Explain, with reference to hydrogen bonding, why the a-helix and B-sheet secondary structures of proteins are different?
This is an IB question, does anyone know what they are looking for?
i know that a-helix is a spiral structure and that B-sheet is pleated sheets but how do i answer in terms of H-bonding?
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a-helix vs. B-pleated sheets in terms of H-bonding watch
- Thread Starter
- 09-11-2008 06:52
- 09-11-2008 06:59
yeah, you just copy and pasted your hw question, so i'm not helping you.
Research this a little more and do it yourself.
I'll give you a tip though, the a is spiral because it doesn't bond to it's neighbours, and b does.
- 09-11-2008 14:23
alpha helix assumes the conformation due to the extensive hydrogen bonding between every four CO and NH groups of the amino acids(if I'm not wrong), whereas beta pleated sheet is due to the parallel nature of the CO-NH groups hence it assumes a sheet form.
Work on from there =)