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Proteins

Aspects of Biochemistry

QuestionAnswer
What is the monomer of all proteins? Amino acids
What is the bond which holds amino acids together in a polypeptide chain? Peptide/amide bonds
Name the 4 parts of a generalized amino acid structure. 1) Amine group 2) Carboxylic acid group 3) Residual group 4) Hydrogen All bonded to a central carbon atom.
What kind of reaction is the formation of a peptide bond? Condensation/dehydration.
What kind of reaction is the breakage of a peptide bond? Hydrolysis
Name the smallest and simplest amino acid, commonly found in collagen. Glycine
Name the amino acid which contains sulfur and is responsible for the formation of disulphide bridges. Cysteine
Which part of a protein determines its properties? The R groups present.
How do amino acids with polar R groups interact with water? They are hydrophilic, attracting water.
How do amino acids with non-polar R groups interact with water? They are hydrophobic, avoiding water.
How do ionised R groups interact with each other? They form ionic bonds.
How do two cysteine groups interact with each other? The S atoms present form disulphide bridges.
What happens if the sequence of amino acids in a polypeptide chain is changed/disrupted? The resulting protein structure will be different and will function differently or not at all.
Describe the primary structure/level of protein organization. Linear sequence of amino acids.
Describe the secondary structure/level of protein organization. Folding of chain into right handed helix (alpha helix) and pleated sheet (beta-pleated sheet). Hydrogen bonds stabilize the structure.
Describe the tertiary structure/level of protein organization. Further folding of chain into complex 3D shape Interactions present include: - disulphide bonds - ionic bonds - hydrophobic interactions - hydrogen bonding
Describe the quaternary structure/level of protein organization. Multiple polypeptide chains interacting with each other. Several bonding interactions present.
What is the N-terminus of a polypeptide? The amino group of the first amino acid in the polypeptide chain.
What is the C-terminus of a polypeptide? The carboxyl group of the last amino acid in the polypeptide chain.
Distinguish between globular and fibrous proteins. Globular eg. haemoglobin - soluble - complex folding - usually metabolically active Fibrous eg. collagen -insoluble - less complex shape - usually metabolically unreactive
Describe the structure of haemoglobin. - 4 polypeptide chains - 2 alpha globins, 2 beta globins - Each globin contains alpha helices. - Haem prosthetic group(Fe2+) at the centre of each globin
What is a prosthetic group in proteins? A part of a protein molecule that is not made of amino acids.
Any protein that has more than one polypeptide chain has this level of protein organization. Quaternary.
Describe the structure of collagen. - 3 polypeptide chains - left handed triple helix - every third amino acid is glycine - many hydrogen bonds present between helices -many covalent bonds between helix bundles forming network of fibres.
What is denaturation of a protein? A process in which proteins lose their shape function.
What can cause the denaturation of a protein? 1. Heat 2. Extremes in acidity or alkalinity 3. Alcohol 4. Heavy metals.
Which level of protein organization cannot be denatured? Primary structure. Denaturation reactions are not strong enough to break peptide bonds therefore the primary sequence of amino acids remains the same after a denaturation process.
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