Structural Proteins Flashcards
List the intracellular structural protein(s)
Keratin
List the extracellular structural protein(s)
- Collagen
- Elastin
Keratin
- Structural protein
- Found in skin, hair, nails hoofs and feathers
- High stability from cysteine disulphide bonds
Alpha-keratin
- Consist of alpha helices
- Forms b-keratin at high temp
- Stabilised by disulphide bonds
- Hair, wool, nail, hoof
Beta-keratin
- Stronger than alpha-keratin
- Beta-pleated sheet
- Feathers and reptile scales
Disulphide bonds in keratin can be reduced by…
Thioglycol
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or another reducing agent
Composition of wool
- 3 alpha keratin macromolecules → 1 Protofibril
- 11 protofibrils → 1 Microfibril
- Microfibril → Macrofibril
- Macrofibril → Wool fibre
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What stabilises the polypeptide chain of keratin?
Disulphide bonds
Cells on the outer layer of the epidermis
- Dead cells
- Held together by a network of keratin fibres
- Provided by keratinocytes
Synthesis of keratin
- Pre-keratin produced in cells
- Skin cells mature and become keratinized
- Cells of the stratum basale go upwards
- Keratin-containing stratum corneum formed
Keratin can be degraded by…
- Thioglycolates
- Keratinase (moth larvas)
List the extracellular matrix components
- Collagen
- Elastin
- Fibronectin
- Laminin
- Proteoglycans
Collagen (extracellular)
- Very abundant fibrous protein
- Insoluble in water
- Skin, bone tendon, cartilage blood vessels
- Not found in plants
Structure of collagen
- Basic unit: Tropocollagen (triple helix structure)
- Striated
- Gly & Pro / hydroxyPro / hydroxyLys are prominant in the peptide chains
How does a lack of vitamin C cause scurvey?
- Vitamin C needed for collagen synthesis
- Bleeding gums, loosening teeth
- Process name
- Enzyme required
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- Hydroxylation of Lysine
- Lysine hydroxylase (Requires vitamin-C)
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End product name
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5-OH-Lys (Hyl)
End product name
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4-OH-Pro (Hyp)
- Process name
- Enzyme required
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- Hydroxylation of Proline
- Proline hydroxylase (requires vitamin C)
Due to the high level of Pro / hydroxyl-Pro, the polypeptide chains of collagen cannot…
- Form alpha-helix/B-sheet
- Left-handed helix conformation instead
- This conformation allows the 3 helices to interlock (tropocollagen)
Structural units of collagen
Tropocollagens → microfibrils → macrofibrils → fibres
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What binds tropocollagen units?
- Cross links (C=C/C=N bonds)
- Disulphide bonds
- H-Bonds
What is the purpose of Pro/Lys being converted to hydroxy-Pro/hydroxy-Lys?
- Pro/Lys cannot hydrogen bond
- Converted to hydroxy- in order to form hydrogen bonds
Lys-aldehyde + Lys-aldehyde →
(Allysine + Allysine →)
Condensation: Cross linkage
Give the varieties of collagen in order of abundance
- Collagen-I
- Collagen-II-IV
- Collagen-V-VII
Every third amino acid in collagen is…
Glycine
(Forms a helix)
What structural change does hydroxy-Lysine undergo during collagen synthesis?
hydroxy-Lysine is glycosylated (Gal-Gal-Glu)
Chains twist together and form a triple helix (procollagen)
Describe the stages of collagen synthesis
- Transcription + Translation
- Pro → OH-Pro, Lys → OH-Lys
- OH-Lys glycosylated → procollagen
- C and N-terminus propeptides removed
- Tropocollagen
- Cross linkage → Type I collagen
Which enzyme removes the C- and N-terminus propeptides?
Procollagen peptidase enzyme
What can degrade collagen?
- Collagenase enzyme
- Microbial collagenase
- Clostridium
- Tissue collagenase
- Tadpole tail resorption
- Wound healing
- Microbial collagenase
Elastin
- Protein in connective tissue
- Important in arteries, lung, skin, bladder
- Elastic and expansible
- Primarily composed of Gly, Pro (Lys)
Describe the structure of elastin
- Linking of soluble tropoelastin molecules
- Cross-linked by H-bonds and covalent bonds
- Insoluble, durable crosslinked array formed
Synthesis of elastin
Begins in the cytoplasm of fibrocytes
- Tropoelastin formation
- Extracellular crossling formation
- Elastin fibre production
Degradation of elastin
- Tropoelastin
- Mature elastin + Elastase enzyme →
- Elastin fragments
Where is elastase formed and stored?
- Pancreas
- Leucocytes, stored in granulocytes