amino acids and proteins Flashcards

1
Q

what are proteins

A
  • they are made up of carbon, hydrogen, nitrogen, oxygen and sometimes sulfur
  • they are the building blocks of life
  • there are millions of different proteins
  • they are the most abundant molecule in cells
  • they make up more than 50% of a cells dry mass
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2
Q

what do proteins do

A
  • enzymes
  • carrier proteins transport molecules across the membrane
  • antibodies defend against disease
  • structural proteins support cells and tissues
  • hormones transmit information
  • transport proteins carry oxygen
  • contractile proteins enable muscle contractions
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3
Q

explain amino acids

A
  • they have a central carbon atom
  • they include a carboxylic acid group, an amino acid group, a hydrogen and a variable r group
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4
Q

how do you join two amino acids

A
  • they are joined by a condensation reaction
  • the reaction involves the removal of a water molecule and the formation of a peptide bond
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5
Q

what is a polypeptide chain

A
  • a chain of amino acids can be build up
  • the sequence and number of amino acids in the chain is determined by the DNA
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6
Q

what are the 4 levels of protein structure

A
  • primary
  • secondary
  • tertiary
  • quaternary
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7
Q

what is the primary structure of a protein

A
  • the sequence of amino acids held together by peptide bonds
  • controlled by the DNA
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8
Q

what is the secondary structure of proteins

A
  • the folding of the polypeptide chain
  • it can coil into alpha helices
  • it can fold into beta pleated sheets
  • held together by peptide and hydrogen bonds
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9
Q

what is the tertiary structure of a protein

A
  • the further folding of the polypeptide chain to give a more complex 3d shape
  • hydrogen bonds between polar r groups
  • di-sulfide bonds between sulfur atoms in r groups
  • ionic bonds between oppositely charged r groups
  • hydrophobic and hydrophilic interactions between r groups
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10
Q

what is the quaternary structure of proteins

A
  • they are proteins that include more than one polypeptide chain
    eg - haemoglobin
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11
Q

explain denaturing of proteins

A
  • heating a protein increases the kinetic energy in the molecules
  • this leads to the atoms vibrating
  • causes the bonds holding the tertiary structure to break and reform which changes the shape of the active site in the protein
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12
Q

what are globular proteins

A
  • they are ball like structures
  • hydrophobic r groups turn inwards towards the center of the amino acid
  • more water soluble
  • tend to have a metabolic role in living organisms
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13
Q

what are fibrous proteins

A
  • they form long fibres
  • regular, repetitive sequence of amino acids
  • usually insoluble in water
  • tend to have structural roles in living organisms
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14
Q

give examples of globular proteins

A
  • enzymes
  • channel proteins
  • transport proteins
  • hormones
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15
Q

give examples of fibrous proteins

A
  • structural proteins
  • hair, skin, ligaments, tendons
  • collagen and keratin
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16
Q

what is the structure of haemoglobin

A
  • has a quaternary structure
  • 4 globin molecules held together by hydrogen bonds
  • it also has a haem group
  • compact
  • soluble in water
17
Q

explain the structure of collagen

A
  • three identical left handed helix polypeptide which form a triple helix
  • the third amino acid is glycine
  • chains held together by hydrogen bonds
  • very stable and insoluble in water
  • molecules cross link through covalent bonds which gives collagen great strength