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Nucleic Acids & Proteins Chapter 3 Biochemistry What you need to know! • How to recognize nucleic acids and proteins by their structural formulas • The cellular functions of nucleic acids and proteins • The 4 levels of protein structure • The denaturing impact that heat, pH, and other variables can have on protein structure Nucleic Acids • Consists of C, H, N, O, P • 3 types: DNA – Deoxyribonucleic Acid RNA – Ribonucleic Acid ATP – Adenosine Triphosphate • Different functions – DNA: hereditary information – RNA: production of proteins – ATP: energy molecule • Monomer = Nucleotide Nucleotide Three parts: 1. Phosphate group 2. Sugar (Deoxyribose in DNA, Ribose in RNA & ATP) 3. Nitrogenous base: (Adenine, Guanine, Cytosine, Thymine, Uracil) Nitrogenous Bases Come in 2 groups: 1. Pyrimidines (single ring): Thymine (T), Cytosine (C), Uracil (U) 2. Purines (double ring): Adenine (A), Guanine (G) • Purines fit with Pyrimidines A pairs with T G pairs with C (2 Hydrogen Bonds) (3 Hydrogen Bonds) • RNA replaces all T’s with Uracil (U) Polynucleotides • Nucleotide monomers can form Phosphodiester bonds – Phosphate-Sugar backbone of DNA and RNA • DNA double helix • RNA single helix ATP • Single nucleotide with 3 Phosphate groups (P) instead of 1 • It can lose P to release energy – ATP ADP + Energy – ADP AMP + Energy Proteins 1. Contain C, H, O, N, S 2. Millions of functions some of which include: • • • • • Enzymatic proteins regulate chemical Rxs Structural proteins support (ex. Muscles, cartilage) Storage proteins store amino acids Transport proteins move substances Hormonal proteins coordinate multicellular organisms • Receptor proteins respond to environmental stimuli • Contractile and motor proteins allow for movement • Defensive proteins protect against disease (antibodies) Proteins 3. Monomers: 20 different amino acids (AA) 4. Polymer = polypeptide • Small protein = ~100 AA • Large protein = 1000’s of AA (Titin) 5. Proteins are sensitive to • • • • temperature pH Imbalanced solutions all cause denaturizing (loss of accurate 3D structure) Amino Acids • Zwitterions: molecules that have both an amino group (NH3) and carboxyl group (COO or COOH) • 20 different AA • All have the same central carbon, amino group, and carboxyl group • Different functional groups (R – side chain) • R can be: – Polar, non-polar, charged, uncharged, hydrophilic, hydrophobic 20 Amino Acids Polypeptides • Connecting multiple AAs • Condensation Reaction forms peptide bond • Repetitive peptide backbone – (NCC-NCC-NCC-NCC) Protein structure (4 stages) • Structure and function determined by # and sequence of AA 1. Primary structure (AA sequence) 2. Secondary structure (Hydrogen to Oxygen) • Primary polypeptide coil and fold • Due to hydrogen bonds between adjacent peptide bonds O H (NOT r-side chains) • Special: alpha-helix, beta-pleated sheet Protein Structure 3. Tertiary Structure (R-side interactions) • Further coiling of secondary polypeptide due to R interactions • Hydrophobic vs. Hydrophilic • Polar Molecules • Formation of disulfide-bridge S-S • Hydrogen bonds • Van der Waals 4. Quaternary structure • Some proteins will associate with other tertiary proteins to form quaternary proteins • Several tertiary polypeptides connect together; usually held together by Rside chain interactions (hemoglobin) Structure Animation http://www.youtube.com/watch?v=lijQ3a8yU YQ Mutations Abnormal Proteins • Gene mutations can lead to the exchange of one or more AAs. This sometimes leads to a non-functional quaternary structure (Structure Function) • Example: Sicle-Cell Anemia, 1 AA is exchanged in the hemoglobin primary structure, resulting in abnormal folding.