proteins Flashcards

1
Q

define amino acids

A

monomers of all amino acids and all amino acids have the same basic structure

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2
Q

define peptide bond

A

bond formed when two amino acids are joined together in a condensation reaction

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3
Q

what elements do all amino acids contain

A

C, H, O, N

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4
Q

what is the element that only three amino acids contain

A

sulfur

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5
Q

what are the four main biological roles of proteins

A

structural: make up most of the body’s tissues e.g. muscles hair skin and ligaments.
metabolic: all enzymes are proteins
signalling: many hormones and receptors are proteins
immunity: all antibodies are proteins

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6
Q

what is the general structure of an amino acid

A

an amino acid has an amino group (H2N), carboxyl group (CHO2) and an R group and a hydrogen (H) atom

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7
Q

what defines an amino acid

A

its R group

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8
Q

what type of bond are amino acids joined together by and what is it called

A

covalent bond called peptide bond.

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9
Q

what kind of reaction occurs when creating a peptide bond

A

condensation

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10
Q

what enzyme breaks down peptide bonds during digestion

A

protease

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11
Q

what are two amino acids called

A

dipeptide

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12
Q

what are more than two amino acids called

A

polypeptide

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13
Q

where does the peptide bond between two amino acids form

A

between the OH of carboxyl group and H of the amine group.

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14
Q

what does a protein consist of

A

one or more polypeptide chains folded into a specific 3D shape

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15
Q

what is the primary structure of a protein

A

sequence of amino acids

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16
Q

what is the secondary structure of a protein

A

the coiling or folding of an amino acid chain, which often arises as a result of hydrogen bonding on different parts of the chain

17
Q

what are the two main formed of the secondary structure of a protein

A

helix and pleated sheet

18
Q

what is the tertiary structure of a protein

A

the 3D shape of the protein molecule caused by interactions such as hydrogen bonding, ionic bonding, disulfide bridges, hydrophilic/phobic interactions

19
Q

what is the quaternary structure of a protein

A

protein structure where a protein consists of more than one polypeptide chain e.g. insulin

20
Q

in a chain of amino acids, what holds the helix secondary structure in shape

A

hydrogen bonds

21
Q

where are H bonds are between in the helix of amino acids

A

the NH of one amino acids and the CO of another amino acid 4 places ahead of it in a chain

22
Q

how do all the different bonds in tertiary structure work

A

hydrogen bonds between polar R groups and other polar R groups, hydroxyl, carboxyl and amine groups. ionic bonds between positively charged R groups. disulfide bridges between cysteine R groups. hydrophobic R groups bend towards the centre of the structure whereas hydrophilic R groups bend towards the water

23
Q

what are the two main categories of three-dimensional tertiary and quaternary structures of protein

A

globular and fibrous

24
Q

what are the characteristics of fibrous proteins

A

repetitive sequence of amino acids
insoluble
structural (collagen, keratin)

25
what are the characteristics of globular proteins
-almost spherical in shape -soluble due to position of hydrophobic/philic R groups -often have very specific shapes due to their roles (enzymes, hormones)
26
what is the structure of fibrous proteins
long rope-like fibres with high tensile strength that are generally insoluble in water and also unreactive.
27
why is collagen found in artery walls
layer of collagen surrounds walls and prevents artery from bursting when withstanding high pressure
28
why is keratin found wherever a body needs to be hard and strong
rich in cysteine which means lots of disulfide bonds so makes the molecule very strong
29
what are the 4 polypeptide chains of haemoglobin made up off
2 alpha-globin chains and 2 beta-globin chains
30
what is the haem group of a haemoglobin molecule
area called prosthetic group which contains an iron ion and can bind to one molecule of oxygen
31
what is a protein that is associated with a prosthetic group called
conjugated protein
32
what is the colour change of haemoglobin when o2 binds to a haem group
purple to bright red
33
why is pepsin so stable in acidic environments
it only has 4 basic R groups