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Biology: 2.1.2 Biological Molecules > proteins > Flashcards

proteins Flashcards

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1
Q

what elements are proteins made up of

A

carbon, hydrogen, oxygen, nitrogen and sometimes sulphur

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2
Q

what are the monomers of proteins

A

amino acids

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3
Q

what is a dipeptide

A

two amino acids joined together

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4
Q

what is a polypeptide

A

multiple amino acids joined together

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5
Q

what is the general structure of amino acids

A

central carbon bonded to an amine group, carboxyl group, variable R group and a hydrogen

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6
Q

what bonds link together amino acids

A

peptide bonds

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7
Q

where does the peptide bond form

A

the carboxyl group of one amino acid and the amine of another

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8
Q

what is the primary structure of proteins

A

sequence of amino acids in a polypeptide chain

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9
Q

what bonds are present in the primary structure

A

peptide bonds between amino acids

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10
Q

what is the secondary structure of proteins

A

changes the shape of the protein so it is no longer flat, this is done by either changing it to an alpha helix or beta pleated sheets

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11
Q

what bonds are present in the secondary structure of proteins

A

hydrogen bonds form between nearby amino acids

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12
Q

what is the tertiary structure of proteins

A

further coiling and folding with many new bonds forming the 3D structure

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13
Q

what bonds are present in the tertiary structure

A

ionic bonds: attractions between oppositely charged R groups

disulfide bonds: amino acid cytesine has sulphur, sulphur atoms bonding together

hydrophobic/hydrophilic interactions: hydrophobic R groups clump together this means hydrophilic R groups are pushed to the outside affecting the folding

hydrogen bonds: form between slight negative and slight positive R groups

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14
Q

what is the quaternary structure of proteins

A

some proteins are composed of several different polypeptide chains held together by bonds (haemoglobin)

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15
Q

what bonds influence the quaternary structure

A

dependant on the tertiary structure so can be ionic, disulfide and hydrogen bonds

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16
Q

what are globular proteins

A

round and compact

17
Q

why are globular proteins soluble

A

hydrophobic and hydrophilic interactions

18
Q

what are the shape of globular proteins

A

spherical

19
Q

what are some general properties of globular proteins

A
  • have a tertiary structure
  • can be complementary to other molecules
  • hydrophilic outside
  • contain prosthetic groups
  • sensitive to temp change/ pH
20
Q

what is haemoglobin

A

globular protein which carries oxygen around the blood

21
Q

why is haemoglobin a conjugated protein

A

has a non-protein group (iron) attached, this is called a prosthetic group

22
Q

how many polypeptide chains does haemoglobin have

A

4 all containing a haem group

23
Q

what is insulin

A

a hormone which is a globular protein secreted by the pancreas

24
Q

why is the solubility of insulin important

A

easily transported via the blood to tissues where it needs to act

25
Q

what is the structure of insulin

A

two polypeptide chains with disulfide bridges

26
Q

what is amylase

A

an enzyme which is a globular protein that catalyses the breakdown of starch

27
Q

what is the structure of amylase

A

single chain of amino acids with both alpha helix and beta pleated sheet sections

28
Q

what is a fibrous protein

A

strong and tough proteins

29
Q

what are some properties of fibrous proteins

A
  • strong
  • insoluble
  • little tertiary structure
  • elongated rod shape
30
Q

how do fibrous proteins provide structure

A

collagen in connective tissue in skin, bone and muscle with its strength making it well suited to its role as well as its insolubility

31
Q

how does keratin provide protection

A

found in external structures of animals such as skin, hair and nails

can be flexible as its in the skin and also rigid in hair and nails

32
Q

what does elastin do

A

shows the flexible nature of fibrous proteins as its elastic so allows blood vessels to return to their original shape (eg in alveoli)

Biology: 2.1.2 Biological Molecules (6 decks)

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