1. Draw sucrose. Label the glycosidic bond.

2. Draw a triglyceride, label the fatty acids and the glycerol.

3. Draw two nucleotides bonded together, use "B" for the bases but draw out all of the atoms in the sugars and the phosphates.
Phosphodiester bonds
Bases (B) B B B B

4. Draw two amino acids joined by a peptide bond, label the peptide bond

5. Where’s the peptide bond. Where are the R groups
Where’s the peptide bond? Where are the R groups? Which Amino acids are these?

6. Where’s the peptide bond. Where are the R groups
Where’s the peptide bond? Where are the R groups? Which Amino acids are these?

7. The 20 amino acids that make up all human proteins

8. Primary Structure
The simple amino acid sequence of the protein

9. Secondary Structure
Hydrogen bonds cause regions of the polypeptide to fold into distinctive shapes called Alpha-helices and Beta-pleated-sheets

10. Tertiary Structure
When the protein folds into its full three dimensional shape. This folding is caused by the properties of the side chains that results in nonpolar regions folding to the inside, polar interactions (positive and negative regions stick together) like hydrogen bonding, and covalent disulfide bonds

11. Tertiary Structure
When the protein folds into its full three dimensional shape. This folding is caused by the properties of the side chains that results in nonpolar regions folding to the inside, polar interactions (positive and negative regions stick together) like hydrogen bonding, and covalent disulfide bonds

12. Tertiary Structure of Insulin
Insulin is a protein produced in the pancreas and released in the blood when your blood sugar level is high. It tells all of the cells in your body to take in sugar from the blood. Excess sugar in the blood can damage your organs. People with type 1 diabetes have a mutation that causes them either not to make insulin or to make defective insulin. People with type 2 diabetes have become desensitized to insulin and so their cells do not respond to it.
Ribbon Model
Space Filling Model

13. Tertiary Structure of Insulin
Insulin is a protein produced in the pancreas and released in the blood when your blood sugar level is high. It tells all of the cells in your body to take in sugar from the blood. Excess sugar in the blood can damage your organs. People with type 1 diabetes have a mutation that causes them either not to make insulin or to make defective insulin. People with type 2 diabetes have become desensitized to insulin and so their cells do not respond to it.

14. Tertiary Structure of Insulin
Insulin is a protein produced in the pancreas and released in the blood when your blood sugar level is high. It tells all of the cells in your body to take in sugar from the blood. Excess sugar in the blood can damage your organs. People with type 1 diabetes have a mutation that causes them either not to make insulin or to make defective insulin. People with type 2 diabetes have become desensitized to insulin and so their cells do not respond to it.
Van der Waals Forces, hydrogen bonding, ionic attraction, polar/non polar interactions play a role in protein docking as well.
Ligand
Receptor

15. Quaternary Structure
When two folded proteins come together to form a protein complex. Not all proteins do this.
Hemoglobin is a protein complex formed by four heme proteins, two alpha globin proteins, and two beta globulin proteins. The alpha and beta globulin proteins each wrap around a heme protein and then these four units fit together to form the quaternary structure of a complete hemoglobin complex.
Hemoglobin is the main protein in red blood cells. The heme proteins have an iron atom at their center which is what holds onto oxygen.

16. Summary of Protein Folding

17. Functions of Proteins Structural Enzymes Hormones
Building blocks of cells and cell products
Ex: Hemoglobin in Red Blood Cells
Ex: Keratin in skin, hair, and nails
Enzymes
Cause chemical reactions to occur (catalysts)
Ex: Amylase – breaks starches into sugars (in mouth)
Hormones
Transmit messages between cells
Ex: Insulin from pancreas tells cells to let sugar in
Ex: Sex hormones tell different parts of the body what to do to prepare for reproduction

18. Enzymes
Cause chemical reactions to occur by lowering the activation energy needed (catalysts). Specifically, they help two reactants come together at just the right angle. Also, they can help put strain on the bonds in a reactant making them easier to break so that the new bonds will more easily form.
hill.com/sites/ /student_view0/chapter2/animation__how_enzymes_w ork.html
The ligand(s) fit into the active site like a lock and key

19. Hormones
Cause a protein to change shapes thereby creating a response. This can lead to a chain reaction in which various hormones and enzymes trigger one another ultimately resulting in a final outcome.
hill.com/sites/ /student_view0/chapter2/animation__how_enzymes_ work.html

20. Hormones Signal Transduction
Cause a protein to change shapes thereby creating a response. This can lead to a chain reaction in which various hormones and enzymes trigger one another ultimately resulting in a final outcome.
Signal Transduction

21. Answers to Macromolecules in Depth assignment:
CARBOHYDRATES
Provide energy and structure
Monosaccharides
Disaccharides
Oligosaccharides
Polysacharides
1:2:1
Glucose
Fructose
Galactose
Sucrase
Lactose intolerant people do not make lactase, the enzyme needed to break down lactose
Starch is a polymer made of hundreds of sugar/glucose molecules attached together. Plants make starch to store a lot of energy.
Glygogen
Cellulose is a starch that has a lot of hydrogen bonds which stabilize it. We cannot digest it because we do not make an enzyme that can break starch down.
We use a dehydration reaction to join two sugars and a hydrolysis reaction to break apart two sugars

22. Answers to Macromolecules in Depth assignment:
LIPIDS
3 fatty acids and a glycerol molecule
Lipases
Cell membranes
Hydrocarbons are long chains of carbon atoms with hydrogen atoms attached to each carbon.
Energy is stored in the bonds between the carbons and the hydrogens
Saturated fats are solid at room temperature because their chains are straight so they stack easily, forming solids; while unsaturated fats have bends in their chains which prevent them from stacking keeping them fluid
Saturated fats
Olestra is a synthetic (man made) fat that the body cannot digest
Phospholipids are polymers with negatively charged phosopate “heads” and two uncharged lipid “tails”. They are the main component in membranes.
The phosphate heads are polar and the lipid tails are nonpolar.

23. Answers to Macromolecules in Depth assignment: PROTIENS
Amino acids food/diet
Ribosomes
Threonine is polar while alanine is nonpolar
Aspartic acid is negatively charged and lysine is positively charged so they are attracted to one another
Once it folds into its final 3D shape
The primary structure is the amino acid sequence of the protein
The secondary structure is the set of alpha helices and beta sheets that form in regions of the protein
Hydrogen bonds
The tertiary structure is the final shape of the whole protein that results from interactions between the side groups
The quaternary structure is when two or more folded proteins combine together to form a protein complex
Foldit is a game in which you try to solve protein folding challenges
R group
R group
R group
R group