1.2 Flashcards

biological molecules 1

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1
Q

what bonds form the 3D structure of a protein

A

hydrogen bonds
disulfide bonds
ionic bonds

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2
Q

how do hydrogen bonds form in proteins

A

negative oxygen in the carboxylic acid and positive hydrogen in amino acid group important in folding and coiling

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3
Q

how do disulfide bonds form in proteins

A

two cysteine molecules close together
oxidation reaction creates covalent bond between two sulfur
stronger than hydrogen bond
needed to hold folding of amino acid chains

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4
Q

how do ionic bonds form in proteins

A

strongly positive and negative amino acid side chains form ionic bonds also known as salt bridges

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5
Q

explain the primary structure of protein

A

sequence of amino acids held by peptide bonds

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6
Q

explain the secondary structure of a protein

A

the arrangement of the polypeptide chain into a regular repeating structure held by hydrogen bonds

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7
Q

what is alpha helix structure

A

spiral coil
peptide bonds form backbone
R group stick out in all directions

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8
Q

what is the beta pleated sheet structure

A

regular pleats held by hydrogen bonds most fibrous proteins have this structure

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9
Q

explain the tertiary structure of proteins

A

level of 3D organization further folding into complex shapes held by hydrogen bonds, disulfide bonds, ionic bonds
e.g. globular proteins

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10
Q

which structure are fibrous & globular proteins

A

fibrous - secondary
globular - tertiary

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11
Q

explain the quaternary structure of a protein

A

3D arrangement of multiple tertiary poly-peptides and the addition of a prosthetic group
e.g. hemoglobin

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12
Q

what is the structure of a fibrous protein and give an example

A

little/no tertiary structure long parallel peptide chains occasional cross-linkages form fibers insoluble
e.g. collagen

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13
Q

state 5 uses of fibrous proteins

A

connective tissue in tendons
matrix of bones
structure of muscles
silk of spiderwebs
silk worn cocoons
keratin

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14
Q

explain the structure of collagen and what it’s used for

A

strengths tendons, bones, ligaments & skin
3 poly peptide chains each about 1000 amino acids
triple helix held by hydrogen bonds, found together in fibrils

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15
Q

what structure do globular proteins have

A

tertiary & sometimes quaternary

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16
Q

why do globular proteins not dissolve in water

A

they are too big so instead form a colloid

17
Q

why are globular proteins important

A

hold molecules in position in the cytoplasm
forms enzymes & hormones

18
Q

what type of proteins are red blood cells

A

globular & conjugated

19
Q

what is a conjugated protein

A

a protein which is joined with a prosthetic group

20
Q

what prosthetic group does a red blood cell have

A

iron

21
Q

what are glycoproteins

A

proteins with a carbohydrate prosthetic group

22
Q

what are the properties of glycoproteins

A

they hold onto a lot of water so it is harder for them to be broken down
very slippery & viscous

23
Q

give an example of a glycoprotein

A

mucus
synovial fluid

24
Q

what are lipoproteins

A

proteins conjugated with lipids

25
Q

why are lipoproteins important

A

transport of cholesterol - lipid prosthetic group enables it to combined with the lipid cholesterol

26
Q

how big are LDLs (low density lipoproteins)

A

22nm

27
Q

how big are HDLs (high density proteins) and why do they have a higher density

A

8-11nm
contain more protein