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Mbb231 > Protein Basis If Life > Flashcards

Protein Basis If Life Flashcards

1
Q

Proteins shapes and surfaces allow:

A

-Interact selectively with other molecules
-High degree of specifity

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2
Q

Protein functions

A

1- Enzymes
2- Structural
3- Motility
4- Regulatory
5- Transport
6- Signaling
7- Receptor
8- Defensive
9- Storage

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3
Q

Amino acid sequence —> 3D structure of proteins —> Determines the protein function

A

Memorize :)

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4
Q

Amino acids polymers

A

Protein

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5
Q

number of standard amino acids

A

20

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6
Q

All amino acids have

A
  • carboxyl group
  • amino group
  • alpha-carbon
  • unique side chain
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7
Q

At PH=7

A

Carboxyl group= losses proton= negatively charged
Amino group= accepts proton= positively charge

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8
Q

Asymmetric alpha carbon

A

All amino acids except glycine have one

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9
Q

Each amino acid except glycine has

A

Asymmetric alpha carbon —> in D or L form

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10
Q

Amino acids in synthesis of a protein always

A

L-amino acids

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11
Q

Properties of amino acids depend on:

A

-size
-shape
-charge
-HB
-hydrophobic character

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12
Q

Acidic AA

A

Negatively charged

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13
Q

Basic AA

A

Positively charged

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14
Q

Polar amino acids location

A

Found on surface

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15
Q

Non-polar AA

A

Usually buried in the core of proteins

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16
Q

How stepwise addition of new amino acids occus?

A

Condensation/Dehydration

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17
Q

Process of elongating a chain of amino acids

A

Protein synthesis

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18
Q

Immediate product of proteins synthesis

A

Amino acids

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19
Q

When poly peptide become a protein

A

Assumed unique and stable 3 dimensional shape

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20
Q

Primary structure

A

-Linear strand of AA
-Size can vary 2–33000

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21
Q

Folding important bonds

A

-covalent bonds — disulfide bonds between sulfur atoms of two cysteine
-not covalent bonds - 4 types
*covalent is much stronger

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22
Q

Disulfide bond

A

Between two sulfur atom of two cysteine
*can be intra- or intermolecular bonds

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23
Q

Secondary Structure (stable types)

A
  • alpha helix
  • betta sheet
  • turn
  • loop
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24
Q

What generate secondary structures?

A

Local Hydrogen Bonds among AA (polypeptide backbones)

25
Q

Alpha helix

A

-spiral in shape
-peptide backbone
-R groups jutting out from the spiral
-HB between NH group of one AA and CO group of second AA (only one turn away)
-can be hydrophobic/hydrophilic
** alpha helix is not hollow

26
Q

Hydropolarity in Alpha helix

A

-Non polar in the middle of
phospholipid — non-polar tails
-Polar in both ends — polar heads

27
Q

Constraints of alpha helix

A

1- repulsion or attraction of AA residues
2- bulkiness of adjacent R groups
3- interactions between R groups 3-4 residues apart
4- HELIX FORMING AA: L/M/E
5- HELIX BREAKERS AA: P/G

28
Q

What determine structure

A

Primary sequence determine structure (identity and sequence of AA)

29
Q

Beta sheet

A

Sheet like conformation with Several polypeptide (strand) side by side in a folded or pleated conformation
-characterized by maximum number of HB
-Beta sheet formers: I,V,F

30
Q

Beta sheet kinds

A

1-parallel
2-antiparallel

31
Q

Alpha helix and Beta sheet

A

-Major internal supportive elements
-60% of a protein

32
Q

Motif

A

Units of secondary structure consist of short stretches of alpha helix and beta sheet

33
Q

DNA binding protein motif type

A

Helix-turn-helix

34
Q

Protein can be classified as —

A

Combination of secondary structures (motifs)

35
Q

Tertiary structure

A

1- conformation of the entire polypeptide
2- stabilized by covalent and non-covalent bonds between side chains
3- tertiary structures are unlimited

36
Q

Two identification way for proteins

A
  1. X-ray crystallography (protein should form pure crystals)
  2. NMR spectroscopy (difficult to use with larger proteins)
37
Q

T or F
Proteins with different primary sequence level may have similar tertiary structure

A

True

38
Q

Similar structure

A

Similar function

39
Q

Domain

A

-Substructure of overall tertiary structure with a specific function
-50-350 AA
-regions with alpha and beta packed compactly
-Proteins with same function may have same domain
-protein with different functions have separate domain for each function

40
Q

T or F?
Protein are capable of internal movement

A

True

41
Q

Every activity in which protein take part

A

Accompany by conformational changes

42
Q

Alpha helix breakers

A

Proline — too bulki
Glycine — too small

43
Q

Quaternary structure

A

More than one subunit held together by non covalent interactions or disulfide bonds between R-group

44
Q

Quaternary structure kinds:

A

1- Homodimer : two identical subunits
2- Heterodimer: two non-identical subunits

45
Q

Hemoglobin

A

Heterotetramer
2 alpha-globin
2 betta-globin

46
Q

Titin (human)

A

Tertiary structure but biggest protein

47
Q

Stable three dimensional structure

A

Native conformation

48
Q

Proteins categories

A

1- Fibrous
2- Globular

49
Q

Fibrous proteins

A

1- extensive regions of secondary structure — highly ordered — repetitive structures
2- common in structural materials
— hair
— skin
— blood vessels

50
Q

Globular proteins

A

Different segments of polypeptide chain fold back on each other creating a compact structure
- maybe mainly alpha helical, mainly beta sheet, or mixture
- each type has unique tertiary structure
- most proteins are globular
-Ex. Enzymes/Transport proteins

51
Q

Denaturation by

A

1- detergent
2- radiation
3- heat

52
Q

Self assembly

A

Primary sequence has all the information of 3D conformation

53
Q

Final confirmation

A
  • most energetically favorable
  • folding happens fast
54
Q

Chaperones

A

Short stretches of hydrophobic AA that are exposed in non-native protein to facilitate proper folding

55
Q

Chaperons of Hsp70

A

Prevent them to bind to other proteins in the cytosol

56
Q

Chaperones will be released if

A

Protein spontaneously fold into native state

57
Q

Chaperones larger

A

Chaperonins

58
Q

Prion

A

Proteinaceous infectious particle
- bad protein convinces good proteins to reform

Mbb231 (19 decks)

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