Bio 210 Exam1 prep

CSUMB Prof. Greg Tyson

Inductive reasoning

IN- specific observations to a broad general rule

ex. all three apples in your bag are sour so you conclude that they are all sour in your bag

Deductive Reasoning

general rule to specific conclusion

ex. all dogs are mammal, buster is a dog so buster is a mammal

Scientific method

ask a question → do background research → form hypothesis (testable) → conduct experiment → analyze data → draw conclusion

this is not a simple process

Biological Organization

Atom- Hydrogen, Oxygen

small molecule- water, carbon dioxide

Large molecule (aka Macromolecule)- DNA/RNA proteins, complex carbs, lipids

Cells- red blood cells, nervous cells, bacteria

Organisms- human, dog, tree

Features of life (with examples)

common set of chemical compounds

made up of cells

extract energy from the enviroment adn use it to do work

regulate internal enviroments

genetic info

exist in populations that evolve over time

Life

Composed of cells, has DNA, involvesenergy transfer and transformation, that life interacts as part of ecosystem, and that evolution is the central idea fundemental to biology

Three domains of life

eukaria

bacteria

archaea

Natural selection

organisms with traits best suited for their envirormoent are more likely to survive and reproduce more over time

How do you group things together on a phylogenetic tree

shared characteristics and DNA sequences

Why do we use model systems

1. similarities between organisms from common desent → make predictions about pheno0menoms that can be applicable to other organisms

2. studying biological processes in organisms are easier to work with (ex. DNA model for students)
   experimental to see if animal learns or reacs differently

Mean

add all numbers then divide by amount of numbers in the set

Median

Number in middle/ the two numbers averaged

Mode

number that is there most frequently

Quantitative data

measured and documentable

qualitative

descriptive, up to the persons observations, differ from people to people

negative/positive controls

the control group where you expect no response or positive where it produces the desired effect

major elements in the human body

nitrogen, hydrogen, oxygen, carbon

proton

positive charge,and has mass, inside nucleus

electrons

negative charge, neglegible mass, outside nucleus

neutrons

neutral charge, have mass, in the nucleus

atomic mass

protons+ neutrons

atomic number

number of protons and “normal” number of electrons

isotope

forms of an element with different numbers of neutrons

what happens if we change the number of subatomic particles of an atom of a particular element?

for protons: it would change the element and therefore mass (rare)

for nutrons: becomes isotope and changes mass

for electrons: changes the charge

orbital

region where an electron is found at least 90% of the time

→ they are filled in a specific sequence, in a series of electron shells, or energy level

first shell (inner most)

1orbital, holds 2 electrons

second shell

4 orbitals, each shell holds 8 elecrons

valence shell (outer most)

determines how an atom behaves

full? atom is stable

unpaired? atom is reactive

is the energy level higher closer to the nucleus in the orbitals or farther away?

farther away

molecular weight

sum of an atomic weight of all atoms inthe molecule

what bonds are shown in this image

top: nonpolar covalent (bonds within the hydrocarbon) shared equally

bottom: van der waals (interactions between nonpolar molecules) weak bond

what bonds are shown in this image

top: polar covalent (bonds within a water molecule ) VERY strong, one atom has a greater electronegativity
bottom: hydrogen bond (interactions between polar molecules)

What bond is shown

Ionic (interactions between atoms with full charges) atom is much mroe electronegative than the other +/-

intramolecular bond

polar, non-polar, covalent, ionic

intermolecular

hydrogen bonds, van der waals forces/bonds

what molecules are hydrophobic

nonpolar (repels water)

what molecules are hydrophilic

polar (attract water)

solute

substance (that goes in liquid)

solvent

liquid (where solute goes in)

whats so special about water

high specific heat

high heat of vaporization

cohesion (held together with H-bonds)

acid/ acidic

releases hydrogen ions in water

→ pH under 7

base

accept H+ ions

buffer

solution that resists significant changes in PH when small amounts of an acid or base are added to it. (usually a weak acid and a conjugate base)

name macromolecules and think about what shape they are

polymerization

combining small molecules into a large chain

→ involves dehydration

depolyrization

breaks downa large chain into individual units

→ involves hydrolysis

-OH

hydroxyl group

-COOH

carboxyl group

-NH2

Amino groups

-PO 2-/4

Phosphate group

-CH3

Methol Group

Isomer

molecule s w/ the same chemical formula, but the atoms are arranged differently

What kind of isomer is this?

CIs-trans: Different orientation around a double bond

What kind of isomer is this?

Optical: mirror images

What kind of isomer is this?

structural: differ in how atoms are joined

proteins and their functions

storage proteins, transport proteins, motor proteins

→ store amino acids for later use

→ bind and cary substances within the organism

→ cause movement of structures in the cell

what are the parts of an amino acid?

disulfide bridge/bond

(-S-S-)strong covalent bond betweent the sulfur atoms in two cysteine amino acids within a protein

→ important in protein folding but most cysteine in a protein are not involved in disulfide bridges

peptide bond

covalent amide linkage that forms between the carboxyl group of one amino acid and the amino group of another

→ -C(=O)-NH-

primary protein structure

sequence of amino acids

secondary loevel for protein structure

H bond interactions between amino andcarboxyl groups of amino acids

→ can form alpha helixs or beta pleated sheets

tertiary protein structure

polypeptide fold, forming specific shapes

quaternary protein structure

2 or more polypeptides assemble to form larger protein molecules

how can proteins unfold?

being heated (considered denatured)

pH changes, high concentrations of polar molecules, non polar substances, via hydrophobic interactions