Proteins |
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Made up of C,H,O and N |
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No set ratio |
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Made up of chains of Amino acids (Usually 75 or more) |
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Amino acid chains formed through dehydration synthesis |
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40% of the human body is made of protein |
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Building blocks of Proteins are Amino acids |
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Amino group (NH2 or NH3) acts as a base (Accepts H+) |
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Carboxyl group (COOH or COO-) acts as an acid (Donates H+) |
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R Group:There are 20 different possibilities |
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Amino acids bond through dehydreation synthesis |
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The amino acids bind together with a peptide bond |
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Peptide bond is formed between C and N no water is lost (Dehydration Synthesis) |
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When original two amino acids form beginning of the chain with one peptide bond is called a Dipeptide |
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It can grow and become a Tripeptide |
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End state is Polypeptide (30 and 30,000 amino acids) |
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Another name fro polypeptide is Protein |
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Every protein is different because the order of amino acids is different |
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Or order of different R groups and how they bond |
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They also function differently |
Levels of Protein Structure |
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Primary Structure |
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First level of how proteins are formed |
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Order of amino acids joined together with peptide bonds |
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Amino acids sequence tgat determine the nature and chem of protein |
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Secondary Structure |
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Second step in forming protein |
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When peptide bond is formed, a double bonded oxygen is left over. |
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Attracted to positive NH3 amino group from other amino acids in the chain |
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This attraction forms a hydrogen bond |
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This causes the chian to twist called alpha helix or a beta pleated sheet |
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Tertiary Structure |
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The next interaction take place between R groups |
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Some R groups are reactive and will interact with other reactive R groups in the chain. |
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These amino acids that are either charged or that have a sulphure atom |
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The interactions (tand attractions and S-S bridges) will fold the molecule over into a highly specific 3 dimensional shape |
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It is 3-D shape that will determine the proteins job or role in the body |
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Quaternary Structure |
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This last level in protein formation is not seen in all proteins |
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Proteins can actually be 2 or more molecules joined to form a functional protein |
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These are held by ionic bond |
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Two Examples |
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Insulin has 2 subunits |
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Hemoglobin has 4 subunits |
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The whole process |
Bonds |
Primary protein structure |
Peptide Bonds |
Secondary protein structure |
Hydrogen Bonds |
Tertiary protein structure |
Interactions between R groups |
Quaternary protein structure |
Ionic Bonds |
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Denaturation |
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Final shape of protein is very specific and enables it to do its job/function |
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Any change in a proteins shape will affect its function |
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Denaturation is when a protein tertiary structure is lost |
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This happens when R group bonds are broken |
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When a denaturation the protein cannot do its joband becomes useless |
How does this happen? |
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Temperature |
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High temperature affects the weak hydrogen bonds and can distort or break them |
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A slight increase in temp can cause reversible change (Fever) |
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A high increase will cause irreversible change (Cooking an egg) |
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Chemicals |
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Heavy metals like lead and mercury are large atoms that are attracted the R groups of amino acids |
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They bond to the R group and distort proteins shape |
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This is usually irreversible |
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PH |
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As some of the R groups are acids and some are bases, every protein (enzyme) has a preferred PH |
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Any change in PH causes a change in the acid base R group interactions and this will change the shape of the protein |
Functions of Proteins |
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Structural |
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Proteins help make up all structurers in living things |
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Actin & Myosin: Muscle Proteins |
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Keratin: Nails, Hair, Horns, Feathers |
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Collagen:Bones, teeth, cartilage, tendon, ligament, blood vessels, skin matrix |
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Functional |
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Other proteins help us to keep our bodies functioning properly and to digest our food |
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Enzymes:Are proteins that are catalysts which speed up reactions and control all cell activities |
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Food Source:Once we have used up all of our carbohydrates and fats, proteins will be a use of energy |
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Proteins are worth the least amount of energy per gram |