AMINO ACIDS, PROTEIN STRUCTURE AND FUNCTION Flashcards

1
Q

What is the chemical structure of amino acids?

A

NH3 - CHR - COOH

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2
Q

peptide bonds

A
  • amino acids joined by peptide bonds
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3
Q

what is an oligopeptide?

A

small proteins with about 10-40 amino acids

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4
Q

one chain polypeptide?

A

myoglobin for oxygen transport

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5
Q

2 chain polypeptide?

A

A and B chains in insulin

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6
Q

3 chain polypeptides?

A

collagen triple helix

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7
Q

2 chain polypeptide?

A

2 alpha 2 beta subunits of Hb

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8
Q

how many R groups are there?

A

20

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9
Q

how many hydrophobic R groups?

A

9

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10
Q

neutral R groups

A
  1. all have OH/=O/NH groups that form H bonds with water.
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11
Q

acidic R groups

A
  1. have a carboxyl group
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12
Q

basic R groups

A
  1. N-H groups of which lysine and arginine are protonated at physiological pH whilst histadine is physiological buffer
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13
Q

give 4 examples of fibrous proteins

A

collagen - bones - tensile strength

elastin - ligaments - elastic strength

proteoglycans - bone - elastic strength

keratin - hair/skin - external protection

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14
Q

give 2 examples of globular proteins; enzymes

A

trypsin - stomach - cleaves proteins

lysozyme - tears - antimicrobial

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15
Q

2 examples of globular protein; transporters?

A

haemoglobin

transferrin (iron transport)

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16
Q

globular protein; hormone example?

17
Q

globular protein immune system example?

A

immunoglobulins

18
Q

give 3 examples of hybrid fibrous-globular proteins?

A

actin, myosin, fibrinogen

19
Q

how is diversity created?

A

20 different amino acids.
different protein sizes.
chemical modification

20
Q

primary structure

A

order of covalent polypeptide sequence, sequence of amino acids

21
Q

secondary structure

A

3D arrangement of amino acids, side chain with each other and main chain. stabilised only by H bonds

22
Q

tertiary structure

A

3D arrangement of individual protein subunits to form multimeric protein

23
Q

quaternary structure

A

3d assembly of individual protein subunits to form multimeric protein

24
Q

alpha helix

A
  • rod like with R groups outside
  • all H bonds are between separate main chains and perpendicular to the direction of the main chain
  • parallel sheets: N-termini are the same end
  • antiparallel sheets: the N-termini are at opposite ends
25
b-turns and loops
two conformational extremes that exist at the surface of globular proteins to link together the individual a-helices and b-strands in the protein core. they are hydrophilic.
26
what is super secondary structure?
all the secondary structures inside the structure
27
what are the common folds of a-helices/b-strands?
all a-helix protein = globin fold of myoglobin and Hb all b-sheet protein = immunoglobin fold of antibodies mixed a-helix/b-sheet proteins; TIM fold with a closed b-sheet barrel buried in core and a-helices flanking this on surface; the other fold variant based on an open twisted b-sheet buried in the core with a-helices above and below it
28
describe the structure of globular proteins?
- compact protein structure - soluble in water / lipid bilayers - secondary structure is complex with mixture of a-helix, b-sheet and loop structures - quaternary structure held together by non-covalent forces - functions in all aspects of metabolism
29
fibrous proteins
- extended protein structure - insoluble in water / lipid bilayers - secondary structure is simple based on one type only - quaternary structure usually held by covalent bridge - functions in structure of body or cell
30
haemoglobin vs myoglobin (globular)
Hb is oxygen carrying protein of blood, myoglobin carries oxygen of muscle. Hb is formed from 4 polypeptide chains (2 a chains and 2 b-chains); 4 hame groups myoglobin has one polypeptide with one haem. hame groups in hb and myoglobin bind to oxygen.
31
immunoglobulins
- part of immune system - recognition of antigens is based on B - sheet structure called Ig fold. - antibodies are y shaped molecules; 2 light chains and 2 heavy chains; arranged as 2 Fab and 1 Fc fragments. Fab recognises antigens, and fc effects the immune response.
32
A-keratin
external protection, toughness, in hair/skin, forms most dry mass of this material, submit contains 2 long a-helices, cross linked by disulphide bridges
33
elastin
connective tissue, relates to elasticity and stretchability, can stretch several times than return to original size, subunits cross linked by covalent bonds, found in arteries (aorta) and lung wall
34
collagen
connective tissue, tensile strength results from use of triple helix secondary structure/assembly of tropocollagen subunits into a fibre/chemical cross linking to strengthen fibre
35
fibrinogen
mixed fibrous - globular proteins; fibrinogen is protective protein that stops bleeding by sealing wounds
36
myosin
responsible for contractile properties of muscle