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BIOC192 > Proteins > Flashcards

Proteins Flashcards

1
Q

Protein structure

A

Non-branching polymers

50 - 100Å

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2
Q

1 Å =

A

10^-10 m

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3
Q

Protein bonds

A

Peptide - covalent bond
2 cysteine = covalent bond = disulfate
Stabilses

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4
Q

Cell signalling

A

Insulin (uptake glucose)

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5
Q

Digestion

A

Trypsin (breakdown protein)

Amylase (starch to sugars)

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6
Q

HIV protease

A

HIV replication

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7
Q

Immune protection

A

Antibodies

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8
Q

Replication and Maintainance

A

DNA and RNA polymerase

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9
Q

Metabolism

A

Alcohol dehydrogenase (ethanol)
Hexokinase (add phosphate to glucose)
Hemoglobin (O2 transport)
ATP synthase

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10
Q

CORN

A

L - most dominant

Clockwise

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11
Q

Non - polar amino acid side chains

A 
Methyl
-SH
-H
Aromatic
methyl + S
Imino acids
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12
Q

Negatively charged polar a.a

A

-COO-

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13
Q

Postively charged polar a.a

A

-NH3+
=NH2+
=NH+ -

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14
Q

Uncharged polar a.a

A

-OH

Amino & carboxyl charges

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15
Q

Peptide bond

A

Planar, trans, rigid

Alpha C on oppo sides

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16
Q

Primary

A

Amino acid sequence

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17
Q

Secondary

A

Local folding

3D arrangement of short adjacent a.a residues

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18
Q

Tertiary

A

3D complete protein

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19
Q

Quaternary

A

Multi subunit protein

20
Q

Alpha helix breakers

A

Glycine - too flexible

Proline - introduce a sharp turn

21
Q

Alpha helix reside/turns

bonding

A

3.6 residues/turn

h-bond b/w n and n+4

22
Q

Alpha helix angles

A 
ɸ = ~-57
Ψ = ~-47
23
Q

Beta structure

A

Adjacent peptide chains - H bonding
Pleated
Parallel/antiparallel

24
Q

Beta sheet numbers

A

2 - 10 strands per sheet

Strand length = 6 - 15 residues

25
Q

Turns

A

High in Gly, Pro

H - bonds (stability)

26
Q

Turns numbers

A

3 - 4 residues

33% residues in turns

27
Q

Function relates to

A

A.a sequence
Higher order
Structure

28
Q

ɸ

A

N - C⍺

O - O collisions

29
Q

Ψ

A

C⍺ - C’ (C’=O)

NH - NH collisons

30
Q

ω

A

Around peptide bond

31
Q

Supersecondary structures

A 
Secondary structure + turns/loops/coils
Helix - turn - helix
β - hairpin
Greek key
Strand - helix - strand
32
Q

Domains

A 
Hydrophobic core (stablises protein)
Hydrophilic parts in contact with solvent
33
Q

Domain types

A

⍺ - domain (mostly helical)
⍺/β domain
Anti-parallel β domain

34
Q

Protein folding instructions

A

In a.a sequence
Proven by Afinsen
Directed by internal hydrophobic residues, form core, hydrophilic exposed

35
Q

Afinsen’s experiment

A

Native ribonuclease
Denature
Given essential componants
Reformed

36
Q

Stablisation of Folding

A

Non - covalent interactions
Covalent bonds
Hydrophobic core

37
Q

Non - covalent interaction examples

A

van der Waals interactions

H - bonds

38
Q

Assistance by Chaperones

A
  • independent
  • dependent
    Chaperonin - dependent
39
Q

Misfolding protein

A

Prions
Other may induce misfolding
⍺ -> β

40
Q

Amino acid modification

A 
Phosphorylation
Hydroxylation
Carboxylation
Metal binding 
Iodination
Glycosylation
41
Q

Phosphorylation

A

Control enzyme activity

42
Q

Hydroxylation

A

Prevent connective tissue diseases

43
Q

Carboxylation

A

Blood clotting

44
Q

PKA definition

A

The pH at which the group is 50% ionized (of ionizable group on an amino acid or protein)

45
Q

Pl definition

A

pH at which the net charge on an amino acid (or protein) is zero

46
Q

Sequence of protein folding

A

1) Formation of short secondary structure segments
2) Nuclei come together, form domain
3) Domains come together (tertiary structure partly disorganised)
4) Adjustments give compact native structure (tertiary)

BIOC192 (6 decks)

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