Diversity Of Life Quiz One

Front 1

Nested Hierarchy

Back 1

Each level encompasses the level below and none of the levels above. {taxonomy}

Front 2

emergent properties

Back 2

properties that emerge because of interactions between parts of the system. emerge at the level of the cell.

Front 3

The cell is...

Back 3

the functional unit of life

Front 4

hypothesis

Back 4

a prediction about an event that is testable, repeatable and falsifiable. can be tested in an objective way.

Front 5

theory

Back 5

a well-substantiated explanation of some aspect of the natural world under CERTAIN CONDIDTIONS

Front 6

law

Back 6

a descriptive generalization about how some aspect of the natural world behaves under certain conditions. usually mathematical. no explanation.

Front 7

why is water useful?

Back 7

fuels cells//excellent solvent//water moderates heat gain and loss//surface tension aids circulation//ice is less dense than water, which sustains life in extreme cold

Front 8

astrobiology

Back 8

the search for life on other planets

Front 9

elements common to life

Back 9

carbon//hydrogen//oxygen//nitrogen//phosphorous/

Front 10

carbon skeleton

Back 10

chains of carbon molecules. organic compounds contain carbon.

Front 11

hydrocarbons

Back 11

compounds composed of only carbon and hydrogen.

Front 12

functional groups

Back 12

a small group of atoms bonded together and that are part of an organic compound that exhibit particular chemical properties. small differences in functional group can equal big differences in an organism. example: there is very little difference between estrogen and testosterone.

Front 13

estrogen mimics//endocrine disrupters

Back 13

chemicals that function like estrogen in the body {ddt,pcb,bpa,atrazine}

Front 14

isomer

Back 14

molecules with the same chemical formula, but different structure.

Front 15

isotope

Back 15

atoms with different numbers of neutrons.

Front 16

4 major classes of macro-molecules

Back 16

lipids//proteins//carbs//nucleic acids

Front 17

macromolecules all have...

Back 17

functional groups//carbon skeletons//monomers

Front 18

monomers

Back 18

small molecules that can join together to form polymers

Front 19

polymers

Back 19

long chain of joined monomers

Front 20

the monomers for protein are

Back 20

amino acids

Front 21

polymers are held together with

Back 21

covalent bonds

Front 22

how many amino acids are there

Back 22

20

Front 23

what is the function of a protein

Back 23

1>>structure {nails, hair, cells} 2>>enzymes {catalyzing reactions} 3>>defense {antibodies} 4>> movement 5>>signalling {cell to cell} 6>>transport

Front 24

primary structure

Back 24

the sequence of a chain of amino acids {1 dimensional}

Front 25

secondary structure

Back 25

pleating or coiling on local H bonds. sequence of aa linked by H bonds.

Front 26

tertiary structure

Back 26

more complex folding based on interactions between side chains. 1>>covalent bonds 2>>h bonds 3>>ionic bonds 4>>hydrophobic interactions.

Front 27

quaternary structure

Back 27

multiple protein interactions.

Front 28

prion

Back 28

misfolded proteins. prion diseases develop when you develop one prion and it then causes the misfolding of other proteins. {mad cow//kuru//traumatic brain injury}.

Front 29

denaturation

Back 29

unraveling of protein shape. lose complex structure first. can be caused by variable temperatures and pH.

Front 30

enzymes

Back 30

a protein catalyst used by biological organisms to speed up and control reactions {reactions: breaking or forming new bonds}

Front 31

activation energy

Back 31

the energy required to initiate a chemical reaction. enzymes can lower the amount of energy needed to speed up reactions.

Front 32

active site

Back 32

place on enzyme where reactants bind

Front 33

induced fit

Back 33

enzyme changes shape to mold to substrate

Front 34

competitive inhibition

Back 34

one molecule blocks active site on enzyme

Front 35

non-competitive inhibition

Back 35

molecule that binds to another part of an enzyme which changes its shape

Front 36

dna

Back 36

the molecule of genetic inheritance. made up of purines and pyrimidines, double and single rings. very stable. always has the same width because of complementary base pairing.

Front 37

dna's double helix//replication

Back 37

during replication, dna helicase "unzips" the strands, forming template strands. the new strand that is added to each side of the template strand is called the complementary strand. code is written from the 5' to 3' end. polymerase adds dna continuously on the 3' end, the leading strand. The strand that starts with the 5' is the lagging strand and is formed discontinuously.

Front 38

diffusion

Back 38

spontaneous movement from an area of high concentration to an area of low concentration {perfume in a room}