AP Bio AP Exam Masterdoc

quantitive data

numerical data

qualitative data

data collected by senses usually should be converted into qualitative

inductive reasoning

specific to general conclusions

deductive reasoning

general to specific conclusions

Hypothesis

Testable idea about how something works

Scientific law

Universal scientific fact

Theory

Summarizes a group of hypotheses

Null hypothesis

hypothesis that research aims to disprove; claims there is no correlation between variables

Alternative hypothesis

Hypotheses that explore different relationships between variables

Variables

Things that change

Constants

Things that don’t change

Independent variable

Factor deliberately changed

Dependent variable

Factor being measured, changes depending on independent variable

Controls

Eliminates error in experiments, increases reliability. Positive=exposed to treatment known to produce a certain effect; Negative=no treatment, known to produce no effect

Mean

Average value

Median

Middle/most value

Mode

Most frequent value

Standard deviation (s)

How data is spread from the mean; high SD= more spread out; low SD= less spread out

Standard error of the mean (SEM)

Confidence in the mean. how precise is it? Low SE=more confidence

Bar graph and error bars

Overlapping error bars=difference isn’t significant

Chi

square

How to find SD

Find mean, Mean: each data point, Square (mean to data point), Add up all values of step 3, Divide by degrees of freedom (n

How to find chi square

Expected given: Each observed minus expected, Square each (observed minus expected), Divide each by each expected, Add up all values, Compare with critical value

How to find chi square with no expectant given

Find expected value by (column total * row total divided by total total) for each value, Continue as normal

chi square results

larger = reject null significant relationship between variables; smaller = opposite larger

macromolecules

Four types: carbohydrates, proteins, lipids, and nucleic acids

Organic compound

molecules containing carbon

CHNOPS

carbon, hydrogen, nitrogen, oxygen, phosphorus, sulfur

protein

made of CHONS

carbohydrate

made of CHO

lipid

made of CHOP, all nonpolar, no specific monomers/polymers

nucleic acid

made of CHONP (nitrogenous base and phosphate group)

monomer

single unit of macromolecule

polymer

more than one unit of a macromolecule

dehydration synthesis

removes a water molecule to bond two monomers together

hydrolysis

breaks down polymer by adding water molecule

glycosidic linkage

the covalent bond between monosaccharides

monosaccharide

monomer of carbohydrates

disaccharide

two monosaccharides

polysaccharides

polymer of carbohydrates

linear

chain of monomers

branched

when nonlinear chain of monomers bonds to create a tree

rings

many simple sugars exist in this form usually monosaccharides

cellulose

structural carbohydrate found in cell wall, hard to break down because linear chain

starch

storage carbohydrate in plants, easier to break down because it's slightly branched

glycogen

storage carbohydrate in animals, easy to break down because it's very branched

fatty acid

a long chain of hydrocarbons

saturated

fatty acid with no double bond, solid at room temp

unsaturated

fatty acid that has double bond, liquid at room temp

glycerol

carbohydrate involved in fatty acids and phospholipids

triglyceride

fat made of glycerol and 3 fatty acids

phospholipid

hydrophilic head, hydrophobic tail, glycerol backbone

amphipathic

having both hydrophilic and hydrophobic parts

cell membrane (phospholipid bilayer)

made of phospholipids, hydrophobic tails face each other and the heads face outward

ester bond

bond between lipids

steroid

lipid, four rings

cholesterol

lipid in the bilayer that allows for fluidity

amino acid

building block/monomer of proteins

amino or N terminus

one functional group of an amino acid

carboxyl or C terminus

the other functional group of an amino acid where new amino acids are added

central carbon

middle part of amino acid

R group/side chain

variable group, several options, makes the amino acid unique

dipeptide

two amino acids

polypeptide

polymer of proteins

peptide bonds

covalent bond between amino acids

protein backbone

chain of amino acids, peptide bonded

secondary structure

backbone held together with hydrogen bonds, slight bending due to interactions between carboxyl and amino terminus

alpha helix

spiral of amino acid chain founding secondary structure

beta sheet

pleated chain found in secondary structure

tertiary structure

3D shape determined by polarity of R group

disulfide bond

bond between cysteine chains, seen in protein folding

hydrophobic interactions

when the R groups are hydrophobic they fold inside the structure away from aqueous solution

quartenary structure

not all have this, only when a protein has more than one chain, large 3D structure as amino acids interact

antibody

type of protein that targets antigens

enzyme

types of proteins that catalyze or speed up reactions

nucleotide

monomer for nucleic acids, pairs are held together by hydrogen bonds

phosphodiester bond

bond between nucleotides

sugar

five carbon sugar (either ribose or deoxyribose)

phosphate

one part of a nucleotide, is negatively charged which gives DNA a negative charge

nitrogenous base

adenine, guanine, thymine, cytosine, uracil

deoxyribose

DNA sugar base

ribose

RNA sugar base

DNA

double stranded

RNA

single stranded

5'

phosphate group end

3'

hydroxyl group end/near sugar

antiparallel

DNA runs 5' to 3' prime in both directions

pyrimidine

one ring, thymine, uracil, and cytosine

purine

double ring, adenine and guanine

cytosine

pairs with guanine, pyrimidine base, has 3 hydrogen bonds and is harder to break

guanine

pairs with cytosine, pyrimidine base, has 3 hydrogen bonds and is harder to break

adenine

pairs with thymine/uracil, purine base, 2 hydrogen bonds and is easier to break

thymine

pairs with adenine, purine base, has 2 hydrogen bonds and is easier to break

uracil

pairs with adenine, purine base, has 2 hydrogen bonds and is easier to break

ATP

RNA monomer

aqueous

water solvent

role of carbon in biological systems

the backbone of organic molecules, which are essential for life. Its ability to form stable bonds with various elements and itself allows for the creation of a vast array of complex molecules, including proteins, nucleic acids, carbohydrates, and lipids. These molecules are crucial for energy storage, structural support, genetic information, and cellular processes.

For each type of biological macromolecule: Identify the monomer, polymer, general structure, functions, examples, and the elements that typically make up that type of macromolecule

Carbs: Monosaccharides, polysaccharides, rings or branched chains, usually acts as sugars, examples glucose and starch, CHO Proteins= amino acids, polypeptides, four types of structures, have specific functions throughout the body, example enzyme,

Identify the type of macromolecule when given its chemical structure

Carbs=CHO; Proteins=CHONS; Lipid=CHOP; Nucleic acid=CHONP

Explain what dehydration synthesis is and the types of covalent bonds formed between monomers of the different types of macromolecules

Dehydration synthesis= when a water molecule is removed to bond two monomers; Proteins=peptide bonds; Carbs=glycosidic linkages; Nucleic acids=phosphodiester bonds; Lipids=ester bonds