1. Comparison of Ionic, Polar Covalent, and Nonpolar Covalent Bonds

2. Formation of an Ionic Bond
A valance electron from Na is transferred to Cl
Cl now has 18e and 17p resulting in a – charge
Na has 10e and 11P resulting in a + charge.

3. Nonpolar and Polar Covalent Bonds
Non polar covalent Bonds equally share electrons
Polar covalent bonds share electrons unequally

4. Hydrogen Bonds Too weak to bind atoms together
(intra-molecular bonds= within molecule)
Important as inter-molecular bonds
between to different molecules
Important for giving proteins (enzymes) and DNA both shape and functionality.
Hold water molecules together
Responsible for surface tension in water

5. Hydrogen Bonds in Water

6. Hydrogen Bonds

7. Properties of Water Water makes up to 50-80% of all living cells.
Water stabilizes internal temperature of the body
Hydrogen bonds stabilize large shifts in temperature
Evaporate cooling (sweating) is critical from maintaining 98.6 degrees temperature in hot environments or increased physical workloads.
Water is necessary for all biochemical reactions that take place in the body.

8. Polarity of Water Oxygen has a greater electronegativity.
Hydrogen’s one electron spend more time in Oxygen's outermost energy level.
The result is more electrons around the oxygen making it more negative.
Hydrogen losses its electron. Its proton is unopposed making it more positive.

9. Properties of Water Water makes up to 50-80% of all living cells.
Water stabilizes internal temperature of the body
Hydrogen bonds stabilize large shifts in temperature
Evaporate cooling (sweating) is critical for maintaining 98.6 degrees temperature in hot environments or increased physical workloads.
Water is necessary for all biochemical reactions that take place in the body.

10. Properties of Water
Water is a powerful splitting agent. (Hydrolysis) means water splitting. Occurs in breaking down reactions
Is known as the universal solvent. ( Polarity allows it to dissolve stuff.) water molecules slit the ionic bonds in Na+Cl-

11. Polarity
Polar molecules associate with water and will dissociate from lipids (fats) .
Polar = hydrophilic (philic = loving)
Lipophobic (lipid fearing)
Non-polar molecules associate with lipids will not associate with water and are considered to be
Non-polar = hydrophobic (water fearing)
Lipophilic= Lipid loving

12. Organic Compounds Organic compounds contain carbon as the backbone.
It has the ability to create 4 covalent bonds which is important for making large complex structures.
Organic compounds include :
Carbohydrates (sugars)
Lipids (fats and oils)
Proteins ( muscle, enzymes)
Nucleic acids (DNA and RNA)
They may be built up or broken down depending on what the system requires.
May have a variety of functional groups

13. 7

14. 8

15. Dehydration Synthesis
Dehydrate( remove water)/ Synthesis( Build)
Monomers bond together to form a polymer with the removal of a water molecule (dehydration)
Removal OH– of one and H+ of the other hydroxyl group forms the water.
A covalent bond will result.

16. Hydrolysis Translates into Water/splitting
Addition of a water to a polymer causes (lysis) of the covalent bond joining the 2 monomers.
Reestablishes the hydroxyl groups in both monomers
All digestion reactions consists of hydrolysis reactions

17. Monomers/Polymers nucleotides DNA, RNA Carbohydrates Fats (lipids)
Monosaccharides Polysaccharides
Fats (lipids)
Glycerol + 3 fatty Acids Triglycerides
Protein
Amino acids Polypeptide
Nucleic Acids
nucleotides DNA, RNA
Dehydration Synthesis
Hydrolysis

18. Carbohydrates
Hydrophilic organic molecule that : contain carbon, hydrogen, and oxygen 1:2:1 atomic ratio( carbo/carbon:hydrate/H2O)
i.e. glucose = C6H12O6
Names of carbohydrates
word root sacchar- or the suffix -ose often used
Glucose is a monosaccharide which functions as a major fuel source for the cells.

19. Carbohydrates
Dehydration synthesis reactions allow the cell store excess carbohydrates in the form of glycogen.
Hydrolysis reactions allow the cell to break the bonds holding the polysaccharide together allowing it to release more simple sugars.

20. Disaccharides Major disaccharides sucrose = table sugar
glucose + fructose
Lactose = sugar in milk
glucose + galactose
Maltose = grain products
glucose + glucose
All digested carbohydrates converted to glucose broken down in ATP (Cellular fuel).

21. Glycogen
Glycogen is an energy storage polysaccharide produced by animals. 2 storage sites:
Liver cell: synthesize glycogen after a meal which can be broken down later to maintains blood glucose levels.
Muscle cells: Store glycogen within the muscle at is only used by the muscle cell.

22. Starch and Cellulose
Starch: is the storage form of sugar produced by plants. We produce an enzyme that breaks the bonds between the sugars allowing digestion to occur. i.e. potatoes and grains
Cellulose: provides structure to plants but contains a different type of bond. The β form is insoluble because we don’t produce the enzyme .i.e. dietary fiber

23. Lipids Hydrophobic organic molecule Chain of 4 to 24 carbon atoms
Composed of carbon, hydrogen and oxygen
Better fuel source since it contains many more carbon and hydrogen molecules.
There is an unlimited supply.
Chain of 4 to 24 carbon atoms
carboxyl (acid) group on one end, methyl group on the other and hydrogen bonded along the sides
Classified
saturated - carbon atoms saturated with hydrogen
unsaturated - contains C=C bonds without hydrogen

24. Lipids Found in the Body
Neutral fats – found in subcutaneous tissue and around organs.
Phospholipids – chief component of cell membranes
Steroids – cholesterol, bile salts, vitamin D, sex hormones, and adrenal cortical hormones
Eicosanoids – prostaglandins, leukotrienes, and thromboxanes:
These play a role in various reactions in the body such as inflammation and immunity.
Lipoproteins – transport fatty acids and cholesterol in the bloodstream
Fat-soluble vitamins – A,D, E, and K

25. Triglycerides Functions energy storage in adipose (fat) tissue
Fats contain 9 kcal per gram where as carbohydrates and proteins contain 4 kcal per gram.
They contain more energy rich hydrogen.
insulation
Prevent heat loss from the body
protection
Adipose tissue cushions the organs.

26. Triglycerides (Neutral Fats)
Contain C, H, and O, but the proportion of oxygen in lipids is less than in carbohydrates 3
Fatty acids are bonded to a glycerol molecule during dehydration synthesis.
At room temperature : Contain double bonds.
when liquid called oils
often mono and polyunsaturated fats from plants
when solid called fat
saturated fats from animals.
No double bonds.
Function - energy storage, insulation and shock absorption

27. Neutral Fats (Triglycerides)
Composed of three fatty acids bonded to a glycerol molecule

28. Phospholipids
Modified triglycerides with two fatty acid groups and a phosphorus group

29. Protein Functions Catalysts
proteins which are enzymes significantly increase the rate of a chemical reaction i.e. Salivary Amylase increases the rate of hydrolysis of starch.
Structural
hold the parts of the body together i.e. collagen, elastin and keratin
Communication
act as chemical messengers between body areas .i.e. hormones such as insulin.
Transport
allow substances to enter/exit cells
Carry things in the blood i.e. hemoglobin, lipoproteins,

30. Protein Functions Movement
Actin and myosin function in muscle contraction
Defense
Antibodies( immunoglobulins) recognize and inactivate foreign invaders( bacteria, toxins, and some viruses)
Metabolism
Help regulate metabolic activities, growth and development
Regulation of pH
Plasma proteins such as albumin can function both as an acid or a base. Therefore have an important role as a buffer

31. Amino Acids Structure Building blocks of protein
Amino and carboxyl group groups are common in all Amino acids.
R-group (radical group): 20 amino acids are different both structurally and from a functional level.

32. Different R- groups

33. Protein
Macromolecules composed of combinations of 20 types of amino acids bound together with peptide bonds
Animal ,dairy and right combination of beans and rice are good sources of protein.
Enzymes are specific types to proteins that enable reactions.

34. Protein Structure Primary structure
amino acid linked together by peptide bonds. The order of the amino acids critical for both form and function. No hydrogen bonds formed.
Secondary structure :The primary structure will now form hydrogen bonds and take one of 2 forms:
α helix (coiled), β-pleated sheet (folded)
Tertiary structure
more hydrogen bonds form and increased interaction between R groups in surrounding water results in protein taking a globular 3 dimensional shape.
Quaternary structure
two or more separate polypeptide chains conjugate and form a functional protein
Hemoglobin.

35. Structural Levels of Proteins
Primary – amino acid sequence
Secondary – alpha helices or beta pleated sheets

36. Structural Levels of Proteins
Tertiary – superimposed folding of secondary structures
Most enzymes are in this form.
Quaternary – polypeptide chains linked together in a specific manner

38. Functional Proteins (Enzymes)
Enzymes are chemically specific. They fit a specific substrate like a lock and key.
Enzyme names usually end in –ase
for example Lactase will be specific for the substrate lactose ( Glucose Galactose)
Gycosidic bond
Frequently named for the type of reaction they catalyze i.e. hydrolases add water during hydrolysis reactions.
lipase/lipids, protease/ proteins,
Act as biological catalysts which lower activation energy allowing reactions to occur at faster rates.

39. Activation Energy
Activation energy refers to the extra energy required to break an existing chemical bonds and initiate a chemical reaction.
Activation energy determines rate of reaction (higher activation energy = slower reaction)
catalyst - substance that lowers the activation energy by influencing (stressing) chemical bonds

40. Characteristics of Enzymes

41. Enzymatic Reaction Steps

42. Enzyme Substrate Complex
Enzymes need their 3 dimensional structure
created by both Hydrogen and disulfide bonds which is specific to a certain substrate.
Proper conditions are needed to keep these enzymes functioning. pH
Temperature

43. Protein Denuaturation
Hydrogen bonds are broken and tertiary level protein reverts back to primary structure. Peptide bonds are still intact.

44. Protein Denuaturation
Proteins will become denatured if:
∆ pH
↑ temperature
Hydrogen bonds are broken from complex tertiary level proteins to basic primary structure.
Peptide bonds are still intact.
Visible changes you see when frying an egg

45. Nucleic Acids Two major classes – DNA and RNA
Composed of carbon, oxygen, hydrogen, nitrogen, and phosphorus
Five nitrogen bases contribute to nucleotide structure
Adenine (A) Thymine (T)
Guanine (G) Cytosine (C)
Uracil (U) replaces Thymine in RNA

46. Nucleotides The structural unit of the a nucleotide is composed of
N-containing base A,T,C,G and U in RNA
Pentose sugar: Ribose, and deoxyribose
Phosphate group

47. Deoxyribonucleic Acid (DNA)
Double-stranded helical molecule confined in the nucleus of the cell
Helical shape is a result of H-bonds between a purine on one strand and a pyramidine on the other strand
A only pairs with T
G only pairs with C
Replicates itself before the cell divides, ensuring genetic continuity
Provides instructions for protein synthesis

48. Structure of DNA

49. Structure of DNA

50. Ribonucleic Acid (RNA)
Single-stranded molecule
Made from the nucleotides that complimentary pair
A U G C
Three varieties of RNA:
messenger RNA: transcribe DNA and carry it out of nucleus.
transfer RNA: Bring amino acids to site of protein synthesis (ribosome).
ribosomal RNA: building blocks of ribosomes ,made in the nucleolus

51. Adenosine Triphosphate (ATP)
Adenine-containing RNA nucleotide with three phosphate groups
Second and third phosphate groups are attached by high energy covalent bonds
The 3rd high energy phosphate bond of ATP is hydrolyzed producing ADP + P + energy
The cell can recycle the ADP and P back into ATP using the energy harvested from dietary foods primarily carbohydrates and lipids.
Source of immediately usable energy for the cell.
It is the currency that all cellular reactions accept.

52. Adenosine Triphosphate (ATP)
Figure 2.22

53. How ATP Drives Cellular Work
Figure 2.23