Biological systems interact, and these systems and their interactions possess complex properties. STOP at enduring understanding 4A

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2 Biological systems interact, and these systems and their interactions possess complex properties. STOP at enduring understanding 4A

3 Homework Watch the Bozeman video called, Biological Molecules

4 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

5 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.

6 Nucleic Acids (RNA or DNA) Biological information is encoded in sequences of nucleotide monomers.

7 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

8 Which part(s) of a nucleotide stay the same? Which differ?

9 RNA vs. DNA DNA and RNA differ in function and differ slightly in structure, and these structural differences account for the differing functions.

10 How does the structure of RNA similar to DNA? How is it different?

11 Figure 3.27a 5 3 Sugar-phosphate backbones Hydrogen bonds 3 5 (a) DNA Base pair joined by hydrogen bonding

12 Figure DNA Functional differences between DNA and RNA 1 Synthesis of mrna mrna NUCLEUS CYTOPLASM

13 Figure DNA 1 Synthesis of mrna mrna NUCLEUS CYTOPLASM 2 Movement of mrna into cytoplasm mrna

14 Figure DNA 1 Synthesis of mrna mrna 2 3 NUCLEUS Movement of mrna into cytoplasm Synthesis of protein mrna CYTOPLASM Ribosome Polypeptide Amino acids

15 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

16 Homework Read pages in your textbook. REALLY REALLY REALLY read this section well.

17 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

18 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?

19 Proteins The specific order of amino acids in a polypeptide (primary structure) determines the overall shape of the protein

20 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.

21 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)

22 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)

23 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)

24 Figure 3.18 Peptide bond New peptide bond forming Side chains Backbone Amino end (N-terminus) Peptide bond Carboxyl end (C-terminus)

25 Begin the activity BCR-ABL protein

26 Homework Read pages in your textbook.

27 Objective: You will be able to describe the 3D conformation of proteins. Do Now:

28 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

29 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

30 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)

31 Figure 3.21ba Secondary structure helix pleated sheet Hydrogen bond strand Hydrogen bond

32 Tertiary level Disulfide bridge Hydrogen bond Hydrophobic interactions and van der Waals interactions Ionic bond Polypeptide backbone

33 Collagen

34 Protein Structure and Function A functional protein consists of one or more polypeptides precisely twisted, folded, and coiled into a unique shape

35 Complete Protein Folding Activity

36 Free-Write Write a few sentence that answers the question: How does a chain of amino acids develop into a three dimensional conformation.

37 Homework Read pages in your textbook.

38 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

39 Figure 3.6a Short polymer Unlinked monomer Dehydration synthesis removes a water molecule, forming a new bond. Longer polymer

40 Figure 3.6b (b) Hydrolysis: breaking down a polymer Hydrolysis adds a water molecule, breaking a bond.

41 Lipids Are MOSTLY nonpolar Fats (triacylglycerols vs. phospholipids)

42 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)

43 2014 Pearson Education, Inc.

44 Carbohydrates A monosaccharide

45 Disaccharide This covalent bond is called a glycosidic linkage

46 Polysaccharides Polysaccharides, the polymers of sugars, have storage and structural roles

47 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

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