ap bio unit one notes

Nucleic acid: phosphate group, sugar, nitrogenous base

Protein: carboxyl group, essential carbon with an r group, amino group (lots of amino acids come together to make a polypeptide, which is the same thing as a protein - peptide bonds)

If there’s nitrogen it’s either protein or nucleic acid

Lipids: 3 different things - have 3 tails of fatty acids (triglyceride), two tails (phospholipid), 4 fused rings together (steroid)

Glycerol is the backbone that you attach things to (like tails)

Lipids don’t have monomers or polymers

Carbs: CHO, either a line with a lot of OHs or rings

-OH hydroxyl

-NH2 amino

-COOH carboxyl

-CO…. Carbonyl

P and stuff around it phosphate group (no carbon)

Hydrophilic Amino Acids:

+/-

N-H

O-H

F-H

Hydrolysis breaks things

Dehydration synthesis bonds things

Connect amino acids - peptide bonds

Connect two monosaccharides - glycoside linkage

Connect two nucleic acids - phosphodiester link

Connect nucleotides from 3’ - 5’

Head of a phospholipid is polar because the head of the phospholipid is charged and water likes charged things, tails are nonpolar - can have unsaturated or saturated tails

Unsaturated = double bonds

bent/Kink in it

Takes up more room

Liquid at room temperature

Olive oil

Saturated = no double bonds

Straight lines

Takes up less room

more dense

More likely to be solid at room temperature

Butter

DNA: deoxyribose so it has H instead of OH (de-oxy(gen))

A C T G

RNA: ribose so it has two OH groups

Uracil

Protein structure:

Primary is determined by which amino acids we use in what order (long chain) (swapping them out)

…………….

Secondary is influenced by the hydrogen bonding and the backbone

alpha - spiral

Beta - zigzag

Tertiary folding is determined by how the different side chains interact

Disulfide bridge

Question - covalent bonds increase stability between folds and last longer inside the cell

Hydrophobic interactions helps the things that don’t like water fold on the inside, but the disulfide bridge is way stronger so it overrides the hydrophobic interactions

If one amino acid gets swapped out then it might end up in a very different spot - wouldn’t affect secondary because secondary has nothing to do with the backbones, but it would affect tertiary because that’s all about the backbone and side chains

Quaternary is two separate chains held together

Covalent bonds = STRONGGG

Cysteine = amino acid that does the sulfide briding

Cytosine = nucleotide found in DNA and RNA

3 I have to know:

Standard deviation describes where the data from your experiment is (with just a sample of people)

Xi - individual data point

X- average

N-1 - degrees of freedom

Standard error describes where the real average likely is if you did the experiment a bunch of times (with the entire population)

You have to get standard deviation to get standard error

Chi-squared tells us when something is so wrong that there’s a connection (eg blonde girls at academy)

Overlapping error bars - you can’t say it’s different because you don’t really know

If it’s two degrees of freedom and it’s OVER 5.99, you reject the null hypothesis because that’s crazy there’s almost no chance of that randomly happening

If it’s below

If it’s two degrees of freedom and it’s UNDER 5.99, you fail to reject the null hypothesis because what happened was what should’ve happened and/or it wasn’t crazy wrong

LEARN FAIL TO REJECT AND REJECT - NEVER NEVER NEVER ACCEPT AND

ALWAYS USE 0.05

HIGHER = REJECT

DNA has thymine, RNA has uracil - rest are same

Starch is used for energy

Cellulose is used for structure