proteins Flashcards

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1
Q

what is the monomer of a protein?

A

an amino acid

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2
Q

how are proteins linked to DNA?

A

order of bases=amino acid order=protein which coded for a characteristic

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3
Q

what is the general structure of an amino acid?

A

R
H—- | ===O
N–C–C
H—- | —–OH
H

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4
Q

how many naturally occurring amino acids are there? give examples

A

20 eg. serine, glutamine, leucine
each with a different R group

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5
Q

what do 2 amino acids join together?

A

condensation reaction forms peptide bond, molecule of water produced
-OH and H removed

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6
Q

what is the primary structure of an amino acid?

A

-the specific order of amino acids in a polypeptide
-determined by DNA sequence of gene

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7
Q

bonds in primary structure

A

covalent bonds

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8
Q

what is the secondary structure?

A

-polypeptide sections twist and fold into shapes
-alpha helix and beta pleated sheet (flat)

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9
Q

bonds in secondary structure

A

hydrogen bonds form along polypeptide chain, due to attracting O and H charges

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10
Q

what is the tertiary structure?

A

-overall 3D shape of the polypeptide chain
-critical for how protein functions

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11
Q

bonds in tertiary structure

A

hydrogen bonds, ionic bonds, disulfide bonds, non polar hydrophobic interactions

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12
Q

what is the quaternary structure?

A

-shows how the individual sub units (polypeptide chains) are arranged to form a larger 3D structure
-shows position of any prosthetic groups

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13
Q

bonds in quaternary structure

A

hydrogen, van der Waals, forces between non polar side chains

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14
Q

what is a prosthetic group?

A

when proteins are accompanied by non protein molecules which make up the structure and help to carry out the role

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15
Q

what is a conjugated protein?

A

a globular protein with a non protein element called the ‘prosthetic group’

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16
Q

what is a globular protein+ examples

A

spherical soluble protein
eg. haemoglobin, insulin, enzyme

17
Q

structure of haemoglobin

A

-quartnenary protein with 4 polypeptides-2 alpha helix, 2 beta pleated sheet
-prosthetic ‘haem’ group

18
Q

function of haemoglobin

A

-transports oxygen
-‘haem’ group binds irreversibly to oxygen

19
Q

structure of insulin

A

-spherical, compact, soluble
-complex shape, folds into tertiary shape
-has precise shape for receptors

20
Q

function of insulin

A

-hormone that regulates blood glucose concentration

21
Q

enzyme structure

A

-quartnernary protein
-contains 4 ‘haem’ prosthetic groups

22
Q

enzyme function

A

-catalyses reaction
-interacts with hydrogen peroxide to speed up its breakdown

23
Q

fibrous proteins meaning and examples

A

insoluble and strong proteins with structural role for support/protection
-collagen, keratin, elastin

24
Q

collagen function

A

-connective tissue in skin, tendons, ligaments and nervous system

25
Q

collagen properties

A

-stable as R groups repel
-flexible, rope like for movement
-closely packed triple helix
-durable due to tropocollagen-proteins join end to end to form long fibrils which cross link to produce strong fibred

26
Q

keratin function

A

-protective skin barrier
-helps form hair and nails
-heals wounds

27
Q

keratin properties

A

-large proportion of cysteine
-form strong disulfide bonds
-strong, inflexible, insoluble

28
Q

elastin function

A

-gives structure and flexibility to expand and retract

29
Q

elastin properties

A

-quaternary structure made for stretching molecules
-tonoelastic-elastin joins together

30
Q

strength of hydrogen bonds in tertiary structure

A

individually weak but collectively stable

31
Q

strength of ionic bonds in tertiary structure

A

stronger than H bonds

32
Q

strength of disulfide bonds in tertiary structure

A

very strong

33
Q

strength of hydrophobic/hydrophillic interactions in tertiary structure

A

weak interactions

34
Q
A