Structure of Proteins (AQA AS Biology)

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Blood
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#1
Report Thread starter 7 years ago
#1
I'm currently writing up my revision notes and I'm trying to simplify everything so that I can remember it.

I currently have:

Primary structure - sequence of amino acids in a polypeptide chain

Secondary structure - hydrogen bonds form between the amino acids causing the polypeptide chain to coil into an alpha helix or fold into a beta pleated sheet.

However, I have no idea on how to simplify the tertiary and quaternary structure - could anyone help?
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beyknowles
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#2
Report 7 years ago
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(Original post by Blood)
I'm currently writing up my revision notes and I'm trying to simplify everything so that I can remember it.

I currently have:

Primary structure - sequence of amino acids in a polypeptide chain

Secondary structure - hydrogen bonds form between the amino acids causing the polypeptide chain to coil into an alpha helix or fold into a beta pleated sheet.

However, I have no idea on how to simplify the tertiary and quaternary structure - could anyone help?
It might help to summarise from this:

The tertiary structure is the final specific geometric shape that a protein assumes. This final shape is determined by a variety of bonding interactions between the "side chains" on the amino acids. These bonding interactions may be stronger than the hydrogen bonds between amide groups holding the helical structure. As a result, bonding interactions between "side chains" may cause a number of folds, bends, and loops in the protein chain. Different fragments of the same chain may become bonded together.
There are four types of bonding interactions between "side chains" including: hydrogen bonding, salt bridges, disulfide bonds, and non-polar hydrophobic interactions.

( http://www.elmhurst.edu/~chm/vchembo...rtprotein.html )
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Blood
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#3
Report Thread starter 7 years ago
#3
(Original post by beyknowles)
It might help to summarise from this:

The tertiary structure is the final specific geometric shape that a protein assumes. This final shape is determined by a variety of bonding interactions between the "side chains" on the amino acids. These bonding interactions may be stronger than the hydrogen bonds between amide groups holding the helical structure. As a result, bonding interactions between "side chains" may cause a number of folds, bends, and loops in the protein chain. Different fragments of the same chain may become bonded together.
There are four types of bonding interactions between "side chains" including: hydrogen bonding, salt bridges, disulfide bonds, and non-polar hydrophobic interactions.

( http://www.elmhurst.edu/~chm/vchembo...rtprotein.html )
Thank you
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