2.9 Proteins Flashcards

2.9 i) Know the basic structure of an amino acid. ii) Understand the formation of polypeptides and proteins. iii) Understand the significance of a protein’s primary structure in determining its three-dimensional structure and properties. iv) Know the molecular structure of a globular protein and a fibrous protein and understand how their structures relate to their functions (including haemoglobin and collagen). (22 cards)

1
Q

What are proteins?

A

polymers made of amino acids (the amino acids are monomers)

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2
Q

Proteins examples:

A
  • enzymes
  • hormones
  • antibodies
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3
Q

What is a dipeptide?

A

formed when two amino acids join together

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4
Q

What is a polypeptide?

A

formed when more than two amino acids join together

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5
Q

What is the basic structure of an amino acid?

A

H
|
.. NH2 - C - COOH
|
R
(ignore the dots - only for formatting)

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6
Q

Identify the chemical groups in an amino acid:

A

NH2 - amine
R - carbon-containing variable side group (different for each amino acid)
COOH - carboxyl group

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7
Q

How many amino acids are there?

A

20

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8
Q

What do you call the amino acids that animals have to obtain through their diet?

A

essential amino acids

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9
Q

How are polypeptide chains formed?

A
  • amino acids are joined by condensation reactions
  • the OH on the COOH and the H on the NH2 are lost to form water
  • the bond forms between C and N
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10
Q

What are the bonds between amino acids called?

A

peptide bonds

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11
Q

What is the primary structure of a protein?

A

the sequence of amino acids in the polypeptide chain

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12
Q

What is the secondary structure of a protein? How does it form?

A
  • hydrogen bonds form between amino acids in the polypeptide chain
  • this causes the polypeptide chain to either
  • coil into an alpha helix (like an extended spring)
  • or fold into a beta pleated sheet
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13
Q

What is the tertiary structure of a protein?

A
  • the polypeptide chain further bends and folds into a precise 3D structure
  • this is due to the bonds that form between amino acids in the polypeptide chain
  • the further bending and folding also depends on the polarity of the R groups: polar R groups face inwards (away from water) and non-polar R groups face outwards (towards water)
  • the bonds that form include:
    ionic bonds
    chemical bonds e.g. disulfide bonds
    more hydrogen bonds
  • for proteins made from a single polypeptide chain, their tertiary structure forms their final 3D structure
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14
Q

Describe the ionic and disulfide bonds that form at the tertiary structure of a protein:

A
  • ionic bonds: the electrostatic attraction between oppositely charged ions (some R groups ionise, and so ionic bonds can form)
  • disulfide bonds: covalent bonds that form between a sulfur atom on one cysteine (amino acid) and a sulfur atom on another cysteine
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15
Q

What is the quaternary structure of a protein?

A
  • some proteins are made of several different polypeptide chains held together by bonds
  • the quaternary structure forms when different polypeptide chains assemble together
  • e.g. haemoglobin, insulin, collagen
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16
Q

What are conjugated proteins?

A

proteins containing another chemical group called a prosthetic group (a group that is not part of an amino acid)
e.g. iron group in haemoglobin

17
Q

State the bonds that form at the different structural levels of proteins:

A
  • primary structure: peptide bonds
  • secondary structure: hydrogen bonds
  • tertiary structure:
    ionic bonds
    disulfide bonds (and other chemical bonds)
    hydrophobic and hydrophilic interactions
    hydrogen bonds
  • quaternary structure: all of the above
18
Q

What is the significance of a protein’s primary structure in determining its three-dimensional structure and properties?

A
  • the primary structure of a protein is the amino acid sequence in a polypeptide chain
  • this sequence determines what types of bonds will form
  • e.g. disulfide bonds will form if cysteines are present in the amino acid sequence
  • the types of bonds and where these bonds form will determine how the polypeptide chain folds
  • and so will determine its 3D structure/shape
  • the 3D structure of the protein then determines its properties and its function in the body
19
Q

What are globular proteins? What are their properties?

A
  • spherical, compact proteins made up of multiple polypeptide chains
  • they are soluble and so can be easily transported in fluids: this is because the hydrophilic parts of the chains face outwards and the hydrophobic parts of the chain face inwards
  • their 3D structures are crucial for binding to other substances
20
Q

What are examples of globular proteins? Explain how their 3D structures are important:

A
  • e.g. haemoglobin: a globular protein made of 4 polypeptide chains. its solubility means it can be easily transported in the blood. this is important because it is responsible for transporting oxygen. the iron-containing haem groups present bind to oxygen
  • e.g. enzymes: their 3D structures are crucial for catalysing reactions
21
Q

What are fibrous proteins? What are their properties?

A
  • proteins made of long, insoluble polypeptide chains that coil tightly to each other to form a rope like shape
  • the chains are held together by lots of bonds (e.g. disulfide and hydrogen bonds) - this makes them strong
  • cross links between chains add additional strength
  • often found in supportive tissue due to their strength
22
Q

What are examples of fibrous proteins? Explain how their 3D structures are important:

A
  • e.g. collagen: a strong, fibrous protein that forms connective tissue in animals. its 3D structure is important as it provides strength
  • e.g. keratin: found in hair, nails, and skin