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Molecules and Cells (Unit 1) > Protein 4 > Flashcards

Protein 4 Flashcards

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Organic Chemistry 101 flashcards
1
Q

How many hypervariable regions are there?

A

6; 3 for each chain

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2
Q

How many main different types of collagen are there?

A

6

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3
Q

Collagen Amino Acid Content from highest to lowest

A

Glycine> proline>hydroxyproline>hydroxylysine

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4
Q

Is an a-helix usually right-handed or left-handed?

A

Right

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5
Q

Collagen I

A
  1. Skin, bone, tendon, scar tissue, heart valve, intestinal and uterine wall
  2. Low carbohydrate, Low hydroxylysine
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6
Q
  1. Crosslinked collagen form _____, which are further crosslinked to form ____. Crosslinking decreased ____.
A

Fibrils; fibers; flexibility

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7
Q

Collagen IV

A
  1. Basement membrane, lens capsule
  2. High carbohydrate, high hydroxylysine, High hydroxyproline, Low alanine, arginine,
  3. Contains cysteine
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8
Q

Complementary interactions of ______of adjacent triple helical molecules further enhance formation of the overlapping fibers

A

Surface ionic charges

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9
Q

Interchain hydrogen bonding between the NH of _____and the CO of ____proline help to strengthen the triple helix.

A

Glycine; Proline (or Hydroxyproline)

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10
Q

Collagen is most prevalent in _____and least prevalent in ____

A

Skin; liver (percentages go down as you go down body)

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11
Q

The hypervariable regions are also called_____

A

Complementary determining regions

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12
Q

Glycine faces inside in the triple helix and forms a _______stripe that stabilizes the molecule. Why can glycine do this?

A

Hydrophobic; it’s small enough

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13
Q

Example of globular proteins

A

Myoglobin

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14
Q

Collagen III

A
  1. New born Skin, scar tissue, blood vessels, intestinal and uterine wall
  2. Low carbohydrate, high hydroxyproline and glycine
  3. Contains cysteine
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15
Q

Goodpasture’s syndrome

A

Hypersensitivity to antigens present in type 4 Collagen

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16
Q

There are _____ antigen binding sites per Ig.

A

2

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17
Q

What kind of helix makes up collagen?

A

Triple Helix (3 chains)

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18
Q

Hypervariable regions come together to form the _______

A

Antigen binding site

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19
Q

Essential cofactor in the hydroxylation of proline

A

Fe

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20
Q

Examples of fibrous proteins

A

Collagen

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21
Q

Where in the body is elastin prominent?

A
  1. Ligaments
  2. Lungs
  3. Walls of arteries
  4. Skin
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22
Q

The secondary structure of collagen appears due to the frequent appears of which amino acids?

A

Proline and hydroxyproline

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23
Q

Regular fibrous protein structures arise from high _______regularity.

A

Primary

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24
Q

What role does ascorbate play in the hydroxylation of proline?

A

Prevents the side reaction from derailing from the primary reaction

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25
Q

All collagens have extensive ____repeats

A

Tripeptide

26
Q

Examples of fibrous protein.

A
  1. Elastin
  2. a-Keratin
  3. tropomysosin
  4. Collagen
  5. Fibrinogen
27
Q

Every THIRD residue in the tropocollagen chains is a ______.

A

Glycine

28
Q

The secondary structure of collagen is a ________coil

A

Left-handed

29
Q

Papain cleavage produces what components?

A

Two Fab and 1 Fc

30
Q

What cell is collagen secreted from?

A

Fibroblasts

31
Q

Scurvy

A

Vitamin C deficiency

32
Q

Which fibrous protein types exists as dimers of right-handed a-helical chains?

A

a- elastin and tropomyosin

33
Q

Antibody- antigen binding mediated by _______forces only.

A

Noncovalent

34
Q

Which fibrous protein is involved in blood clotting?

A

Fibrinogen

35
Q

What are different types of Ehlers- Danlos Syndrome (EDS)? Which are most common?

A
  1. Hypermobility (Most common)
    1. Tendency of joints to dislocate, due to mutations in Collagen type III
  2. Classic (common)
    1. Skin forms cigarette-like scars
    2. Highly elastic
    3. Velvety skin that tears and bruises easily
    4. Difficult to heal
  3. Vascular
    1. Most serious and most rare
    2. Can cause rapture of blood vessels or organs
  4. Arthrochalasis
    1. Loose and unstable joints
36
Q

Are helical or non-helical segments of the triple helix involved in crosslinking?

A

Non helical

37
Q

Collagen II

A
  1. Cartilage, vitreous
  2. Medium carbohydrates, medium hydroxylysine
38
Q

What bonds add to stabilization of Ig structure?

A

Disulfide

39
Q

The basic functional unit of collagen is the ______

A

Tropocollagen; triple helix

40
Q

How is Type I Collagen Made?

A
  1. Procollagen a- chains are synthesized by ribosomes on rER
  2. Sugar added to polypeptide
  3. Procollagen trimers are formed
  4. Chaperones are bound to prevent premature aggregation
  5. Folded procollagen sent to and through Golgi Apparatus
  6. The N and C terminals are removed by proteases
  7. Trimers assemble into fibrils are covalently crosslinked
41
Q

What is the difference between fibrous and globular proteins?

A

An important differentiating feature is that fibrous proteins are insoluble in water, weak acids and weak bases but soluble in strong acids and alkalis where as globular proteins are soluble in water, acids and bases

42
Q

Which types of fibrous protein lacks a regular secondary structure?

A

Elastin

43
Q

Give four examples of coil-coiled fibrous proteins.

A
  1. Fibrinogen
  2. Myosin
  3. Elastin
  4. Keratin
44
Q

Ehlers-Danlos Syndrome (EDS) is caused by faulty synthesis of which protein?

A

Collagen; due to mutations in genes

45
Q

What major roles do fibrous proteins play?

A

Structural and mechanical

46
Q

Where in the body is collagen found?

A

Connective tissue (bone, cartilage)

47
Q

What characteristic of Ig stimulate the formation of large aggregates, when Igs detect invaders?

A

Bivalency

48
Q

Why is the hydroxylation of proline in collagen important?

A

Stability, proper assembly of triple helix, and secretion

49
Q

How do the chains in the triple helix align?

A

Parallel

50
Q

Examples of fibrous proteins

A

•Examples: elastin, a-keratin, tropomyosin, collagen

51
Q

•Elastin:

–Abundant in ligaments, ______, walls of arteries, and _______

–lacks regular ________ structure

–Forms crosslinks involving ________ residues

A

Lungs; skin

Secondary

Lysine

52
Q

•Alpha-keratin and tropomyosin:

–Exist as __________ or (rarely) trimers of _______ a-helical chains

–Chains run in _______

–Coil about each other in ________ supertwist

–Each chain contains repeating ______

  • Residues a and d interface across dimer (or trimer) to form _________ STRIPE that stabilizes coiled-coil structure
  • Residues e and g often _______; form interchain ___________
A

Dimes; right-handed

Parallel

Left- handed

Heptad

Hydrophobic

Charged; Salt bridges

53
Q

Ehlers-Danlos Syndrome (EDS)

  • Caused by faulty synthesis or structure of the important connective tissue protein _______
  • _______ major types

Hypermobility Type:

–Tendency of joints to __________or subluxate (partial dislocation)

–due to mutations in type ________ collagen and/or the extracellular matrix protein ___________

•Other types:

–Classic: features________that forms cigarette-like scars; highly ________, velvety skin that ________and tears easily; difficult to heal

–Vascular: most serious and most rare; can cause premature death due to rupture of ________ or ________; thin, translucent skin; extensive bruising

–_____________: also rare; loose and unstable joints; stretchy, fragile skin

  • Often due to ___________ in genes for various collagens
  • One type (kyphoscoliosis) due to mutation in gene for _________
A

Collagen

Six

Dislocate

Type III; Tenascin-X

Skin; eastic; bruises

blood vessels; organs

Arthrochalasis

Mutations

Lysyl hydroxylase

54
Q

Collagen is secreted from __________

A

Fibroblasts

55
Q

___________ caused by dietary deficiency (in vitamin C)

A

Scurvy

56
Q

–The __________dominant genetic disorder __________, also known as “brittle bone disease”

  • due to a deficiency in Type______ collagen
  • Usually due to _________mutation within the a(I) chain gene
A

Autosomal; osteogenesis imperfecta

One

Point

57
Q
  • The autoimmune disorder Goodpasture’s syndrome:
  • believed to be a hypersensitivity reaction to antigens present in the _________ domain of the a3 chain of type _______ collagen in the ________membrane of the glomerulus of the _________ and the __________alveolus
  • immune system wrongly recognizes these motifs as foreign and produces antibodies ______toward them, elliciting an immune response.
A

Noncollagenous; IV; basement; kidneys; pulmonary

IgG

58
Q

Hydroxylation of Proline

  • Essential cofactor: _________
  • _______ also essential; prevents a concurrent prolyl hydroxylase-catalyzed side reaction from derailing the hydroxylation reaction
  • Hydroxylation essential for stability and proper assembly of _________ triple helix, and for its _______

–In absence, __________, ________, and ________ become fragile due to defective structure

A

Fe2+

Ascorbate

Procollagen; secretion

Skin; tendons; blood vessels

59
Q

Secondary Structure of Collagen Polypeptides/Chains

  • Secondary structural unit is NOT an ________
  • The tripeptide repeats drive the formation of a helix similar to a ___________helix characterized by:
  • Structure minimizes steric clash between the __________ side chain and the peptide backbone
A

a-helix

Polyproline type II

pyrrolidine

60
Q

___________segments near the ends of the a-chains are involved in crosslinking

A

Nonhelical

61
Q

The immunoglobulin fold is the fundamental __________ structural element of Ig. Two ___________ b-sheets pack against each other to form a ____________type structure.

A

Tertiary; antiparallel; barrel

62
Q
A

Molecules and Cells (Unit 1) (48 decks)

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