Protein Denaturation (Part 1) PDF

Biochemistry: DENATURATION OF PROTEINS Presented by Avionna D. Pico of 1-BN BSN Table of Contents: 01 PROTEINS 02 DENATURATION OF PROTEINS 04 IMPORTANCE 05 TEMPERATURE 06 PH LEVEL What are PROTEINS? Proteins are large, complex molecules made up of smaller units called amino...

Biochemistry: DENATURATION OF PROTEINS Presented by Avionna D. Pico of 1-BN BSN Table of Contents: 01 PROTEINS 02 DENATURATION OF PROTEINS 04 IMPORTANCE 05 TEMPERATURE 06 PH LEVEL What are PROTEINS? Proteins are large, complex molecules made up of smaller units called amino acids. They are essential nutrients for the body and play a critical role in almost every biological process. Proteins help build, repair, and maintain body tissues (like muscles, skin, and organs) and are vital for producing enzymes, hormones, and immune system components. What are PROTEINS made of? All proteins are organic macromolecules Contain the elements; Amino Carboxyl Carbon, Hydrogen, Oxygen group group and Nitrogen The protein building block or monomer is called an amino acid molecule Side chain (R-group) AMINO ACIDS POLYPEPTIDE PEPTIDE PROTEIN PROTEIN STRUCTURE Summary of Proteins Organic macromolecules Primary Structure - unique containing C, H, O, N sequence of amino acids Amino acids are the monomers Secondary Structure - local folding Proteins are created when amino patterns; alpha helices and beta acids chemically combine sheets, stabilized by hydrogen bonds The bond that connect the amino Tertiary Structure - overall 3D shape, acids is called a peptide bond formed by interactions among Small or short protein molecules amino acid side chains. are called protein polymers or Quaternary Structure - when peptides multiple polypeptides chains join Longer protein polymers or together to form a functional protein peptides is called a polypeptide complex  Denaturation of Proteins Denaturing of proteins refers to the process in which a protein loses its native structure and unfolds due to external factors, such as changes in temperature, pH, or exposure to chemicals. This alteration disrupts the weak bonds (like hydrogen bonds and disulfide bridges) that maintain the protein's specific three- dimensional shape. Denaturation of Proteins Key Points on Denaturation of Proteins: Loss of Structure - Denaturation causes Reversibility - In some cases, proteins to lose their secondary, tertiary, or denaturation is reversible, and the quaternary structures while leaving the protein can regain its original shape primary structure (the sequence of amino under appropriate conditions. But in acids) intact. many instances, especially with extreme heat or harsh chemicals, denaturation is Functionality Impact - This loss irreversible. of structure typically results in a loss of biological function because the protein can no longer interact properly with other molecules.  Importance of Denaturation of Proteins Denaturation is important because it helps us understand how proteins work and respond to changes in their environment. Health and Medicine: Understanding Food Preparation: Cooking denatures proteins, denaturation is essential in medicine, as changing texture and making food safer and extreme conditions (like high fevers) can easier to digest. denature critical proteins in the body, Digestion: it unfolds their complex structures, making them more accessible to digestive leading to health risks. enzymes like pepsin in the stomach. Proteins Sterilization: Heat or chemicals denature are broken down into smaller peptides and proteins in bacteria, helping to sterilize amino acids that can be easily absorbed in the medical tools and surfaces. small intestine  Denaturing Agents Denaturing agents are substances or conditions that disrupt the structure of proteins, causing them to lose their natural shape (or "denature") and often their function. Physical Agents: heat, mechanical Chemical Agents: acids and bases, organic agitation, radiation solvents, heavy metals, reducing agents, salts  Chaperones or Chaperonins Chaperones, or chaperonins, are specialized proteins that help other proteins fold correctly into their functional 3D structures. During or after protein synthesis, newly made proteins often need assistance to achieve their correct shape, especially under conditions that could lead to misfolding or aggregation. In short, chaperones are like the cell's folding assistants, ensuring proteins get into the right shape to function properly and stay healthy. Denaturing Agent: Temperature is a physical denaturing agent because high temperatures increase the kinetic energy of molecules, causing proteins to lose their structure. When the temperature rises, the increased energy breaks hydrogen bonds and hydrophobic interactions that hold the protein's shape together. This leads to unfolding of the protein and loss of its original structure. Examples: Cooking an egg High fever Denaturing Agent: pH changes pH changes (chemical denaturing agent) can denature proteins by disrupting the bonds that maintain their structure. When the pH changes (becomes more acidic or basic), it affects the charges on parts of a protein. This change messes up the bonds that hold the protein’s shape, causing it to lose its structure and function. Change in pH = Change in Charge Ionic Interactions & Hydrogen Bonds are affected Ionic Interactions Proteins have positively charged amino groups (NH₃⁺) and negatively charged carboxyl groups (COO⁻) Ionic Interactions In basic conditions, NH₃⁺ loses a hydrogen and becomes neutral (NH₂), breaking its bond with COO⁻. Ionic Interactions In acidic conditions, COO⁻ gains a hydrogen, becoming neutral (COOH), and also loses its bond with NH₃⁺. Hydrogen Bonds Proteins also rely on hydrogen bonds, which form because of charges between atoms like oxygen and hydrogen. Hydrogen Bonds Adding too many hydrogen ions (like in an acidic environment) disrupts these bonds, causing the protein to lose its structure  Thank You! Denaturation of Proteins (Part 1) Presented by Avionna D. Pico of 1-BN BSN References: Professor Makkieh. (2020, August 21). Protein denaturation - quick explanation! [Video]. YouTube. https://www.youtube.com/watch?v=oyzx7ttssss Kiki Sanford. (2017, February 24). What is Protein Denaturation? - Food Science [Video]. YouTube. https://www.youtube.com/watch?v=WFmgPrZ02Yg Madpathi, A. (2018, February 21). PROTEIN DENATURATION [Slide show]. SlideShare. https://www.slideshare.net/ArchanaMadpathi/protein-denaturation? fbclid=IwY2xjawGWcvlleHRuA2FlbQIxMAABHYHOtUCg66R7C0yk2IS0RU- H2PQLQcBAsfJP_wxqz_I_de1nLK5yXZonDA_aem_8YNF6oR2prKnWSFQCWhg3w#31 Khan Academy. (n.d.). https://www.khanacademy.org/science/biology/macromolecules/proteins-and-amino- acids/a/introduction-to-proteins-and-amino-acids Amoeba Sisters. (2018, September 24). Protein structure and folding [Video]. YouTube. https://www.youtube.com/watch?v=hok2hyED9go Nucleus Biology. (2021, December 10). Proteins [Video]. YouTube. https://www.youtube.com/watch?v=kMg517MHDJs