CT 3 part 2 Flashcards

1
Q
A
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2
Q

tf Ehlers-Danlos Syndrome, has inc crossliking of collagen

A

F

lowered

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3
Q

Poor wound healing

and Musculoskeletal deformities

A

Ehler danslos

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4
Q

Hyp

A

CANNOT be incorporated into a growing polypeptide chain so addition of [14C] Hyp will not result in formation of [14C] collagen

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5
Q

Proline and hydroxyproline are both radioactive but

A

Hyp CANNOT be incorporated into a growing polypeptide chain

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6
Q

Unique to collagens;

A

Unique to collagens; glycosylated hydroxylysyl residues

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7
Q

2 types of O linked glycosylations

A

serine and 5 hydroxylysine

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8
Q

asparagine

A

N glycosyl Linkage

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9
Q

glycosylations of

A

glucose and galactose

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10
Q

After post-translational modification, the 3 polypeptides associate to form the procollagen molecule.

A

After post-translational modification, the 3 polypeptides associate to form the procollagen (Type I procollagen) molecule.

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11
Q

where is procollagen made

A

in the ER lumen

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12
Q

Extension peptides

A

help guide the formation of the triple helix.

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13
Q

Each polypeptide is —- through a large portion of the molecule and stabilized partly by —— of the pyrrolidone rings of proline.

A

Each polypeptide is helical through a large portion of the molecule and stabilized partly by steric repulsion of the pyrrolidone rings of proline.

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14
Q

3 polypeptides (Pro α Chains) wind around each other to form a —- —–, with —— bonds between individual chains

A

3 polypeptides (Pro α Chains) wind around each other to form a —- —–, with —— bonds between individual chains

procollagen

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15
Q

Residues in each chain are —— staggered such that a gly, an X and a Y from ——chains are on the same level along the helix axis.

A

Residues in each chain are vertically staggered such that a gly, an X and a Y from different chains are on the same level along the helix axis.

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16
Q

procollagen

A

stiff cable

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17
Q

H-bonds form between —- and —- in procollagen

A

H-bonds form between the N-H of Gly and O in procollagen

18
Q

procollagen C terminal

A

disulfide linkage

19
Q

cooperative interactions

A

determines stability of collagen molecules

20
Q

-NH of Gly and the C=O of second residue in triplet of neighboring chain

A

have a h bond

21
Q

Gly as every third amino acid

Hyp content

Total imino acid content

A

determine stability of collagen molecule

22
Q

inc temp

A

collagen loses its rodlike shape, the viscosity of the solution drops

helical structure destroyed

23
Q

after TM

A

collagen is a random coil

24
Q

Tm is the temperature at

A

temperature at which 1/2 of the helical structure is lost

26
Q

abnormal collagen

A

smaller Tm

27
Q

abruptness of the transition indicates that the stability of collagen molecules depends upon—- cooperative interactions

A

abruptness of the transition indicates that the stability of collagen molecules depends upon weak cooperative interactions

29
Q

Hyp cntent

A

inc the TM and stabilizes the collagen triple helix

30
Q

pro and hyp inc with

A

warm blooded animals

Tm also increases

31
Q

H bonding in collagen occur

A

between peptide -NH of Gly and the C=O of second residue in triplet of neighboring chain

OH groups of Hyp also participate in Hbonding

32
Q

Mutation of a single gly

A

can be lethal

33
Q

close packing and stabilization of triple helix

A

Glycine

34
Q

OI

A

Mutation of a single T for a G

35
Q

glycine to cysteine mutation

A

OI

36
Q

Skeletal deformities, brittle bones

A

OI

37
Q

Triple helix is disrupted

A

OI

38
Q

Rupture arteries

Rupture uterus

A

Ehlers-Danlos Syndrome, Type IV

39
Q

Thin, translucent skin ,Bruise easily

A

Ehlers-Danlos Syndrome, Type IV

40
Q

Perforate intestines

A

Ehlers-Danlos Syndrome, Type IV

41
Q

Defects in type III collagen

A

Ehlers-Danlos Syndrome, Type IV

42
Q

Gly , Skip exon

A

Ehlers-Danlos Syndrome, Type IV