Protein Structure Flashcards

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1
Q

What is the primary structure of a protein?

A

The primary structure is the order in whicht the amino acids have been synthesised together into the polypeptide. It determines all the higher levels of the proteins structure.

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2
Q

What is the secondary structure of a protein and what are the three main types?

A

This is stabalised by hydrogen bonding along the backbone of the polypeptide strand and the three main types are:

1) a-helix: A spiral shape with the R groups sticking outwards.
2) B-sheet: Parts of the chain run alongside eachother forming a crinkly sheet with the R groups sticking above and below. They are usually anti-parallel but can sometimes be parallel depending on the N and C termini.
3) Turns: This is where the chain folds back on itself.

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3
Q

Describe tertiary structure.

A

This is the final folded shape of the polypeptide and is produced by interactions of the R groups. They can be hydrophobic interactions (hydrophobic R groups are repelled by water and pushed to the inside of the protein), ionic bonds (between COO- and NH3+), van der waals interactions (LDF, permanent dipole to dipole, hydrogen bonding), or disulphide bridges (covalent bonds between sulfur containing R groups in the amino acid cysteine).

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4
Q

What are prosthetic groups?

A

Prosthetic groups are non-protein groups which are strongly bound to some proteins to give them added functions (e.g. haem groups in haemoglobin).

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5
Q

What is quaternary structure?

A

Most proteins which have several connected polypeptide subunits have quaternary structure. Proteins with a quaternary structure can show cooperativity between their polypeptides because changes to the shape of one subunit can affect the properties of the other subunits.

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