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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
Alpha helix
-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
Hydropolarity in Alpha helix
-Non polar in the middle of phospholipid — non-polar tails -Polar in both ends — polar heads
27
Constraints of alpha helix
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
What determine structure
Primary sequence determine structure (identity and sequence of AA)
29
Beta sheet
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
Beta sheet kinds
1-parallel 2-antiparallel
31
Alpha helix and Beta sheet
-Major internal supportive elements -60% of a protein
32
Motif
Units of secondary structure consist of short stretches of alpha helix and beta sheet
33
DNA binding protein motif type
Helix-turn-helix
34
Protein can be classified as —
Combination of secondary structures (motifs)
35
Tertiary structure
1- conformation of the entire polypeptide 2- stabilized by covalent and non-covalent bonds between side chains 3- tertiary structures are unlimited
36
Two identification way for proteins
1. X-ray crystallography (protein should form pure crystals) 2. NMR spectroscopy (difficult to use with larger proteins)
37
T or F Proteins with different primary sequence level may have similar tertiary structure
True
38
Similar structure
Similar function
39
Domain
-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
T or F? Protein are capable of internal movement
True
41
Every activity in which protein take part
Accompany by conformational changes
42
Alpha helix breakers
Proline — too bulki Glycine — too small
43
Quaternary structure
More than one subunit held together by non covalent interactions or disulfide bonds between R-group
44
Quaternary structure kinds:
1- Homodimer : two identical subunits 2- Heterodimer: two non-identical subunits
45
Hemoglobin
Heterotetramer 2 alpha-globin 2 betta-globin
46
Titin (human)
Tertiary structure but biggest protein
47
Stable three dimensional structure
Native conformation
48
Proteins categories
1- Fibrous 2- Globular
49
Fibrous proteins
1- extensive regions of secondary structure — highly ordered — repetitive structures 2- common in structural materials — hair — skin — blood vessels
50
Globular proteins
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
Denaturation by
1- detergent 2- radiation 3- heat
52
Self assembly
Primary sequence has all the information of 3D conformation
53
Final confirmation
- most energetically favorable - folding happens fast
54
Chaperones
Short stretches of hydrophobic AA that are exposed in non-native protein to facilitate proper folding
55
Chaperons of Hsp70
Prevent them to bind to other proteins in the cytosol
56
Chaperones will be released if
Protein spontaneously fold into native state
57
Chaperones larger
Chaperonins
58
Prion
Proteinaceous infectious particle - bad protein convinces good proteins to reform

Mbb231 (19 decks)

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