. Structural components
    • Collagen forms a mesh of fibres in skin and blood
      vessels to prevent tearing, and in bones to prevent
      fractures
    • Spider silk is used make webs; stronger than kevlar
      and steel (resisting breakage)
  5. Movement
    • Actin and myosin are involved in the contraction of
      muscles
  6. Transport
    • Hemoglobin is responsible for transporting oxygen
  7. Sensitivity
    • Rhodopsin is the membrane protein of rod cells
      that absorb light
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12
Q

What is the proteome?

A

A proteome is all of the proteins produced by a cell, a tissue, or an organism

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13
Q

What is the difference between genome and proteome?

A

The genome (all of the genes of an organism) of an organisms is fixed, while the proteome is variable. This is because the proteins made in an organism (even in a single cell) vary over time depending on the cell’s activity.

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14
Q

Why are proteomes unique?

A
  1. Differences in activity

2. Differences in the amino acid sequences (due to differences in genes)

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15
Q

What is denaturation?

A

Denaturation is a structural change in a protein that results in the loss of its biological properties, as the tertiary structure of a protein (the way it folds) determines its function

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16
Q

What are the 2 causes of denaturation?

A
  1. Heat
    • High levels of thermal energy break hydrogen
      bonds, causing the protein to unfold
    • Optimum temperature for human proteins is
      generally 37 degrees Celsius
  2. Extremes of pH
    • Changes the charges on the R group, breaking
      ionic bonds within the protein