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Explore the processes of condensation and hydrolysis in the formation and breakdown of essential organic compounds like carbohydrates, lipids, proteins, and nucleic acids in living organisms. Learn about the structure and function of molecules involved and the levels of protein structure. Discover how denaturation affects protein function and the role of DNA and RNA in encoding genetic information.
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Condensation vs. Hydrolysis AP Biology
Condensation and Hydrolysis Condensation Two molecules combine Hydrolysis A molecule splits into two smaller ones
Carbohydrates • Monosaccharides • 6 Carbon sugars • Glucose • Fructose • Galactose • 5 Carbon sugars • Deoxyribose • Ribose
Carbohydrates • Oligosaccharides • Disaccharides • Sucrose • Lactose • Maltose • Formed by condensation reactions
Fatty Acids • Carbon backbone • Carboxyl group (- COOH) • Unsaturated • One or more double bonds in backbone • Saturated • All single bonds in backbone
Triglycerides • Neutral fats • Three fatty acids and a glycerol • Condensation reaction • Body’s mostabundant lipid • Functions: • Energy reservoir • Insulation
Structure of Amino Acids • Central carbon atom • An amino group • A carboxyl group • A hydrogen atom • One or more atoms “R Group”
Peptide Bond Formation • A type of condensation reaction
Levels of Protein Structure • Primary structure: The sequence of amino acids in a polypeptide chain. • Secondary structure: The polypeptide chains folds on itself to form a helix or a pleated sheet. • Tertiary structure: The helix and or pleated sheet fold on itself to form a globular structure • Quaternary structure: two are more tertiary structures binding together.
Second Level of Protein Structure • Hydrogen bonds • Helical coiling • Sheet-like pattern
Third Level of Protein Structure • Additional folding of secondary structure • R Group interactions • Hydrogen bonds • Disulfide bridges
Fourth Level of Protein Structure • Two or more polypeptide chains joined by • Weak bonds (Hydrogen bonds) • Covalent bonds between sulfur atoms and R groups • Collagen • Keratin • Hemoglobin
Structural Changes by Denaturation • Disruption of three-dimensional shape of protein • Changes in temperature and pH • Loss of function • Some proteins have organic compounds attached • Glycoproteins • Lipoproteins
DNA Double stranded Hydrogen bonds between strands Twisted helically Four kinds of nucleotide monomers (A, T, C, G) Encodes protein-building instructions RNA Single stranded Four kinds of nucleotide monomers (A, U, C, G) Do not encode protein-building instructions Key players in the protein-building processes mRNA, tRNA, rRNA Two types of Nucleic acid
Nucleic Acids - DNA and RNA • Building blocks • Four kinds of nucleotides • Differ only in component bases
Single Strand of Nucleic Acid A series of covalently bonded nucleotides Nucleotides form together by condensation reactions
In Conclusion • Organic compounds have elements covalently bonded to carbon atoms • Living cells assemble organic compounds: lipids, carbohydrates, proteins, and nucleic acids • The building blocks are amino acids, nucleotides, simple monosaccharide sugars, and fatty acids • Complex carbohydrates are energy storage forms and structural materials
In Conclusion • Lipids are used as energy storage and structural components • Proteins are made of amino acids. They form structural part of the body as well and enzymes. • Nucleic acids are the basis of inheritance and reproduction • developed by M. Roig