Proteins

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Proteins

Postby J3 » Sun Nov 11, 2007 3:52 pm

Heyy i am overrrstuck on this questions: :(


What is the importance of hydrogen bonds in protein folding?

What is the importance of water-repelling and water-attracting amino acid side groups?

PLease HELpppp
:!: :)
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Postby Happydadtoo » Sun Nov 11, 2007 4:49 pm

Hi!

H-bonds provide the secondary structure of the protein - they create the alpha helix which makes up most of most proteins and the beta-pleated sheet which makes up a FEW (always extracellular and structural) proteins.

They also make up most of the tertiary structure too (though disulphide bridges also help here. Because H-bonds needs H atoms (doh!) and some of these change position with pH, the tertiary structure of a protein changes shape with pH and so therefore, does the shape of the active site. So..... H-bonds explain the pH curve of a typical enzyme.

The hydrophobic amino-acids collect towards the centre of the ptrotein, excluding water AND/OR are the exposed amino-acids in proteins which are embedded in membranes (and thus surrounded by lipid).
The hydrophyllic amino-acids are on the outside, where they are exposed to water AND form the central 'tube' of channel proteins in membranes.
They have some other uses too - histones wrap themselves around DNA and that interaction is helped by hydrophobic amino-acids as well as the basic ones (which react with the acidic phosphate groups on the DNA).

Hope that all helps a little
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Postby J3 » Tue Nov 13, 2007 8:35 pm

THAnkYUuu It Helped ALOOT xDD
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