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Primary structure entails the sequence of amino acids or the order in which the amino acids are covalently linked together. Amino acid proline creates a bend in the backbone as a result of of its cyclic structure. Because proline does not match into the alpha-helix it can cause the polypeptide helix to show. Proline does not match into the alpha-helix because: 1.) rotation across the bond between the nitrogen and the alpha-carbon is restricted, and 2.) proline’s alpha-amino group can not participate in intrachain hydrogen bonding. Sometimes there are other buildings discovered that end up altering or modifying the alpha-helix. This results in the formation of totally different protein buildings. 3o structure of a protein; this method exposes a beam of X-rays into pure crystals and a diffraction sample results. Greek Key:anti-parallel sheet that has the polypeptide chain doubling back on itself in a sample. B-meander unit: anti-parallel sheet is formed by a collection of tight reverse turns that join the polypeptide chain. The alpha-helix, beta-pleated sheets, and some other variation in secondary structure can come together in alternative ways allowing for differing kinds of polypeptide chain folding.
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