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CARBON AND MOLECULAR DIVERSITY. The structure and function of macromolecules: Proteins and Nucleic Acids Chapter 5. Objectives. Describe the properties of a Protein
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CARBON AND MOLECULAR DIVERSITY The structure and function of macromolecules: Proteins and Nucleic Acids Chapter 5
Objectives • Describe the properties of a Protein • Understand how proteins are structured. Be able to explain each level of organization affects the shape and specificity of the protein • Describe the properties of a Nucleotide • Describe the differences in structure between major nucleic acids and how the structure correlates with function
PROTEINS: MOLECULAR TOOLS OF THE CELL. • Amino acids: the monomer building block of Proteins • A Polypeptide is a structural term used to describe a polymer of amino acids • Protein is a functional term applied to one or more polypeptides that perform a task within a cell • Functions of proteins may include: • Structural, Storage, Transport, Hormonal, Receptor, Contractile, Defensive, Enzymatic
STRUCTURE OF AMINO ACID. • Hydrogen atom. • Carboxyl group. • Amino group. • Variable R group.
Peptide Bond: The covalent bond between two amino acids formed via condensation synthesis.
Proteins are Flexible • Leads to complex three dimensional shapes
So what. Why should we care? • Flexibility within the polypeptide chain allows for potential interactions between various regions of the polypeptide and/or with other polypeptides. • This leads to diverse chemical structures, each potentially capable of performing a different role within the cell.
FUNCTION DEPENDS ON SPECIFIC CONFORMATION. • Primary level of organization • Sequence of amino acids, numbered from the amino end • Secondary level of organization • H bond interactions between the amino acid • Tertiary level of organization • “R” group interactions • Quaternary level of organization • subunit interactions
Protein Structure • Primary level of organization • Defined as the sequence of amino acids • Numbered from the amino end • Each protein has a unique combination of amino acids
Protein Structure • Secondary level of organization • H bond interactions between the amino and carbonyl groups of amino acids • helix, H bonds between every 4th AA • Pleated sheet, H bonds between protein regions lying parallel to each other
Pleated sheet: H bonds between protein regions lying parallel to each other; drawn as arrows in models • helix: H bonds between every 4th AA
Protein Structure • Tertiary level of organization • “R” group interactions, bonds • Disulfide bridges • Ionic bonds • H bonds • Hydrophobic interaction between nonpolar AA • reinforced by van der Waals
Protein Structure • Quaternary level of organization • subunit interactions
Changes in Protein Conformation • Denaturation: loss of a protein’s shape • Principally influenced by • pH: Disrupts H-bond interactions • Temperature: May break disulfide bonds • Protein folding is sometimes assisted by molecular chaperone proteins
NUCLEIC ACIDS: INFORMATIONAL POLYMER • Nucleic acids are polymers of monomer units called nucleotides • Nucleic acids store and transmit hereditary information: gene • Two major forms of nucleic acid polymers: DNA and RNA
Nucleotide Structure • Three parts to the monomer • Phosphate group • Sugar • Ribose • Deoxyribose • Nitrogenous base: • Pyrimidine • Purine
Nucleic Acids Polymers • Nucleotide polymers are created via phosphodiester linkages between the phosphate of one nucleic acid and the sugar of another
Synthesis is 5’-3’ • Because of the action of the enzymes involved in the attachment of the monomer units, nucleic acid synthesis always occurs from 5’ toward 3’ end
Monomer Unit Created During Synthesis • The nucleotide monomer is created during polymerization from a higher energy molecule: the nucleoside.
Nucleic Acids • DNA: Pyrimidines on one chain are attracted to Purines on an adjacent chain, H bonds
RNA Structure • RNA is also synthesized from nucleosides where Ribose is the sugar and the nitrogenous base Uracil replaces that of Thymine • Unlike DNA, RNA functions as a single polymer but may “double up” on itself via complimentary base pairing