Bio 208 Final Set 1

Front 1

Charles Darwin brought
biology into focus in 1859
when he presented two
main concepts in The
Origin of Species.
The first was that
contemporary species
arose from a succession
of ancestors through
“_______ _____ ______________” (evolution).

Back 1

Decent with modification

Front 2

The second was that the
mechanism of evolution is
____________ ______________.

Back 2

natural selection

Front 3

Darwin explained natural selection by connecting
two observations:
Observation 1: Individuals in a population of any
species vary in many _______________ __________.
Observation 2: Any population can potentially
produce ______ _____ ___________ than the environment
can support.

Back 3

inheritable traits

far more offspring

Front 4

natural selection creates a _____________ ______ _________among
variant members of a population (PT).

Back 4

struggle for existance

Front 5

Natural selection, by its cumulative effects over
vast spans of time, can produce new _________
from ____________ species.

Back 5

species
ancestral

Front 6

Descent with ________________ accounts for both the unity
and diversity of life.

Back 6

modification

Front 7

In many cases, features shared by two species are
due to their descent from a ____________ ancestor.

Back 7

common

Front 8

Differences are due to modifications by __________ ___________ modifying the ancestral equipment in
different environments.

Back 8

natural selection

Front 9

The _____ is the lowest level of organization that can
perform all activities required for life

Back 9

cell

Front 10

All cells -Are enclosed by a ________________
• Use _____ as their genetic information

Back 10

membrane
DNA

Front 11

A ______________cell has membrane-enclosed organelles, the largest of which is usually the nucleus

Back 11

eukaryotic

Front 12

By comparison, a __________ cell is simpler and
usually smaller, and does not contain a _______ or other
membrane-enclosed organelles

Back 12

prokaryotic

nucleus

Front 13

____________ Charge 0, Mass +1, in nucleus

Back 13

Neutrons

Front 14

__________ Charge +1, Mass +1, in nucleus

Back 14

Protons

Front 15

__________ Charge -1, Mass 0, in orbital

Back 15

electron

Front 16

Atoms exist as a nucleus with __________ charge,
surrounded by a cloud of electrons in
orbitals

Back 16

positive

Front 17

Functional groups are
side groups that give
properties to ________
structures

Back 17

carbon

Front 18

There are 6 functional groups
H
C
C
A
S
P

Back 18

Hydroxyl
•
Carbonyl
•
Carboxyl
•
Amino
•
Sulfhydryl
•
Phosphate

Front 19

Written as OH-
Is polar as a result of the
electronegative oxygen atom
drawing electrons toward itself.
Attracts water molecules, helping
dissolve organic compounds such
as sugars (see Figure 5.3)

Back 19

Hydroxyl

Front 20

Written as >CO
Kentones if the group is within a carbon skeleton
Aldehydes if the group is at the end of the skeleton

Back 20

Carbonyl

Front 21

Written as -COOH
acts as an acid

Back 21

Carboxylic

Front 22

Written as -NH2
Acts as an base

Back 22

Amino

Front 23

Written as -SH

Back 23

Sulfhydryl

Front 24

written as -OPO3 2-

Back 24

Phosphate

Front 25

WRitten as -CH3

Back 25

Methyl

Front 26

Carbohydrates: general functions and properties

Monosaccharides have the formula (CH2O)n
n = 3 ______ C3H6O3
n = 5 ________C5H10O5
n = 6 _________ C6H12O6
Functions: energy storage (starch)
Structure
(cellulose,
chitin
)
Information (
cell
surface
receptors)

Back 26

triose
pentose
hexose

Front 27

_____________
sugar is formed
from fructose and glucose

Back 27

Sucrose

Front 28

_________________ are Large and complex: carbohydrates, proteins and
nucleic acids

Back 28

Polymers

Front 29

General functions of polymers

Back 29

1. Storage
2. Structure
3. Information

Front 30

Monomers are joined to form polymers by a process called
______________ ______________ or ___________.
One H2O is ___________ for each bond formed.
Energy is ____________

Back 30

dehydration synthesis
condensation

released

required

Front 31

Polymers are broken down by
_____________. One H2O is____________
for each bond broken.
Energy is ______________

Back 31

hydrolysis

consumed

released

Front 32

____________
are
unbranched
polymers built from the
same set of 20 amino acids

Back 32

Polypeptides

Front 33

____________ ___________
are organic molecules with carboxyl and
amino groups

Back 33

amino acids

Front 34

Amino acids differ in their properties due to differing side
chains, called __ groups

Back 34

R

Front 35

Amino acids are the
subunits of ___________

Back 35

proteins

Front 36

The alpha
-
carbon has 4 groups
attached; 1
-
3 are common to
all amino acids

-
1,2,3,4

Back 36

1. Amino group
2. Carboxyl group
3. H
4. R-group

Front 37

Amino acids are linked by
____________ bonds

Back 37

peptide

Front 38

A functional protein consists of one or more
________________ precisely twisted, folded, and
coiled into a unique shape

Back 38

polypeptides

Front 39

The coils and folds of
__________________ ________________
result from hydrogen bonds between repeating
constituents of the polypeptide backbone

Back 39

secondary structure

Front 40

Typical secondary structures are a coil called
an___________
and a folded structure called a
_____________ _______

Back 40

helix
pleated sheet

Front 41

The ____________ structure of a protein is its unique
sequence of amino acids
•
__________ structure, found in most proteins,
consists of coils and folds in the polypeptide
chain
•
______________ structure is determined by interactions
among various side chains (R groups)
•
____________ structure results when a protein
consists of multiple polypeptide chains

Back 41

primary
secondary
tertiary
quaternary

Front 42

This loss of a protein’s native structure is
called
_____________________

Back 42

denatured

Front 43

1st Law of thermodynamics:

Back 43

E cannot be created or destroyed.

Front 44

2nd Law of thermodynamics:

Back 44

During E
interconversions
, some E is always lost as
random thermal movement or heat, which is not available to
do work.

Front 45

The ___________
= randomness, disorder or chaos of the universe is
always increasing.

Back 45

entrophy

Front 46

Metabolism involves:
1) Making and breaking ____________ bonds.
2) Getting, using, and changing the form of __________.
3) Reactions are catalyzed by _____________.
4) Several enzymes may be organized into a pathway

Back 46

covalent
E (energy)
enzymes

Front 47

Forward
reaction:
Respiration (in mitochondria)
Catabolism (degrade to simpler forms)
Exergonic
(E released)
Glucose + O2>>>> CO2+ H2O + E Forward reaction

Back 47

yea

Front 48

CO
2
+ H
2
O + E >>>> Glucose + O
2
Reverse reaction
Reverse reaction:
Photosynthesis (in chloroplasts) light energy stored in chemical bonds
Anabolism..build up to make complex molecules from simple ones
Endergonic
(E required)
Catabolism and anabolism drive one another

Back 48

yea

Front 49

__________energy is related to the locationof molecules

Back 49

potential energy

Front 50

_____________energy is used in the process of doing work

Back 50

kinetic

Front 51

unit of energy

Back 51

calorie

Front 52

1 calorie is the amount of energy needed to raise _______ of ____________ 1 degree_________

Back 52

1gram of water celisus

Front 53

To do work, cells manage energy resources by
__________ ___________
, the use of an
exergonic
process to drive an
endergonic
one

Back 53

energy coupling

Front 54

____________
products
are > stable than reactants;
stability is related to their
enthalpies and therefore is
unchangeable)

Back 54

exergonic

Front 55

Old bonds must be broken,
which requires E
____________________ _______________
“barrier” must be overcome

Back 55

Activation Energy (EA)

Front 56

_____________
are
biological
catalysts.

Back 56

Enzymes

Front 57

Substrates
bind to an enzyme’s
___________ __________

Back 57

active site.

Front 58

Upon
binding,
the
shape
of the enzyme and its active
site change “
_________ __________

Back 58

induced fit”

Front 59

______________ inhibitors bind to the
active site of an enzyme, which
prevents the substrate from
binding

Back 59

Competitive

Front 60

_________________inhibitors
bind
to an
allosteric
site
(i.e.,
not the
active site).
Structure of active
site is changed, so substrate
nolonger
can bind.

Back 60

Noncompetitive

Front 61

1) _____________ hold the enzyme
in an active form and increase enzyme activity
2) _____________ hold the enzyme
in an inactive form and decrease enzyme activity

Back 61

Activators
Inhibitors