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Biochemistry 8th Edition Berg Test Bank Full clear download (no error formatting) at :

Chapter 2 Protein Composition and Structure

1) Which of the following is most often found in proteins?

A) D-amino acids

B) L-amino acids

C) an equal amount of D- and L-amino acids

D) amino acids with the -carbon exclusively having an R absolute configuration

E) amino acids with the -carbon exclusively having an S absolute configuration

Answer: B

Section: 2.1

2) A term that describes a molecule that contains both positive and negative charges but

overall has a neutral charge is

A) enantiomer

B) amino acid

C) racemate

D) zwitterion

E) amphipath

Answer: D

Section: 2.1

3) Which amino acid forms disulfide bonds?

A) histidine

B) methionine

C) proline

D) serine

E) cysteine

Answer: E

4)

W h i ch of the following amino acids h as an ioni z able R -group with a p K a n ear n eut ral

pH?

A)

his ti dine

B)

s erine

C )

asp art i c a cid

D)

l ysine

E)

t

yros i ne

Answer: A S ection: 2.1

5)

Fo rm at i on of a p ep t ide b ond produces

as a b yp rod u ct.

A)

ammonia

B)

carbon dioxide

C)

water

D)

H +

E)

OH

Answer: C

Section: 2.2

6)

backbone?

What type of plot allows one to investigate the likely phi and psi angles of the peptide

A) Hill

B) Lineweaver-Burk

C) Hanes-Woolf

D) Ramachandran

E) Michaelis-Menten

Answer: D

Section: 2.2

A)

p rim ar y

B)

s econd ar y

C )

t erti ar y

D)

qu at ern a r y

E)

both second ar y a nd t erti a r y

Answer: B S ection: 2.3

8)

The ov er al l th ree-dim en s ion al s t ru cture of a s i n gle po l yp ept i de is r efe rred t o as

A)

primary structure

B)

secondary structure

C)

tertiary structure

D)

quaternary structure

E)

both secondary structure and tertiary structure

Answer: C

Section: 2.4

Fill-in-the-Blank Questions

9)

is a fibrous protein and is the primary component of wool and hair.

Ans: -Keratin

Section: 2.3

10)

Every third residue in the protein collagen is

Ans: glycine

Section: 2.3

.

11)

Disulfide bonds in proteins can be reduced to free sulfhydryl groups by reagents such as

.

Ans: β-mercaptoethanol

Section: 2.6

12)

A protein is considered to be

coiled structure without its normal activity.

Ans: denatured

Section: 2.6

when it is converted into a randomly

13)

cartilage, and teeth.

Ans: Collagen

Section: 2.3

is t he m ajor fibrous prot ein pres ent i n sk i n, bon e, t endon,

14)

Collagen contains

Ans: hydroxyproline

Section: 2.3

15)

Agents such as

by disrupting the noncovalent interactions.

_, a modified amino acid.

and guanidinium chloride denature proteins

Ans: urea

Section: 2.6

16)

refers to the spatial arrangement of subunits and the

nature of their interactions. Ans: Quaternary structure

17)

The

Section: 2.5

oriented in the same directions (N → C). Ans: parallel Section: 2.3

Multiple-Choice Questions

β-sheet structure occurs when the two strands are

18)

Which of the following is a function of proteins?

A)

energy carrying molecules

B)

catalysts

C)

storage of genetic information

D)

None of the answers is correct.

E)

All of the answers are correct.

Ans: B Section: Introduction

19)

Key properties of proteins include

A)

a wide range of functional groups.

B)

an ability to possess either rigid or flexible structures as dictated by functional

requirements.

D)

All of the ans wers are co rrect.

E) a wide ran ge of fu n ction a l groups and an abi l i t y to pos s ess ei ther ri gid or fl e x ible s t ru ctures as d i ct at ed b y f un ction al requi rem ents.

Ans: D S ection: Int rodu ction

20)

W h at is t he ch arged gro u p (s) pres ent in gl yc ine at a pH of 7?

A) NH 3 + B) C OO C ) NH 2 + D) NH 3 + and C OO E) All the ch ar ged grou p s are p resent.

Ans: D S ection: 2.1

21)

At a pH of 12, wh at is t he ch ar ged group (s ) p res ent in gl yci n e?

A) NH 3 + B) C OO C ) NH 2 + D) NH 3 + and C OO E) All the ch ar ged grou p s are p resent.

Ans: B S ection: 2.1

22)

W h at do the amino aci ds T yr, Asn, and Thr h ave i n com m o n?

A)

aro m at i c ri n gs

B)

n e gat ivel y cha r ge d at pH 7.0

C )

pos i t i v el y ch a r ge d at pH 7.0

D)

double bonds i n s i de ch ai ns

E)

pol ar

Ans: E S ection 2.1

23)

W h i ch two am i no acids cont ai n a su l fur atom?

A)

s erine and m ethionine

B)

s erine and th r eon i ne

C )

m ethionine and threonine

D)

c yst ei n e and m ethionine

E)

c yst ei n e and th r eon i ne

Ans: D S ection: 2.1

24)

W h i ch of the following p ai rs of amino acids i s po s itivel y ch a r ged a t a n eut r al p H?

A)

Lys , A r g

B)

T yr, Ar g

C )

C ys, M et

D)

Leu, P ro

E)

Asp, Glu

Ans: A S ection: 2.1

25)

P h e-Al a-Gl y- Ar g

In the fo l lowing p ept ide, whi ch am ino acid is the N-t erm i nus?

A) P he B) Ala C ) Gl y D) Ar g E) P he and Ar g

Ans: A S ection: 2.2

26)

are no oth e r p rot ein mod ifi cations.)

W h at is t he app rox i m at e m ass of a p rot ei n cont aining 200 amino acids? (As s ume there

A) 2,000 B) 11,000 C ) 22,000 D) 222,000 E) None of th e answers i s co rrect.

Ans: C S ection: 2.2

27)

W h i ch ind i v i du al won a Nobel P ri z e for his (h er ) l andm ark work in s eq u en cing t he

p

rot ein insu l i n?

A) P a uling B ) M c C l i nto c k C

A) P auling B) M cC l i nto ck C ) Gilb ert D) M ax am E) S anger

Ans: E S ec tion: 2.2

Ans: E S ection: 2.2

28)

W h y is the p ep t ide bond pl an ar?

A)

Bul k y s i de ch ains p r ev en t free ro t ation around the bond.

B)

It con t ai ns p arti al doubl e -bond ch aract er, p rev ent i ng rot ation.

C )

H yd ro gen bondi n g b et w een the NH and C =O gro u ps l imi t s m ov em en t .

D)

All of the ans we rs ar e co rrect.

E)

None of the a nsw ers i s c o rrect .

Ans: B S ection: 2.2

29)

The con fi gu r at ion of m ost p eptide bonds i n a p rot e in is

A) cis B) ci r cul ar C ) p arall el D) t rans E) p erp end i cu l ar

Ans: D S ection: 2.2

30)

W h at s t ru cture(s) did Pauling and C o re y p redi ct i n 195 1?

A) α helix B) β sh eet C ) β turns D) P auling and C o re y p r edi ct ed all th ree of these s t ru ctures. E) α helix and β sh eet

Ans: E S ection: 2.4

31)

The t erm q u at ern ar yw i th resp ect to p rot ein s t ru cture m eans

A) a r ep eati n g s t ru ctur e s t abiliz ed b y int r ach ain h yd rogen bonds. B) the abili t y t o fo rm all four kinds of non cov al en t bonds. C ) a multisubun i t st ru ct ure. D) a l i n ea r s equ en ce of f our am ino acids. E) None of th e answers i s co rrect.

Ans: C S ection: 2.5

32)

W h ere ar e Ω and β tu rns and l oops o ft en found?

A)

in a h yd r ophobic pock et

B)

on the int erior cl eft

C )

at the p ro t ein i nt erf ace w ith l i gand

E)

None of the answ ers is co rrect .

Ans: D S ection: 2.3

33)

W h at are so m e of the m o di fi cat i ons t h at p ro t eins a cqui re?

A)

cl eav a ge and t rimm i ng o f the p rotein

B)

addition of carbo h yd r ate groups

C )

phospho r yl at i on of cert ai n groups

D)

All of these ar e m odi fi cat ions prot eins acqui re.

E)

addition of carbo h yd r ate groups and phospho r yl at i on of cert ai n gr oups

Ans: D S ection: 2.6

34)

a wat er -so l ubl e, gl obul ar p rot ei n?

W h i ch of the following a mino acid res i du es wou l d most likel y b e bu ried i n the i nt erior of

A)

Asp

B)

S er

C )

P he

D)

L ys

E)

Gln

Ans: C S ection 2.5

S ho rt -Answer Qu estions

35) How do es a pro t ei n s am ino acid s equ en c e in fluen ce the t ert i ar y s t r u ctu re? Ans: A prot ei n wi ll spon t an eo us l y fold into a three-d i m ens i on al s t ru cture d eterm i n ed b y the amino aci d s equ en ce. S ection: Int rod u ction

36)

W h at is t he adv ant age of h av i ng 20 di ffere nt am i no acids av ail able to fo rm p rot eins?

Ans: The am i no acids p rovide a ri ch div ers it y of fun ction al groups, whi c h can ind ep end en t ly cont ribute to p rot ei n stru cture and fun ct ion. In ad dition, m an y can b e mod i fi ed, in creas i ng t h e div ers i t y of fun ct i on al gr oups. S ection: Int rod u ction

37) W h at is t he adv ant age of p ro t ein i nt eraction and as semb l y with oth e r prot eins? Ans: W h en p rot eins i nteract or as s embl e, n ew fun ct i ons and sp eci fi ci t y b e come a v ai l ab l e. P rot ein i nt eract i ons al l ow n ew binding s i t es at the as s embl y int erface, as well as p roviding mult i fun ction al activi t y a nd sp eci fi ci t y, su ch as fo und i n po l ym eras es and s i gn al t ransd u ction. S ection: Int rod u ction

38) W h at are t he three aro m atic am i no acids? Ans: ph en yl al an i ne, t yr os i n e, and tr yptop h an S ection: 2.1

39) W h i ch am i no acid s i de ch ains are cap ab l e of ion iz ation? Ans: The am i no acids a re Asp, Glu, His, C ys, T yr , Lys , and Ar g. S ection: 2.1

40) How do es t he p rot ein b ac kbone add to s t ru ctural s t ab i li t y? Ans: The p ro t ein b a ckbone co nt ai ns t he p eptide bond, whi ch is an am ide cont ai ning an N H group and a C =O ( carbo n yl ) group. P eptide bonds are ki n et ical l y s t able o n c e fo rm ed, h aving

v er y l ow rat es of h yd ro l ys i s. H yd r o gen-bond fo rm at ion b et ween the h yd ro g en on t he ni t rogen and the o x ygen f rom oth er carbo n yls i n either al p ha h eli ces or in b eta sheets suppo rt the p rot ein con fo rm ation. S ection: 2.2

41) W h y are all the t h eo reti cal comb i n at i ons of phi an d psi not possibl e? Ans: S t eric hind ran c es of the s ide ch ains m ake cert ain c ombin ations and an gl es i mpos s ibl e. S ection: 2.2

42) Des cribe so m e of the f eat u res of an α h elix . Ans: The α h elix is a co i l st abili z ed b y int r ach ain h yd ro gen bonds b et we en t he c arbo n yl

o x ygen o f a r es i due and t he amide h yd ro gen o f the fou rth res i due awa y. Th ere a re 3.6 amino

aci ds p er turn. Th e h yd ro gen bonds are b etween a mino acid res i du es t h at h ave three int erv eni n g

residu es. Thus, t h ese am ino acid res i du es are fo u nd on the s ame side of t h e co i l. The h el i x is almost alwa ys ri gh t -h an d ed, al t hou gh l eft -h an d ed h eli ces ar e, in t h eo r y, po s s i bl e. S ection: 2.3

43)

W h at is t he h yd r ophobi c eff ect” as i t relates t o p ro t ein s t ru cture?

Ans: The three-dim ensi on al s t ru cture of a wat er-soluble p rot ein i s s t abi l i z ed by the t end en c y of h yd rophobi c groups t o as semble in the int erior of t he mol ecul e. S ection: 2.1

44) -Ke ratin is r eferre d to as a coi l ed -coil p ro t ein. D es cribe the p rot ein st ru ct u re of -

k eratin.

Ans: Two α h eli ces entwin ed t o fo rm a v er y s t a ble do u ble h el i x of app rox i m at el y 100 nm in

l en gth.

S ection: 2.3

45) W h at are p rions? Ans: P rions are p rot eins t h at c an as s ume (aft er infecti o n or b y ot h er causes) a n ew prot ein s t ru cture, whi ch is s el f -p r op agat i n g. M am m al i an p rion diseas es a re f at al. S ection: 2.6

46) W h at do es the modificat ion involving the att ach m ent of acet yl groups t o the amino t ermini of prot ei ns do? Ans: The ac et yl a t ion of t he am ino t ermini of p rot ei ns m ak es t h ese pro t eins m o re res i st ant to

d egradation. S ection: 2.6

47) In the ri bonu cl e ase ex p er im ents perfo rm ed b y Anf ins en, what was t he s i gn i fi can c e of the

p res enc e of the redu ci n g agent β -m er capto ethano l ?

Ans: The red u ci ng a ge nt r edu c ed i n co rrect l y p a i red d i s u l fide bonds, al l owing t h em to refo rm

with the co rre ct p ai ri n g u ntil t he most s t able con form at ion of the p rot ein h ad b een obt ained. S ection: 2.6

48) W h at is t he adv ant age of h av i ng cert ai n are as of p art i al l y co rrect fo l d ed re gion s? Ans: If so m e re gions i nt er act p referent i al l y, l endi n g s t a bili t y to c ert ain co n fo rm a tions as t he

p rot ein folds, t h e y can i mp act the ov er all s t ru cture of the p ro t ein. S ection: 2.6

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