topic 1 - proteins Flashcards

cgp (topic 1A) 8 - 9

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1
Q

what are proteins made from

A

long chains of amino acids

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2
Q

what is a monomer of proteins

A

amino acids

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3
Q

how is a dipeptide formed

A

when two amino acids join together by a peptide bond

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4
Q

what are protein made up of

A

one or more polypeptides

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5
Q

what is an amino acids general structure

A

a carboxyl group (-COOH)
an amine/ amino acid group (-NH²)
an R group/ variable side group

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6
Q

what is the only difference between the 20 amino acids

A

the R group

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7
Q

how are polypeptides formed

A

when more than two amino acids are joined together by peptide bonds

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8
Q

how do two amino acids become a dipeptide (detailed)

A

amino acids are linked together by condensation reactions to form a dipeptide - a molecule of water is released during the reaction - the bonds formed between amino acids are called peptide bonds

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9
Q

how many structural levels do proteins have

A

four

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10
Q

what are the proteins four structures

A

primary, secondary, tertiary, quaternary structures

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11
Q

what is the proteins primary structure

A

this is the sequence of amino acids in the polypeptide chain

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12
Q

what is the proteins secondary structure

A

the polypeptide chain doesn’t remain flat and straight - hydrogen bonds form between the amino acids in the chain, making it automatically coil into an alpha helix or fold into a beta pleated sheet

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13
Q

what is the tertiary structure

A

the coiled or folded chain of amino is often coiled and folded further - more bonds form between different parts of the polypeptide chain, including hydrogen bonds and ionic bonds (attractions between negative and positive charges on different parts of the molecule)
disulphide bridges also form when two molecules of the amino acid cysteine come close together - the sulfur atom in one cysteine bond to the sulfur atom in the other
for proteins made from a single polypeptide chain, the tertiary structure forms their final 3D structure

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14
Q

what is the quaternary structure

A

some proteins are made of several different polypeptide chains held together by bonds
the quaternary structure is the way these polypeptide chains are assembled together
for proteins made from more than one polypeptide chain the quaternary structure is the protein’s final 3D structure

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15
Q

four examples of proteins

A

enzymes, antibodies, transport proteins, structural proteins

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16
Q

how do enzymes structure make them specialised to carry out its particular job

A

enzymes - soluble and often have roles in metabolism, some hep synthesize large molecules
structure: usually roughly spherical in shape due to the tight folding of the polypeptide chain

17
Q

how do antibodies make them specialised to carry out its particular job

A

antibodies - involved in the immune response
structure: made of two light polypeptide chains and two heavy polypeptide chains bonded together
antibodies have variable regions - the amino acid sequences in these regions vary greatly

18
Q

transport proteins make them specialised to carry out its particular job

A

transport protein - transport molecules and ions across membranes
structure: channel proteins are present in cell membranes - channel proteins contain hydrophobic and hydrophilic amino acids, causing the protein to fold up and firm a channel

19
Q

structural protein make them specialised to carry out its particular job

A

structural proteins - physically strong
structure: consist of long polypeptide chains lying parallel to each other with cross links between them
include keratin and collagen

20
Q

what test do you use for proteins

A

biuret test

21
Q

what does a biuret test find out

A

if a substance contained protein

22
Q

what are the two stages to a biuret test

A

(1) test solution needs to be alkaline, so you add a few drops of sodium hydroxide solution
(2) add copper (II) sulfate solution
- if protein is present the solution turns purple
- if no protein solution stays blue