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Biochemistry (Cole) > Lecture 30 Protein Synthesis and Protein Functions > Flashcards

Lecture 30 Protein Synthesis and Protein Functions Flashcards

1
Q

Amino acids

A
  • primary structure of a protein
  • grouped by side chain (charged, uncharged polar, or non polar)
  • side chain is important for function, and restrict rotation around the alpha carbon in terms of what type of confirmation you can achieve
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2
Q

Secondary structure

A

-secondary structure refers to the stretches of the polypeptide chain that form alpha helices or b sheets

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3
Q

B sheets

A
  • parallel

- or anti parallel

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4
Q

What determines the rotation of the amino acid?

A
  • the type of side chai (can have profound effect on structure and function)
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5
Q

Tertiary structure

A
  • full 3D structure of protein

- globular, or linear, rod shaped etc.

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6
Q

Quaternary structure

A
  • used for proteins that have multiple polypeptide chains that make them up
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7
Q

LRP5 HBM mutation

A
  • glycine substituted for valine at 171

- changes ability of protein to interact with certain regulator of LRP5 and prevent inhibition of LRP5 pathway

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8
Q

Protein motifs

A
  • shared sequences of amino acids that can be used to identify potential members of a protein family
  • shared motifs generally equate to similar functions
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9
Q

Protein domains

A
  • structural entities that function essentially independently within a protein and can be built form a specific motif or set of motifs
  • beta propellor domains
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10
Q

YWT on LRP5

A
  • motif (4 of them)
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11
Q

EGF

A
  • motif on LRP5
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12
Q

LDL receptor

A
  • motif on LRP5
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13
Q

Types of protein sequence motifs

A
  1. Proteolytic enzyme cleavage sites
  2. Phosphorylation sites
  3. Binding motifs
  4. Transmembrane spanning sequences
  5. Protein secretion leader sequences
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14
Q

Do structural arrangement of motifs predict function

A

Not necessarily

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15
Q

Do sequence motifs that can be found in both proteins and DNA have biological significance?

A

Yes

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16
Q

Proteolytic enzyme cleavage sites

A
  • cleave specific sequence

- motif

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17
Q

Phosphorylation sites

A
  • critical to regulation of activity

- motif

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18
Q

Helix-loop-helix

A

common in transcription factors and consists of alpha helices bound by a looping stretch of amino acids

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19
Q

Helix-turn-helix

A
  • DNA binding motif consisting of two a helices joined by a short stretch of amino acids
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20
Q

Zinc finger motif

A
  • DNA binding motif consisting of two B strands
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21
Q

DNA replication

A
  • has sequencing motifs like TATA box that are promoters and transcription factor binding sites
22
Q

What can DNA sequence tell us

A
  • eventual protein function and what gene might do
23
Q

Major proteins of the enamel

A
  1. Amelogenin
  2. Ameloblastin
  3. Enamelin
  4. Kallikrin 4
  5. Mmp-20
24
Q

Amelogenin

A

Stabilizes the amorphous Ca-P phase , control of apatite crystal morphology and organization, control of enamel thickness
- Amelogenins have the ability to self assemble into nanosperes and thereby guide HAP crystal formation/growth

25
Q

Ameloblastin

A
  • Cell adhesion protein, controls cell differentiation, maintains rod integrity
26
Q

Enamelin

A
  • Cooperates with amelogenin to control mineral nucleation and elongated growth
27
Q

Kallikrin 4

A
  • Digests enamel proteins during maturation stage facilitating their removal and hardening the final layer of enamel
28
Q

Mmp-20

A
  • Cleaves amelogenin, ameloblastin, and enamelin at the secretory stage to produce stable intermediates with defined functions
29
Q

What is enamel formed by?

A
  • ameloblasts
30
Q

What is enamel composed of?

A
  • 90% amelogenin and 10% enamelin
31
Q

What happens when apatitie crystals grow?

A
  • amelogenin is removed
32
Q

AMelogeniin features

A
  • high in proline, luecine, histidine, and gluatamine, but contains no hydroxyproline or cystine
33
Q

How many genes are there for amelogenin?

A
  • one on the X chromosome (AMELX)
  • one on the Y chromosome (AMELY)
  • this results in differences in the enamel between males and females
34
Q

Why can enamel not regenerate?

A
  • because it is an acellular material

- its ameloblasts have been removed

35
Q

During what phase are constitutens released to form enamel?

A
  • secretory phase
36
Q

What is formed first dentin or enamel?

A

Dentin

37
Q

Odontoblasts

A
  • produce dentin`
  • differentiate from cells in the dental papilla
  • Secrete their organic matrix around the area that is directly adjacent to the inner enamel epithelium
  • odontoblasts move towards center of tooth forming the dontoblast process
  • odontoblasts process secretes hydroxapatite cystals and mineralizes matrix forming the mantle dentin
  • primary and secondary dentin form through different processes
38
Q

Odontoblast processes

A
  • highly branched

- secretory pipes

39
Q

Main extracellular molecule associated with dentin?

A
  • type I collagen
40
Q

Sibling family proteins

A
  • small integrin binding lingand N linked Glycoproteins
41
Q

Types of Sibling proteins

A
  • DSPP
  • DMP1
  • Bone sialoprotein
  • Osteopontin
  • MEPE
42
Q

Dentin Sialophospho proteins (DSPP)

A
  • immediately cleaved after secretion into DSP, DGP, and DPP
43
Q

Dentin Matrix Protein 1 (DMP1)

A
  • Produced by odontoblasts and early stage osteocytes
44
Q

Bone sialoprotein

A
  • Role in biomineralization
45
Q

Osteoprotein

A
  • HA binding and contains an RGD motif, mineralization inhibitor
46
Q

MEPE

A
  • matrix extracellular phosphoglycoprotein contains an RDG motif and in bone appears to be an inhibitor of mineralization
47
Q

Cementum

A

made by cementoblastas

- made up of collagen and other proteins

48
Q

Acellular cementum

A
  • forms first

- cementoblasts arising from dental follicle

49
Q

Cellular cementum

A
  • cemtoblasts arising from adjacent area of bone

- anchoring tooth in bone

50
Q

What cells form peridontal ligament?

A
  • fibroblasts from dental follicle
51
Q

What is the function of the peridontal ligament?

A
  • provides cushion so forces of mastification dont fracture bone (buffers the force of chewing)
52
Q

Cells of peridontal ligament

A
  • secrete collagen which interacts with fibers on surface of adjacent bone and cementum

Biochemistry (Cole) (25 decks)

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