Objective: You will be able to explain how the subcomponents of nucleic acids determine the properties of that polymer. Do Now: Read the first two paragraphs from enduring understanding 4.A
Essential knowledge: The subcomponents of biological molecules and their sequence determine the properties of that molecule. Structure and function of polymers are derived from the way their monomers are assembled.
Nucleic Acids (RNA or DNA) Biological information is encoded in sequences of nucleotide monomers.
Figure 3.26a 5 end Sugar-phosphate backbone (on blue background) 5 C 3 C Identify the 3 parts of a nucleotide Nucleoside Nitrogenous base 5 C 3 C Phosphate group (b) Nucleotide Sugar (pentose) 3 end (a) Polynucleotide, or nucleic acid
Which part(s) of a nucleotide stay the same? Which differ?
RNA vs. DNA DNA and RNA differ in function and differ slightly in structure, and these structural differences account for the differing functions.
How does the structure of RNA similar to DNA? How is it different?
Figure 3.27a 5 3 Sugar-phosphate backbones Hydrogen bonds 3 5 (a) DNA Base pair joined by hydrogen bonding
Figure 3.25-1 DNA Functional differences between DNA and RNA 1 Synthesis of mrna mrna NUCLEUS CYTOPLASM
Figure 3.25-2 DNA 1 Synthesis of mrna mrna NUCLEUS CYTOPLASM 2 Movement of mrna into cytoplasm mrna
Figure 3.25-3 DNA 1 Synthesis of mrna mrna 2 3 NUCLEUS Movement of mrna into cytoplasm Synthesis of protein mrna CYTOPLASM Ribosome Polypeptide Amino acids
Individual Work Use DNA kits to build DNA Create a key for the parts Hints Yellow tube is for covalent bond connecting sugar and phosphate group Look at number of bonds for each sub component You have enough to create 6 nucleotides on each side Page 258 (250-old) will be very helpful in your endeavor
Objective: You will be able to explain how the subcomponents of proteins determine the properties of that polymer. Do Now: List what you can remember about amino acid or protein structure
Genetic information flows from a sequence of nucleotides in a gene to a sequence of amino acids in a protein. How would you define transcription? How would you define translation?
Proteins The specific order of amino acids in a polypeptide (primary structure) determines the overall shape of the protein
The R group of an amino acid can be categorized by: Chemical properties Hydrophobic, hydrophilic and ionic The interactions of these R groups determines the structure and function of that region of the protein.
Figure 3.17a Notice the C-H bonds Nonpolar side chains; hydrophobic Side chain (R group) Glycine (Gly or G) Alanine (Ala or A) Valine (Val or V) Leucine (Leu or L) Isoleucine ( le or ) Methionine (Met or M) Phenylalanine (Phe or F) Tryptophan (Trp or W) Proline (Pro or P)
Figure 3.17b Notice the O-H bonds Polar side chains; hydrophilic Serine (Ser or S) Threonine (Thr or T) Cysteine (Cys or C) Tyrosine (Tyr or Y) Asparagine (Asn or N) Glutamine (Gln or Q)
Figure 3.17c Electrically charged side chains; hydrophilic Acidic (negatively charged) Basic (positively charged) Aspartic acid (Asp or D) Glutamic acid (Glu or E) Lysine (Lys or K) Arginine (Arg or R) Histidine (His or H)
Figure 3.18 Peptide bond New peptide bond forming Side chains Backbone Amino end (N-terminus) Peptide bond Carboxyl end (C-terminus)
Objective: You will be able to describe the 3D conformation of proteins. Do Now:
Proteins The specific order of amino acids in a polypeptide (primary structure) interacts with the environment to determine the overall shape of the protein Structure and function are related
The sequence of amino acids, determined genetically, leads to a protein s three-dimensional structure Primary Structure The shape is also affected by secondary tertiary and quaternary structure
Figure 3.18 Primary Structure Where is the backbone? Peptide bond New peptide bond forming Side chains Backbone Amino end (N-terminus) Peptide bond Carboxyl end (C-terminus)
Figure 3.21ba Secondary structure helix pleated sheet Hydrogen bond strand Hydrogen bond
Tertiary level Disulfide bridge Hydrogen bond Hydrophobic interactions and van der Waals interactions Ionic bond Polypeptide backbone
Collagen
Protein Structure and Function A functional protein consists of one or more polypeptides precisely twisted, folded, and coiled into a unique shape
Figure 3.23-2 Normal protein Denatured protein
Figure 3.23-3 Normal protein Denatured protein
Objective: You will be able to explain how the subcomponents of lipids and carbohydrates determine the properties of that polymer. Do Now: Make a list of facts that you remember about phospholipids
Figure 3.6a Short polymer Unlinked monomer Dehydration synthesis removes a water molecule, forming a new bond. Longer polymer
Figure 3.6b (b) Hydrolysis: breaking down a polymer Hydrolysis adds a water molecule, breaking a bond.
Lipids Are MOSTLY nonpolar Fats (triacylglycerols vs. phospholipids)
Figure 3.12 Fatty acid (in this case, palmitic acid) Glycerol (a) One of three dehydration reactions in the synthesis of a fat Ester linkage (b) Fat molecule (triacylglycerol)
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Carbohydrates A monosaccharide
Disaccharide This covalent bond is called a glycosidic linkage
Polysaccharides Polysaccharides, the polymers of sugars, have storage and structural roles
Figure 3.11 (a) and glucose ring structures Glucose Glucose (b) Starch: 1 4 linkage of glucose monomers (c) Cellulose: 1 4 linkage of glucose monomers