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    Can anyone help me with trying to describe both primary and secondary structures of proteins please for applied science level 3 unit 13. Any info is much appreciated.
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    Hi, I'll give a little overview of what the primary and secondary structures of proteins mean.

    The primary structure of a protein is the specific sequence of amino acids that make up the polypeptide chain. The amino acids are held together by peptide bonds and must be in a specific order to form a specific protein. The polypeptide chain is formed by the bonding of the alpha-carboxyl group of one amino acid to the alpha-amine group of another.

    Secondary structure in proteins can show two forms. Alpha-Helix structures or beta-pleated sheets. The alpha-helices are formed when the carbonyl O of one amino acid hydrogen bonds to the amine H in another amino acid, forming a curled helix, and leaving the R-groups to "stick out" to the side where they are free to interact. Beta-pleated sheets form where hydrogen bonds between a carbonyl O and an amine H in two amino acids form when they are lined up adjacently, forming a sheet like structure.

    Proteins can form both alpha helices and beta pleated sheets in their structures, just one, or none at all. The R-groups are not involved with the hydrogen bonding in secondary structure.

    Hope that helps
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    Thanks a lot this helped me massively
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    (Original post by Adam__nicholson)
    Can anyone help me with trying to describe both primary and secondary structures of proteins please for applied science level 3 unit 13. Any info is much appreciated.
    hi
    can you help me with unit 13.1 please p1 and d1. I find unit 13 very hard. pease
    thank you very much
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    (Original post by jsg9)
    Hi, I'll give a little overview of what the primary and secondary structures of proteins mean.

    The primary structure of a protein is the specific sequence of amino acids that make up the polypeptide chain. The amino acids are held together by peptide bonds and must be in a specific order to form a specific protein. The polypeptide chain is formed by the bonding of the alpha-carboxyl group of one amino acid to the alpha-amine group of another.

    Secondary structure in proteins can show two forms. Alpha-Helix structures or beta-pleated sheets. The alpha-helices are formed when the carbonyl O of one amino acid hydrogen bonds to the amine H in another amino acid, forming a curled helix, and leaving the R-groups to "stick out" to the side where they are free to interact. Beta-pleated sheets form where hydrogen bonds between a carbonyl O and an amine H in two amino acids form when they are lined up adjacently, forming a sheet like structure.

    Proteins can form both alpha helices and beta pleated sheets in their structures, just one, or none at all. The R-groups are not involved with the hydrogen bonding in secondary structure.

    Hope that helps
    hi
    have you Dinah unit 13.1 .p1 and d1 can you please help me.
    thank you.
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    (Original post by abbdul)
    hi
    have you Dinah unit 13.1 .p1 and d1 can you please help me.
    thank you.
    Unfortunately not, I don’t take applied science. If you have any specific questions I might be able to help?
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