[cs_content][cs_section parallax=”false” separator_top_type=”none” separator_top_height=”50px” separator_top_angle_point=”50″ separator_bottom_type=”none” separator_bottom_height=”50px” separator_bottom_angle_point=”50″ style=”margin: 0px;padding: 45px 0px;”][cs_row inner_container=”true” marginless_columns=”false” style=”margin: 0px auto;padding: 0px;”][cs_column fade=”false” fade_animation=”in” fade_animation_offset=”45px” fade_duration=”750″ type=”1/1″ style=”padding: 0px;”][cs_text]The Biochemistry of Movement > 9.7.4. Proteins are used as both structural molecules and enzymes to catalyse metabolic reactions > The Chemical Features Of A Protein >[/cs_text][cs_text style=”color: #800000;font-family: “Oxygen”,sans-serif;”]Explain, using a named example, the relationship between the chemical features of a protein and its shape using appropriate diagrams or models[/cs_text][cs_text]
- There are 20 different amino acids found in proteins. Protein molecules are made of long sequences of amino acids, which are connected by covalent peptide bonds.
- Thousands of proteins are known, and each one has a unique, specific amino acid sequence between 50-2000 amino acids long.
- When a polypeptide is formed, the side chain will remain the same.
- Primary structure is the amino acid sequence in the polypeptide chain.
- Secondary structure is the way in which the polypeptide chain folds.
- Tertiary structure refers to the way the secondary structure folds back upon itself or twists around to form a three-dimensional structure (the protein). This is the overall structure of the polypeptide chain.
- Quaternary structure: This is how multiple polypeptide chains join together.
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