1-24 Given what you know about the differences between prokaryotic cells and eukaryotic cells, rate

the following processes to study in the model organism, E.coli. a) b) c) d) e) 1-26 "ou wish to e#plore how mutations in specific genes affecting sugar metabolism might alter tooth development. $hich organism is likely to provide the best model system for your studies and why% a) !umans b) &ice' &ice are the best model because they are mammals and thus share a high degree of similarities to humans. &ice are small, ine#pensive, easy to maintain, and can reproduce (uickly. c) E.coli d) Arabidopsis e) Gorillas 1-27 )ircle the simplest model organism best used to study the following processes' *rocess a chloroplast function b immunology C.elegans mouse &odel +rganism Arabidopsi s yeast E coli. Drosophila Arabidopsi s yeast Formation of the endoplasmic reticulum DN replication !ow the actin cytoskeleton contributes to cell shape !ow cells decode their genetic instructions to make proteins !ow mitochondria get distributed to cells during cell division Bad Good Bad Good Bad

c Development of a multicellular tissue Drosophil a

2-24 *hospholipids can form bilayer membranes because they are' a) hydrophobic b) lipids c) amphipathic' they have both polar and nonpolar parts duality which causes to form a spontaneous bilayer in an a(ueous environment d) hydrophilic e) amphoteric 2-25 $rite out the se(uence of amino acids in the following peptide using the full names of the amino acids' *roline , -aline , .hreonine , Glycine , /ysine , )ysteine , Glutamine 2-28 DN differs from 0N in' a) the number of different bases used b) the number of phosphates between the sugars in the sugar1phosphate backbone c) the kind of sugar found in the sugar1phosphate backbone' .he sugar in 0N is different in having an additional !+1group on the )123 which is cis1 with respect to the )1431+!. d) one of the purines used e) the chemical polarity of the polynucleotide chain 4-17 hemoglobin molecule a) b) c) d) e) is composed of four protein domains is a dimer of polypeptide chains has two binding sites for nitrogen gas is composed of two different types of protein subunits is composed of four identical protein subunits

4-20 For each of the following indicate whether the individual folded polypeptide chain forms a globular 5G) or fibrous 5F) protein molecule a) b ) c) d ) e) f) 4-23 .he human immune system produces billions of different immunoglobulins, also called antibodies which enable the immune system to recogni7e and fight germs by specifically binding one or a few related antigens. 5-9 .he DN from two different species can often be distinguished by a difference in the' a) b) c) d) e) 5-11 )onsider the structure of the DN double heli# a) :t would be better to separate the strands and each take one strand, because one would ;ust be breaking the hydrogen bonds holding the base pairs together. 6eeping the specific base pairs in one strand allow for the future copying of the DN strand. b) It has not escaped our notice that the specific pairings we have postulated immediately suggest a possible copying mechanism for the genetic material. .his statement implies that DN is the carrier of the genetic code and the process of replication or copying is how genetic material passes from generation to another. ratio of 9 . to G 9 ) ratio of 9 G to ) 9 . ratio of sugar to phosphate presence of bases other than , G, ) and .. number of strands in the heli# 6eratin /yso7yme 8lastin )ollagin F G F F

!emoglobin G ctin G

3-28 )onsider a description of an en7ymatic pathway that begins with the binding of substrate < to en7yme 8 and ends with the release of product * from the en7yme. 8 9 < 8< 8* 8 9 * =nder many circumstances,
!m =

[ E ][ ] [E ]
] = !m %

a) $hat proportion of en7yme molecules are bound to substrate when [

!m =

[ E ][ ] [E ]

.he concentration of the uncombined en7yme'

[ E ] = [ E> ] [ E ]
!m =

( [ E> ] [ E ] )[ ] [E ]
[ ][ E> ] [ ][ E ] [E ]

!m =

[ E ] ! m = [ ][ E> ] [ ][ E ] [ E ] ! m + [ E ][ ] = [ ][ E> ]

[ E ]( ! m + [ ] ) = [ ][ E> ] [ E ] = [ E> ][ ] !m + [ ]
5?)

6nowing the relationships'

# = "2 [ E

and #m = " 2 [ E > ]

By dividing these, two rates'

# = "2 [ E ] # [E ] = #m [ E > ] #m = " 2 [ E > ]

[ E> ] =

[ E ]#m
#

52)

[E ] = #

"2

54)

<ubstituting e(uations 52) ad 54) into 5?)'

[ E ] = [ E> ][ ] !m + [ ]

[ ]##m # = " 2 " 2 ( ! m + [ ] )#

#=

# = "2

[ ]##m " 2 ( ! m + [ ] )#

[ ]#m ( !m + [ ])
]

# [ ] = #m ! m + [

if

[ ] = !m

then
# = #m [

[ ] =? ] +[ ] 2

b) 0ecall that when [ ] = ! m , the reaction rate is #ma# 2 . Does the answer to a) make sense in light of this rate information% "es.

3) )onsider the following reaction se(uenced'

"? " 2

<98

( E )?

"4 " @

(E )2

"A $+ E

Develop a suitable rate e#pression for product formation [ v = " A ( E a) .he e(uilibrium approach Formation of [ ( E

)2]

by using'

)? ] '
v = "? ( [ E > ] [ ( E

) ? ] )[ ] + "@ [ ( E ) 2 ]
) ? ] + "4 [ ( E ) ? ]

5?)

Disappearance of [ ( E

)? ] '
v = "2 [( E
52)

t steady state'

"? ( [ E > ] [ ( E
Formation of [ ( E

) ? ] )[ ] + "@ [ ( E ) 2 ] = " [( E ) ] + " [( E ) ]

2 ? 4 ?

54)

)2]'
v = "4 [( E

)? ]

5@)

Disappearance of [ ( E

)2]'
v = "@ [( E

) 2 ] + "A [ ( E ) 2 ]
) 2 ] + "A [( E ) 2 ]

5A)

t steady state'

"4 [( E

)? ]

= "@ [( E

5B)

From this e(uilibrium e(uation, we can rearrange 54) to get " @ [ ( E

)2] '
5C)

"@ [( E

) 2 ] = " 2 [ ( E ) ? ] + " 4 [ ( E ) ? ] "? ( [ E> ] [ ( E ) ? ][ ] ) ) ? ] + " 4 [ ( E ) ? ] "? ( [ E> ] [ ( E ) ? ][ ] ) + " [ ( E ) ]

A 2

8(uation 5C) can be added to 5B)

"4 [( E
<implify'

)? ]

D "2 [( E

5E)

> D "2 [ ( E 0earranging 5F)'

) ? ] "? ( [ E> ] [ ( E ) ? ][ ] ) + " [ ( E ) ]

A 2

5F)

"2 [( E
<ince v = " A [ ( E

) ? ] + "? ( [ E> ] [ ( E ) ? ][ ] )

D "A [( E

)2]

5?>)

)2] '
v = "2 [( E

) ? ] + "? ( [ E> ] [ ( E ) ? ][ ] )

5??)

b) .he (uasi1steady1state approach !ere we assume that the initial substrate concentration greatly e#ceeds the initial en7yme concentration. :f

[ ] >> [ E> ]
v = "2 [( E

then

) ? ] + "? ( [ ( E ) ? ][ ] )