Lec 8 Protein PDF

Summary

This document is lecture notes on proteins, covering their different types, structures, and classifications. It details the primary, secondary, and tertiary structures of proteins, as well as chemical classifications of proteins, and related topics such as denaturation and protein hydrolysis. Includes details about globular proteins and fibrous proteins.

Full Transcript

# Lecture 8: Proteins ## **Protein** - Polymer of amino acids - Histon protein rich of basic amino acids [positive charge] ## Classification - According the shape: - **Structural**: Plays a role in the structure of a protein. They're insoluble in water. Examples are keratin and fibrous proteins...

# Lecture 8: Proteins ## **Protein** - Polymer of amino acids - Histon protein rich of basic amino acids [positive charge] ## Classification - According the shape: - **Structural**: Plays a role in the structure of a protein. They're insoluble in water. Examples are keratin and fibrous proteins - **Dynamic**: - Enzymes, hormones - Steroids, insulin, glucagon - Antibodies - Have regulatory function - Transport protein - Hemoglobin, myoglobin - Lactopheren make the immunity higher against infection - Myoglobin: storage O2 in muscles ## Chemical Classification - **Primary Structure of Protein**: The particular sequence of amino acids that is the backbone of a peptide chain or protein. A single polypeptide chain, for example, is the hair pin shape. **-Ala - Leu - Cys - Met**. ## Secondary Structure - **Alpha Helix**: Three-dimensional arrangement of amino acids with the polypeptide chain in a corkscrew shape. Held by H bonds between the H of - N-H group and the - O of C =O of the fourth amino acid along the chain. It looks like a coiled, "telephone cord". - **Beta pleated sheet**: - Poly peptide chains are arranged side by side. - Hydrogen bond between chains. - R groups of extend above and below the sheet. - Typical of fibrous proteins such as silk. - **Triple Helix**: Three poly peptide chains, woven together, like a rope. Glycin, Proline, hydroxy Proline and hydroxy lysin. H bond between - OH groups gives a strong structure. Typical of Collagen: connective tissue skin tendons and cartilage. ## Tertiary Structure. - Specific overall shape of protein. - Cross linked between R groups of amino acids in chain. - DiSulfide: S-S - H bonds: C=O No - Ionic: -Coo H3N+ - Hydrophobic: CH3 H3C- - **DiSulfide (S)**: Two Cysteines - **Ionic (acid and base)**: Aspartic acid and lysine - **H bond (Co. OH)**: Serine and threonine - **Hydrophobic CH₃**: Leucine and valine ## Protein types - **Globular protein**: Spherical shape. - Insulin - Hemoglobin. - Enzymes - Antibodies - **Fibrous protein**: are long, thin fibers. - Hair - Wool - Skin - Nail ## Quaternary Structure - Protein with two or more chains polypeptide. - Example is hemoglobin [carries oxygen in blood. Four polypeptide chains. Each chain has a heme group to bind oxygen]. ## Denaturation - **Denaturation**: Disruption of secondary, tertiary and quaternary protein structure. - **Physical**: - Heat - Pressure - Break down H bond and disrupt hydrophilic bond. - **Chemical**: - Acids/base - Break H bonds between polar R group and ionic bonds. - Strong acids/bases only are irreversible ## Protein Hydrolysis - Break down of peptide bonds. - Requires acid or base, water and heat. - Gives Smaller peptides and amino acids. - Similar to digestion of protein using enzymes in stomach. - Occurs in cells to provide amino acids to synthesize other proteins and tissues. - Water + HCL + enzyme (Catalyst) play a role in digestion. - Children need protein than people (old edge) - Decreasing of the Source of protein (to save Kidney) - Decreasing of activity of enzymes in old edge ## Application of Denaturation - Hard boiling an egg. - Wiping the skin with alcohol swab for injection. - Cooking Food to destroy E. Coli - Heat used to cauterize blood vessels. - Autoclave sterilizes instruments. - Milk is heated to make yogurt ## Some notes in Structural proteins. - **Where is the Collagen**: Skin, Cartilage, components of bones and tendon. - **Keratin**: Hair, skin, nails, bird feathers. - **Elastin**: used in contractile protein. (Energy + heat) movement - **Actin. Myosin**: In the event of a heart attack, not in normal level. - **Fibral protein**: plays a role in blood clotting # Other notes - **H₂O₂**: Milk protein, Sugar + milk = lactose - **Immunogloblin**: Exists in the cell. - **Antibodies**: defends the cell against disease. - **Globular protein**: spherical, 4:10 - **Fibrous protein**: elongatudinal, 10 or more than 10 - **Congiucated protein**: Not pure protein.

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