1. Biomolecules

2. BIOMOLECULES
Carbohydrates
Fats
Proteins

3. Organic Compounds Carbohydrates
A group that includes things like table sugars and starches.
Includes Simple and Complex groups

4. Simple Carbohydrates Simple Monosaccharides Fructose Glucose
Disaccharides
Sucrose
Lactose

5. Monosaccharides

6. Disaccharides

7. Glycogen: a Polysaccharide

8. Complex Carbohydrates
Polysaccharides are long branching chains of simple sugars, specifically glucose.
Starch is a storage carbohydrate in plants.
Glycogen is a storage carbohydrate in animals.
Liver and muscles

9. How the Body Uses Sugars
Glycogen exists in the body as a reservoir of available energy that is stored in the chemical bonds within individual glucose monomers.
Hydrolysis of glycogen, as occurs during periods of fasting, leads to release of the glucose monomers into the blood, thereby preventing blood glucose from decreasing to dangerously low levels.
Glucose is often called “blood sugar” because it is the major monosaccharide found in the blood.

10. Lipids
Lipids are molecules composed predominantly (but not exclusively) of hydrogen and carbon atoms.
These atoms are linked by nonpolar covalent bonds. Thus, lipids are nonpolar and have a very low solubility in water.
Lipids can be divided into four subclasses: fatty acids, triglycerides, phospholipids, and steroids.
Solid at room temp = fat;
Liquid at RT = oil

11. Triglycerides

12. polyunsaturated) fats are liquid at room temp.
Unsaturated (mono- &
polyunsaturated) fats
are liquid at room temp.
Trans fats have added hydrogen (hydrogenated) (p 29)
Triglycerides: 3 FA + Glycerol
Saturated Unsaturated Polyunsaturated

13. Trans Fats

14. Organic Compounds Lipids, Fats or Triglycerides
Composed of Glycerol backbone plus 3 fatty acid chains
Saturated Fats
Contains only single bonds between the carbons on the fatty acid chains
Solid at room temperature
Unsaturated Fats
Contains one or more double bonds between the carbons on the fatty acid chains
Semi-solid or liquid at room temperature
Mono, di- and polyunsaturated fats
Will only dissolve in other lipids and insoluble in water.
Like Dissolves in Like

15. Phospholipid

16. Phospholipids

17. Organic Compounds Phospholipids Modified triglycerides
Phosphorous head and two fatty acid tails
Amphipatic
Hydrophilic, as well as
Hydrophobic
Found only in human cell membrane as a bi-layer
Hydrophobic – Tails on the inside of the membrane
Hydrophilic – Heads on the outside of the membrane

18. Cholesterol

19. Steroids
Cholesterol decreases cell membrane permeability to small water-soluble molecules.

20. Steroids

21. Organic Compounds Steroids Parent compound is cholesterol.
Used for the production of steroid hormones.
Can dissolve in fatty substances.
Dissolves through cell membrane and nuclear membrane and attaches directly to DNA
Starts Transcription of proteins
Such as enzymes
Cholesterol can be produced through de-novo synthesis

22. Organic Compounds Proteins
composes 10 – 30% of cell mass and is the basic structural material of the body.
Some are structural.
Bones, hair, connective tissue
Some are functional.
Antibodies, enzymes, protein hormones

24. Amino Acids

25. Organic Compounds Amino acids. The Building Blocks of Protein
Composed of
an amine groups
a carboxyl group
a “R” or Functional group.
20 different types of amino acids
9 Essential
Must acquire these through the foods we eat
11 Non-essential
Can be produced through de-novo synthesis

26. Peptide Bond

27. Peptide Bonds
Most proteins contain from 1500 to 50,000 amino acids in the human body.

28. Primary Structure of a Polypeptide Chain28

29. Conformation
Interactions between side groups of each amino acid leads to bending, twisting, and folding of the chain into a more compact structure.
The final shape of a protein is known as its conformation. 29

30. Amino acid interactions30

31. Polypeptides: Conformations

32. Hemoglobin 32

33. Proteins
Hydrogen bonds form and break quickly and can thereby change the protein shape and its function

34. Protein Structure Globular Proteins Compact, spherical proteins
Have tertiary or quaternary structures
Also known as functional proteins
Antibodies
Hormones
Enzymes (catalysts)
Membrane Transporters
DNA Regulatory Proteins for transcription

35. Proteins Fibrous proteins are stable.
Globular proteins are very unstable.
Hydrogen bonds can form and break easily.
Hydrogen bonds can break when:
A PO4 group is added

37. Adenosine Triphosphate
The transfer of a high energy phosphate group to an enzyme causes a change in confirmation
The change in enzyme shape allows the enzyme to quickly catalyze the reaction

39. Protein Structure Change in shape of protein = Denatured
Change in conformation =
Change in configuration
Denatured
When globular proteins lose their shape they can’t perform their function any longer.
pH drops.
Temperature rises above normal levels.

40. Enzymes Enzymes are globular proteins that act as catalysts.
A catalyst speeds up a chemical reaction but it itself is not used up
Enzymes are recycled
The function of a globular protein depends on the arrangement of the atoms

41. Mechanism of Enzymes Three Basic Steps
The Enzyme binds with a substrate at its active site.
The Enzyme-Substrate Complex is rearranged to form a product.
The Enzyme releases the product and goes back to its original shape
The Enzyme can be used again to catalyze another reaction

42. Enzymes
The job of an enzyme is to lower the activation energy
Some enzymes carry a helper of “cofactor” such as iron or copper.
Vitamins, especially B complex.

43. Feedback Inhibition of Biochemical Pathways

44. Activation Energy
Fig 4-3

45. Some more characteristics of enzymes:
Usually end in –ase
Inactive form: -ogen

46. Naming of Enzymes mostly suffix -ase first part gives info on function
examples
Kinase
Phosphatase
Peptidase
Dehydrogenase

47. Protein Molecules Specificity
The ability of a protein to bind to a certain ligand or a group of related ligands
Some proteins are very specific about the ligands they bind, others bind to whole groups of molecules

48. Affinity
The degree to which a protein is attracted to a ligand is referred to as its Affinity.
High affinity proteins are more likely to bind a certain molecule than a low affinity protein