proteins Flashcards

1
Q

what are the monomers for protein

A

amino acids

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2
Q

all proteins contain which elements

A

-nitrogen
-carbon
-hydrogen
-oxygen

some contain sulfur

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3
Q

why do proteins have a specific role

A

because each protein has a specific shape

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4
Q

amino acids can link together in a chain of peptide bonds to form…

A

a polypeptide

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5
Q

what bond links/binds together amino acids

A

peptide bond

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6
Q

how many different types of amino acids are there

A

20, and they all have the same general formula

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7
Q

what is the general formula for an amino acid

A

R-CH(NH2)-COOH

H R O
I I II
N - C - C
I I I
H H OH

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8
Q

give the structure of an amino acid

A

-each amino acid contains a central alpha carbon to which a nitrogen containing amine group (H2N) and a carboxyl group (COOH) are attached
-the R group indicates the variable group (20 different options)

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9
Q

R groups can be….

A

-positively charged
-negatively charged
-hydrophilic attracted to water
-hydrophobic repelled by water

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10
Q

how is a peptide bond formed

A

the hydroxyl group from one amino acid combines with a hydrogen atom from the amino group in the second amino acid to form a water molecule which is removes and a bond is formed

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11
Q

what is formed when two amino acids join together

A

dipeptide

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12
Q

if there is 10 amino acids present how many peptide bonds are there

A

9, always one less than number of amino acids

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13
Q

what is a protein

A

a polymer made up of the monomers amino acids- chain of amino acids

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14
Q

what is the primary structure

A

-number and sequence and order of amino acids in a polypeptide chain
-proteins are different from each other because their primary structures, amino acids sequence and numbers are different.

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15
Q

what is the secondary structure

A

-it is a 2D shape
- polypeptide folds into alpha helixes or/and beta pleated sheets
- held together by many weak hydrogen bonds between the C=O groups of the carboxyl group of one amino acid and H in the amine group of another

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16
Q

what is the tertiary structure

A

-further folding of secondary structure/polypeptide chain into a specific unique 3D shape
-the R groups on the amino acids in polypeptide chain determine how the chain folds into it’s specific 3D shape

17
Q

why is the tertiary structure essential to a protein’s function

A
  • the shape of protein determines how it interacts with other molecules which is necessary for it to carry out its specific function
18
Q

what is the quaternary structure

A

-protein is made up of two or more polypeptide chains joined together
-sometimes there may be a prosthetic group (non-protein component) in a protein
-haemoglobin is an example and its a globular protein

19
Q

what are globular proteins

A

-they are functional proteins
-approx spherical shape
-soluble in water because globular proteins have got hydrophilic amino acids on their surface so that the hydrophilic R groups can interact with water molecules
-they are transport proteins such as haemoglobin, lipase,DNA polymerase and insulin

20
Q

give examples of globular proteins

A

-they are transport proteins such as haemoglobin, lipase,DNA polymerase and insulin

21
Q

what are fibrous proteins

A

-are structural proteins
-often play a structural role for example in bones or tendons or in the walls of blood vessels such as arteries
-fibrous proteins tend to form long rope-like molecules and 3 alpha helixes
-they have a large proportion of amino acids with hydrophobic R groups therefore they are insoluble in water
-they are tough and strong

22
Q

give 3 examples of fibrous proteins

A

collagen
keratin
elastin

23
Q

why are antibodies only effective against a specific pathogen

A

-antigens on pathogens have a specific shape/3D structure
-antibodies are complementary to the antigen so they bind to it and form antibody-antigen complex

24
Q

when do proteins denature

A

only at high temps and large changes to pH

25
Q

where are the bonds in the tertiary structure formed

A

ionic bonds (quite weak bonds) form between oppositely charged R groups
-weak hydrogen bonds form between C=O and NH of adjacent amino acids
-disulphide bonds only sometimes form if there is Sulfur in the R groups, and they are strong bonds formed between cysteine amino acids only