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What are proteins?
large biological molecules found in all living cells.
→ made of amino acids linked in long chains by peptide bonds.
What are amino acids linked by?
Peptide bonds.
→ this is a condensation reaction - same principle as ester bonds in lipids. Water is released each time.
Where are proteins produced in the cell?
At the ribosomes, during protein synthesis
→ the process: DNA → RNA → Protein
What elements do proteins contain?
Carbon
Hydrogen
Oxygen
Nitrogen
→ ALWAYS contain nitrogen (unlike lipids/carbohydrates)
Name 5 functions of proteins
Enzymes (spped up reactions)
structural support (muscles, hair)
transport (haemoglobin)
Signalling (hormones/ receptors)
Defence (aantibodies)
Primary structure of a protein?
exact sequence of amino acids in the polypeptide chain
→ sequence is determined by DNA code (even one wrong acid can change whole protein!)
Secondary structure of a protein?
local folding of the polypeptide cahin into regular shapes
→ e.g.: alpha-helix (spiral)
Tertiary structure of a protein?
overall 3D shape of shingle polypeptide chain
→ determined by interactions between side chains: hydrogen bonds, hydrophobic interactions,…
Quaternary structure of a protein?
Formed when two are more polypeptide chains combine
What is a base triplet? (codon)
sequence of 3 DNA/RNA bases that codes for one specific amino acid
→ e.g.: GGG → one specific amino acid. There are 20 essential amino acids.
What are the 4 DNA bases?
Guanine (G)
Cytosine (C)
Adenine (A)
Thymine (T)
What is an enzyme?
A biological catalyst - a protein that speeds up chemical reactions in cells
→ ALL enzymes are proteins, but NOT ALL proteins are enzymes!!
Name 4 specific proteins + functions
Haemoglobin (carries O2)
Collagen (bones/ arteries)
Keratin (skin/hair/nail)
Insulin (regulates blood sugar)
Difference between haemoglobin and myoglobin?
Both carry oxygen, BUT:
→ haemoglobin in red blood cells (carries O2 through body)
→ myoglobin stores O2 in muscle tissue
What bonds stabilise the tertiary structure?
Hydrogen bonds, ionic bonds, hydrophobic interactions, disulfide bridges