AP Bio Unit 1 Test

All good science starts with what two things

An observation and a testable question

Null Hypothesis

States that IV has no effect on the DB, assumed to be correct unless statistical analysis of the data contradicts it

Alternate Hypothesis

Normal hypothesis, prediction about the results of the experiment

Independent variable

Variable that is manipulated or changed, variable will vary between experiment groups

Dependent variable

Variable that changes in response to the IV, what is being measured throughout an experiment, IV affects change in the DV

Positive Control Group

Group with the normal amount/type of IV

Negative Control Group

Group that does not receive the IV

Qualitative Data

Observations that cannot be numerically expressed

Quantitative Data

Discrete, measurable units that are numerically expressed

LUTES

Label your axes, use the right graph type, title the graph, error bars, scale your axes properly

Dependent variable on which axis

Y

Independent variable on which axis

X

True mean

Average value for data taken from every member of a population

Sample mean

Averages of data points within individual experimental groups. Used to compare averages between treatment types

Standard Deviation

Quantifies amount of variation in a set, WITHIN a sample

Data falls between ± 1 SD

Not considered significantly different than the mean

Data falls between ± 2 SD

Considered significantly different than the mean

Smaller you Standard Error of the Mean

More likely it is that your sample mean matches the true mean and represents the population as a whole

Error bars represent (± 2 SEM)

Values between which the true mean could fall

If the error bars DO NOT overlap

Differences in sample means are statistically significant

If the error bars OVERLAP

Differences in the sample means are NOT statistically significant

Degree of freedom

Number of categories MINUS 1

P-value in AP Bio

0.05

If chi-square is > than the critical value

we REJECT the null hypothesis

If chi-square is < than the critical value

we FAIL TO REJECT null hypothesis

Cohesion of water molecules

Water molecules sticking together (ex: surface tension)

Why water has all of it’s properties

Polarity and hydrogen bonds

Adhesion

Water’s ability to stick to other things (ex: capillary action)

Why is water polar

Differences in electronegativity, electrons are shared unequally, positive and negative regions created

Cations

Have a positive charge

Anions

Have a negative charge

Carbon

EVERY biomolecule, can form up to four bonds CH4

Nitrogen

Proteins and nucleic acids

Phosphorus

Nucleic acids and certain types of lipids (phospholipids)

Hydrogen

EVERY biomolecule

Oxygen

EVERY biomolecule

Electronegativity

How strongly atoms attract bonding electrons to themselves

Fluorine electronegativity

Most electronegative one (use this to remember the trends)

Electro positivity

A measurement of the ability of elements to donate electrons and form positive ions, low electronegativity

Covalent bonds

Sharing electrons

Ionic bonds

Transfer of electrons

Polar molecules charge

Overall neutral, electronegative element is partially negative and electropositive element is partially positive

Four biomolecules

Carbohydrates, lipids, proteins, nucleic acids

Catabolism

Catabolic reactions break down biological polymers into monomers to help generate ATP

Anabolism

The body builds complex molecules from smaller, simpler ones

Dehydration synthesis

Anabolic, removes water to make a bond between monomers, water is left over

Hydrolysis

Catabolic, breaks polymers using water

Carbohydrates monomers and polymers

Monosarrachides and polysaccharides

Functions of carbs

Short term energy storage

Carbs elemental composition

Carbon, hydrogen, oxygen

Energy storing carbs vs structural carbs shape

Branches vs linear structure that is able to stack

Lipids monomers

Fatty acids

Lipids function

Long term energy storage

Lipid elemental composition

Carbon, Hydrogen, Oxygen

Lipids are what property to avoid water

Hydrophobic

Saturate fats

Do not have double bonds in their molecular structure

Unsaturated fats

Do have double bonds in their molecular structure

What biomolecules are broken down in body for energy

Lipids, carbs, and proteins

Nucleic acids monomers and polymers

Nucleotides, nucleic acids

3 parts of a nucleotide

Sugar, phosphate, nitrogenous base

Nucleic acids elemental composition

Carbon, hydrogen, oxygen, nitrogen, and phosphorus

Nucleic acids functions

Storage of genetic material

DNA differences from RNA

Linear double stranded helix, stores genetic code, has thymine, deoxyribose sugar, more stable than RNA, found in nucleus

RNA differences from DNA

Single stranded, used for protein synthesis, has uracil, ribose sugar, less stable than DNA, found in nucleus and cytoplasm

Proteins monomers and polymers

Amino acids, polypeptides

Proteins elemental composition

Carbon, hydrogen, oxygen, nitrogen, and sulfur

Proteins main function

Wounds and tissue repair

Enzymes

Specialized proteins that speed up chemical reactions in cells to help maintain homeostasis

4 levels of protein structure

Primary, secondary, tertiary, quaternary (all build on each other)

N terminus protein

First amino acid in the chain

C terminus protein

Last amino acid in the chain

All proteins have what structures

Primary, secondary, and tertiary

Only difference between each of amino acids

Structure and chemical properties of the R side chain (could be hydrophobic, hydrophilic, acidic, or basic)

Primary structure protein

Sequence of amino acids formed by dehydration synthesis, determines how protein folds on all levels

Peptide bond is what type of bond

Covalent

Peptide bond forms where

Carboxyl group and amine group of two amino acids

Secondary structure protein

Alpha helices, beta pleated sheets, held with hydrogen bonding, no r-groups involved

Tertiary structure protein

Protein finishes folding, usually functional now, controlled by interactions between R side chains on amino acids

R group interactions

Hydrogen bonds between side chains, charge attraction between acidic and basic charges, disulfide bridges are covalent bonds between sulfur atoms (very strong), the more disulfide bridges there are the stronger the structure

Quarternary structure proteins

Multiple teritaries put together, not all proteins are involved in these structures