organic compounds quiz

null hypothesis

a statement that says how the independent variable would have no effect on the dependent, or how there is no real efect or relationship between the variables you’re testing PURELY DUE TO CHANCE

rejecting the null hypothesis

your critical value is greater than x², meaning there is a likely chance that there is a relationship and that it was not a random fluke

the p value 0.05 means…

the number that measures how likely it is your data occurred by random chance

If x² value is smaller than the critical value…

you are accepting the null, saying that there is not a statistically significant difference between the observed and expected values, accepting the null

Overlapping sem bars mean…

not statistically significant, goes up and down Standard errors of mean, which show how accurate your calculated sample average is compared to the actual true population

Dehydration synthesis other name is

condensation reaction

How does dehydration synthesis/ condensation reaction work?

add up monomers to create polymers by removing a water molecule (monomer + monomer= polymer +h20)

How does hydrolysis work?

breaks down polymer into monomers by adding a water molecule (polymer +water= monomer +monomer)

Carbohydrates

short term energy and fueld (2 though are for building material)

-includes simple sugar like fructose and polymers like starch

What is the ratio for a carb?

1 carbon: 2 hydrogens: 1 oxygen or CH20

What are monosaccharides

they are the monomers of carbs, the simplest form often called simple sugar , like glucose or ribose

What are polysaccharides and examples for storage and structure?

-ong chains of monosaccharides linked by covalent bonds

-For storage in plants, starch is used and for storage in animals glycogen is used

-For structure in plants, cellulose is used, and for structure in arthropods, chitin is used (chitin builds the exoskeleton for them)

Starch, glycogen, cellulose, and chitin are all made of what

glucose

How do you classify carbs/ specifically monosaccharides

-by their structural shape and exact number of carbon atoms they contain

What is it about carbon atoms at the corner of chemical structure rings?

They are implied, representing one carbon each

Digestibility: Starch vs cellulose

Starch is digestible by humans like rice and wheat, while cellulose is not

Lipids 3 categories

-fats

-steroids

-phospholipids

Fats

-also known as triglycerides, made up of 3 fatty acid tails and glycerol

-long term energy storage and provide insulation

Saturated fats

-long hydrocarbon chain saturated with hydrogen atoms

How are saturated fats found in room temp and wehre are they found?

• solid at room temp like butter and lard

• found in animals

• only single bonds, so its a straight line

unsaturated/ polyunsaturated fats

contain one or more carbon to carbon double bond, causing it to bend or kink, preventing molecules from being tightly packed together

What form is unsaturated/ polyunsaturated fats like in room temp/ where is it found?

-primarily found in plants, liquid at room temp as corn oil/ olive oil

Steroids

characterized by 4 fused carbon rings, one example being cholesterol and hormones

Phospholipids

Build a cell membrane of every living cell on earth, the hydrophobic tails pointing inward and the hydrophilic tials pointing outward

Phospholipid from top to bottom is

choline, then phosphate, then glycerol, then fatty acids

-head (glycerol +phosphate group), tail fatty acids (hydrophobic)

Proteins main functions

1. speed up chemical reactions (enzymes, lactase)

2. defense (antibodies)

3. storage (like breast milk storing casein)

4. transport (hemoglobin to oxygen)

5. cell communication (hormones and receptors)

6. movement (actin/ myosin)

7. structure (keratin/ collagen)

Amino acids parts

• the monomers of proteins

• made of a central carbon

• the amino part NH2, which is always positively charged

• acid part COOH, always charged negatively

• R group: side chain

Properties:

could be hydrophilic, hydrophobic, and charged (hydrophilic)

Nonpolar (Hydrophobic) Side Chains

Made almost entirely of carbon and hydrogen atoms, H3N+ is the one outlier to that, a tonof CH3 or CH2

Polar, Uncharged (Hydrophilic) Side Chains

Contains carbon and hydrogen, but features electronegative atoms like Oxygen, nitrogen, sulfur, CONTAIN HYDROXIDE TYPICALLY OR N

Electrically Charged (Hydrophilic) Side Chains

look directly at the ends of the R-group (the side chain) for a permanent plus (+) or minus (-) sign. like not just the horizontal negative 0, the upper attachment having some part sticking out with a charge

Level 1 of protein structure:

Primary

• a peptide bond links the amino acids, forming the polymer version called a polypeptide

• This sequence is essential as if even 1 letter changes, it may stop working or completely alter the type of protein

Whats an example of the important of the order of amino acids?

Sickle cell disease—one amino acid change in hemoglobin alters its shape and function, causing red blood cells to become sickle-shaped.

The Peptide bond formation:

the chain has 2 ends:

-N-terminus = end with a free amino group (NH₂)

• C-terminus = end with a free carboxyl group (COOH)

• New amino acids are added only to the C-terminus, so the protein chain grows N → C.

• ONLY GROWS IN ONE DIRECTION

Secondary (zooming out)

• Local folding of the polypeptide chain into patterns

• Caused by hydrogen bonds between the backbone C=O and N–H groups

• R groups are NOT involved

• 2 types:

  1. α-helix → coiled/spiral shape

  2. β-pleated sheet → folded, sheet-like shape

⚠ Small correction: it’s C=O and N–H, not CH₂ and COOH.

What are R groups?

R groups are the variable side chains attached to each amino acid.

• changes from one amino acid to another

• “rest of the molecule”

Tertiary

• Entire polypeptide folds into its 3D shape

• Caused by interactions between R groups (side chains)

• R groups interact based on their polar, nonpolar, and charged properties

• Types of interactions:

  • Hydrogen bonds

  • Ionic bonds

  • Disulfide bridges

  • Van der Waals interactions

• A protein can have multiple types of interactions at the same time

Basic Principles of Protein Folding

A. Hydrophobic amino acids → inside

• Hydrophobic = water-fearing

• They avoid water, so they tend to bury themselves inside the protein.

• This is called a hydrophobic interaction.

BPOPF 2

B. Hydrophilic amino acids → outside

• Hydrophilic = water-loving

• They tend to stay on the outside, where they can interact with water.

• They can form hydrogen bonds with water and other polar molecules.

BPOPF 3 & 4

• Acidic + basic amino acids → ionic bonds

• Two sulfhydryl (–SH) groups → disulfide bonds

Disulfide bridges:

-covalent cross between sulfhydryls

-these stabilize the 3D structure (less branching out more compact)

Quaternary (doesn’t always get to this point)

-2+ polypeptides bond together

-only then is protein functional

- higher likelihood of them bonding together when highly functional

-goes amino acid to polypeptide to protein

Denaturation

-the proteins structure or function is sensitive to chemical / physical conditions

so if the pH, temp, and salinity (salt content) are not optimal or typically too high , denatures or unfolding

-this is irreversible practically

Nucleic Acids

Function: to store and express hereditary information

DNA

-doubles stranded helix , stores genetic information

Nitrogen bases of adenine, guanine, cytosine, and thymine

-the longer larger sister, sugar (deoxyribose)

RNA

-single stranded, carries info from DNA to the ribosomes

N bases are adenine, guanine, cytosine, and uracil

-types include tRNA, rRNA, and mRNA, and the sugar is ribose

Nucleotides

the monomer of DNA / RNA

-made up of a sugar, nitrogen base, and phosphate group

Info flow into a cell goes…

DNA to RNA to protein

The nitrogen base bonds are…

A-T or G-C

Purines

adenine and guanine (double ring)

pyrimidines

cytosine, thymine (DNA), uracil (RNA) (single ringed)

Dehydration synthesis

joining molecules together by removing water (H₂O).

monomer +monomer= polymer + h20

enzymatic proteins

Accel certain chemical reactions

Defensive proteins

protection against disease

storage proteins

store amino acids, casein is an example of the protein of milk

hormonal proteins

coordination of an organisms activities

receptor proteins

response of cell to chemical stimuli