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bio 101 exam 2 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

anabolism

A

simple compounds are built into
complex molecules, consuming energy in the process

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2
Q

catabolism

A

complex molecules are broken down
into simple compounds, releasing energy in the process

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3
Q

energy

A

the capacity of a system to cause change in its
surroundings, and can exist in various forms

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4
Q

kinetic energy

A

the capacity of a system to cause change in its
surroundings, and can exist in various forms

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5
Q

thermal energy

A

kinetic energy at the atomic level, when
transferred from one object to another is called heat

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6
Q

potential energy

A

the energy of location/structure, and can be
transformed into kinetic energy

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7
Q

chemical energy

A

potential energy stored in chemical bonds,
that can be released through chemical reactions

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8
Q

thermodynamics

A

the study of how
a system transforms and exchanges
energy w/ surroundings

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9
Q

isolated systems

A

there is no
energy/matter exchange with the
surroundings

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10
Q

open system

A

there is energy
transformation and exchange between
the system and surroundings

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11
Q

first law of thermodynamics

A

is that energy can be
transferred or transformed, but NEVER created or destroyed

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12
Q

second law of thermodynamics

A

that during transfer or
transformation of energy, some energy is always converted to
thermal energy and lost as heat

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13
Q

entropy

A

is a measure of how disordered a system is (how
much energy in the system cannot be used to do work)

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14
Q

spontaneous process

A

There are processes that increase the entropy of the universe
without energy input

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15
Q

non-spontaneous

A

There are also processes that can decrease entropy, requiring a
dedicated input of energy

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16
Q

how to calculate changes in free energy

A

^G=^H-T^S FILL IN WITH THE TRIANGLE SIGN WHICH IS change in Toal energy minus temp. in kelvin times change in entropy

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17
Q

what do the free energy calculations mean

A

If the ΔG for a chemical reaction is
negative, that means no energy needs
to be put in for it to happen, and the
reaction is spontaneous

If the ΔG for a chemical reaction is
zero or positive, that means energy
does need to be put in for it to happen,
and the reaction is nonspontaneous

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18
Q

equilibrium

A

the state of maximum stability where forward and reverse reactions occur at the same time

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19
Q

exergonic reactions

A

(negative
ΔG), free energy is released to
surroundings

-spontaneous

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20
Q

endergonic reactions

A

(positive
ΔG), free energy is taken in from
surroundings

-non-spontaneous

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21
Q

energy coupling -pairing endergonic and exergonic reactions

A

where the energy
released from an exergonic reaction
drives an endergonic one

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22
Q

how is atp released

A

The energy stored within ATP is released
when the terminal phosphate bond is
broken by hydrolysis (adding water)

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23
Q

how is atp used to preform work

A

-pump out substances against concentration gradient

  • change the protein shape

-hydrolysis for transport work

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24
Q

how is atp replenished

A

ATP can be replenished by adding a
phosphate group to adenosine
diphosphate (ADP)

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25
Q

role of enzymes as catalysts

A

catalysts that speed up
specific reactions

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26
Q

how do reactions begin through activation energy

A

The amount of energy a reactant molecule
needs to absorb into order to break its
bonds is called activation energy

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27
Q

progression from reactants to transition state to products

A

This makes the molecule increasingly
unstable, and when it has absorbed
enough energy it enters

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28
Q

role of cofactors

A

Enzymes don’t have to act alone, but
can work with nonprotein helpers called
cofactors

These are agents that can bind to the
enzyme (permanently) or with the
substrate (reversibly) & help catalyze
the reaction

Enzymes aren’t always sped up, their
activity can be reduced or blocked by
chemical agents known as inhibitors

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29
Q

how are enzymes regulated

A

by their temp and ph levels

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30
Q

competitive inhibitors

A

can resemble the substrate and bind to
the enzyme’s active site

31
Q

noncompetitive inhibitors

A

do not resemble the substrate,
instead binding to the enzyme away from the active site

32
Q

molecular regulation through allosteric interactions

A

when a regulatory molecule binds to a protein at one site and affects
activity at another site

33
Q

molecular regulation through cooperative interaction

A

substrate binds to one active site
on an enzyme and stabilizes the active site for other substrates

34
Q

molecular regulation through feedback inhibition

A

the end-
product of a metabolic pathway
shuts down the activity of a pathway

35
Q

importance of spatial location of enzymes

A

Enzymes are found where they’re
needed, in specialized locations
throughout the cell (e.g. nucleus for
DNA replication

Some enzymes have fixed locations,
some can be part of multi-enzyme
complexes, some are structural pieces

36
Q

passive transport

A

Small molecules can move into/out of a
cell

37
Q

active transport

A

Small molecules can also move into/out
of a cell

38
Q

bulk transport

A

Large molecules move into/out of a cell

39
Q

basic structural composition of cell membranes

A

Membranes are mostly made of
phospholipids, arranged in a
bilayer

Other macromolecules are also
present, including proteins and
carbohydrates

40
Q

how does the fluidity of membranes vary

A

membranes are fluid, lipids and proteins can
move sideways within membrane and lipids can even flip-flop

41
Q

how are membranes held together

A

by weak
hydrophobic interactions between phospholipid tails

42
Q

in membranes how are agents like cholesterol used for stability

A

Cholesterol is a steroid component
of animal cell membranes that affect
membrane fluidity

43
Q

role of temp to determine membrane fluidity

A

At high temperatures, cholesterol
limits fluidity restricts phospholipid
movement

At low temperatures, cholesterol
promotes fluidity by preventing cell
membrane packing

44
Q

integral proteins

A

Integral membrane proteins reach to the
hydrophobic membrane core

45
Q

peripheral proteins

A

Peripheral membrane proteins are bound
to the membrane surface

46
Q

glycolipids

A

are when lipids are bonded to
these sugar chains

47
Q

glycoproteins

A

are when proteins are
bonded to these sugar chains

48
Q

selective permeability of a membrane

A

some things can cross
through this fluid mosaic structure more easily than others

49
Q

hydrophobic and hydrophilic molecules interacting with selective permeability

A

Hydrophobic molecules (nonpolar)
dissolve in the lipid bilayer and pass
through the membrane easily

Hydrophilic molecules (polar) are
impeded when trying to pass through
the membrane, running into a
hydrophobic wall

50
Q

channel proteins

A

have a hydrophilic
channel that some molecules can use
as a tunnel into the cell

51
Q

carrier proteins

A

bind directly to
molecules and change shape to
chaperone them across the membrane

52
Q

diffusion

A

which is movement
with the goal of equaling out
concentration

53
Q

osmosis

A

When water molecules diffuse
across a selectively permeable
membrane,

54
Q

tonicity

A

The extent to which a solution can
cause a cell to gain or lose water by
osmosis

55
Q

hypotonic

A

water only going in

56
Q

hypertonic

A

water only going out

57
Q

isotonic

A

water is only going both in and out

58
Q

facilitated diffusion and process in membrane proteins

A

transport proteins (such as channel or
carrier proteins) help transport molecules across the membrane

Channel proteins act as corridors that allow specific molecules

59
Q

gated channels

A

here are some types of
ion channels, called gated
channels, that only open or
close in response to a
stimulus

Chemical, electrical, and
mechanical stimuli can
trigger channel opening

60
Q

function of carrier proteins

A

bind to a solute on one side and change shape
to move the solute-binding site across the membrane

61
Q

active transport in gradient

A

passive transport/diffusion, active transport uses
energy to move molecules against concentration gradient

This relies entirely on carrier proteins and almost always on ATP

62
Q

electrochemical transport

A

The movement of ions into/out of a cell

63
Q

electrical force

A

membrane potential

Ions move down electrochemical
gradient, and are transported across
a membrane by electrogenic pumps

64
Q

exocytosis

A

transport vesicles move
the cell membrane, fuse with it and
release their contents outside the cell

65
Q

endocytosis

A

transport vesicles form
at the membrane around a material,
taking their contents inside the cell

66
Q

phagocytosis

A

cellular eating

67
Q

pinocytosis

A

cellular drinking

68
Q

receptor mediated endocytosis

A

means to import macromolecules from the extracellular fluid.

69
Q

how to use microscopy to visualize cells

A

light microscopy passes
light through a specimen and then
through a glass lens
The glass lenses refract and bend the
light to magnify the image back to our
eyes

To study subcellular structures, we
use electron microscopes

70
Q

visualizing organelles by fractionation followed by electron microscopy

A

Scanning electron microscopes (SEMs) focus an electron
beam on the cell surface, providing a 3-D image of the cell
* Transmission electron microscopes (TEMs) focus an
electron beam through a cell to highlight internal structures

71
Q

prokaryotic cells

A

make up bacterial and archaeal organisms

72
Q

eukaryotic cells

A

make up protists, fungi, animals and plants

73
Q

prokaryotic/ eukaryotic similarities

A
  • A cell membrane
  • An internal semifluid substance called cytosol
  • Chromosomes to carry/transfer genetic material
  • Ribosomes to make essential proteins
74
Q
A

biology (1 decks)

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