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IUB BIOL-L 112 - Protein Structure and Function

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BIOL-L 112 1nd Edition Lecture 6 Outline of Last Lecture I. ProteinsII. Amino AcidsA. Nonpolar Side ChainsB. Polar Side ChainsC. Electrically Charged Side ChainsOutline of Current Lecture I. Protein StructureA. Primary StructureB. Secondary StructureC. Tertiary StructureD. Quaternary StructureII. Protein Folding in the CellIII. Nucleic AcidsIV. DNAV. RNACurrent LectureI. The structure of a protein is a unique 3D shape and plays a large role in function. There are four different levels of protein structure: primary, secondary, tertiary, and quaternary. The structure of a protein is affected by the folding that occurs as the protein is synthesized within a cell and the physical/chemical conditions of its environment. These conditions include pH, salt concentration, solvent, heat, and chemicals present that may disrupt bonding. A. The primary structure of a protein is linear and involves only the covalent bonds between the amino acids. This sequence of amino acids is genetically determinedand difficult to break. B. The secondary structure of a protein is held together by hydrogen bonding between parts of the polypeptide backbone, NOT the side chains. It causes coils and folds in the structure. There are two types of secondary structures: alpha-helix coils and beta-pleated sheets. C. The tertiary structure gives a protein its unique shape because of the interactionsbetween atoms on the side chains of the amino acids. It involves both weak and These notes represent a detailed interpretation of the professor’s lecture. GradeBuddy is best used as a supplement to your own notes, not as a substitute.strong chemical bonds (in order of increasing strength): hydrophobic interactions, hydrogen bonding, ionic bonds, and disulfide bonds.D. The quaternary structure is the bonding between 2 or more polypeptides. These bonds are due to interactions between side chains of amino acids and include hydrophobic interactions, hydrogen bonds, ionic bonds, and disulfide bonds.II. Protein folding within a cell is a complicated process that goes through several intermediates before achieving the final and stable state of a protein. Molecules called chaperonins are proteins that assist in this folding process by keeping it the protein in a segregated environment after it detaches from a ribosome so that it is able to form spontaneously. The main point is that the folding process of a protein is critical for its structure, and the structure of a protein is critical for its function.III. Nucleic acids function to store and transmit hereditary information. They include deoxyribonucleic acids (DNA) and ribonucleic acids (RNA). The directional flow of information by nucleic acids starts at DNA and is transcribed in the nucleus to RNA. mRNA then directs the synthesis of proteins on ribosomes through translation. The nucleotides in nucleic acids are nitrogenous bases: pyrimidines and purines. Pyrimidines are cytosine, thymine, and uracil. Purines are adenine and guanine. Uracil is only presentin RNA and thymine is only present in DNA. Phosphodiester bonds connect these nucleotides together through a dehydration reaction.IV. A DNA molecule is made of two chains of polynucleotides that run in opposite directions(5’  3’ and 3’  5’) from each other and spiral into a double helix. The two chains are held together by hydrogen bonds. In DNA, adenine bonds with thymine and guanine bonds with cytosine. V. RNA molecules are single stranded and are more variable in structure. Adenine bonds with uracil and guanine bonds with cytosine by hydrogen bonds. Complementary pairingcan also occur between parts of the RNA molecule or 2 RNA molecules to make molecules such as tRNA, which has an L-shaped


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IUB BIOL-L 112 - Protein Structure and Function

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