Proteins - amino acids Flashcards

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1
Q

what is an amino acid

A

monomers of all proteins with the same basic structure

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2
Q

what are peptides

A

polymers made up of amino acid molecules (the monomers)

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3
Q

what do proteins consist of

A

one or more polypeptides arranged as complex macromolecules and they have specific biological functions.

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4
Q

what do all proteins contain

A

the elements carbon, hydrogen, oxygen and nitrogen. sometimes contain sulfur

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5
Q

what structural properties do proteins have

A

they are the main component of body tissues such as muscle, skin, ligaments and hair

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6
Q

what catalytic properties do proteins have

A

all enzymes are proteins, catalysing many biochemical reactions

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7
Q

what signalling properties do proteins have

A

many hormones and receptors are proteins

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8
Q

what immunological properties do proteins have

A

all antibodies are proteins

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9
Q

what do the protein constituents on membranes act as

A

carriers and pores for active transport across the membrane and facilitated diffusion

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10
Q

how many different amino acids are there

A

over 500

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11
Q

how many amino acids are found in proteins

A

20

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12
Q

what does each protein chain of amino acids have

A

an amine group (-NH2) on one end and a carboxyl group (-COOH) at the other end

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13
Q

what does the R group represent

A

a side chain from the central “alpha” carbon atom and can be anything from a simple hydrogen atom to a more complex ring structure. R groups can vary by size, by charge and by polarity with some being hydrophobic and some hydrophillic

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14
Q

even though each amino acid has the same general structure, what makes each one different

A

the nature of the R group which defines an amino acid. different R groups result in different amino acids.

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15
Q

how do each of 20 amino acids act in our body

A
  • 5 are non essential as our bodies are able to make them from other amino acids.
  • 9 are essential and can only be obtained from what we eat
  • 6 are conditionally essential as they are only needed by infants and growing children
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16
Q

what is the simplest amino acid

A

glycine

17
Q

how do amino acids act as buffers

A

when dissolved in water, the amine group and carboxyl group can ionise. this means the amine group can accept an H+ ion to change from NH2 to NH3+. the carboxyl can give up an H+ to change from COOH to COO-. the carboxyl group acts as an acid in producing H+ ions. the amine group acts as a base in accepting H+ions

18
Q

how does the amine group act as a base

A

in accepting H+ions
at low pH (lots of H+ ions in solution), the amino acid will accept H+ ions
at high pH (where there are fewer H+ ions in solution) the amino acid will release H+ ions

19
Q

why are amino acids amphoteric

A

this means amino acids have acidic and basic problems. in a long chain of amino acids, you will amine and carboxyl groups on each end, but there are also many on the R groups of different amino acids

20
Q

how are protein chains affected by this amphoteric nature

A

by accepting and releasing H+ ions, amine acids can help to regulate changes in pH. this is known as buffering

21
Q

what is a buffer

A

a substance which helps to resist large changes in pH

22
Q

how are amino acids joined together

A

by covalent bonds called peptide bonds

23
Q

how are peptide bonds like glycosidic bonds and ester bonds

A

making a peptide bond involved condensation reactions and breaking peptide bpnds involves hydrolysis.

24
Q

what do protease enzymes break down

A

in the intestine, they break down peptide bonds during digestion. they also break down protein hormones so their effects aren’t permanent.

25
Q

when do amino acids join

A

the R groups are not involved. the hydroxyl in the carboxylic acid group of one amino acids reacts with a hydrogen in the amine group of another amino acid. a peptide bond is formed between the amino acids and water is produced

26
Q

what is the resulting compound when two amino acids join together

A

a dipeptide molecule

27
Q

what does joining a larger chain of amino acids result in

A

polypeptide

28
Q

what is the reaction to form polypeptides catalysed by

A

the enzyme peptidyl transferase present in ribosomes

29
Q

what can proteins consist of

A

a single polypeptide chain or more than one chain bonded together.

30
Q

how do different R groups interact with each other

A

to form different types of bonds

31
Q

what do the different sequences of amino acids lead to

A

different structures with different shapes being produced. the very specific shapes of proteins are vital for the many functions proteins have with living organisms

32
Q

why does the peptide bond have some properties of a double bond

A

the peptide bond is depicted as a single bond but due to the electron arrangement around the bond, it has some properties of a double bond. this means the bond is shorter than a conventional C-N bond. it inhibits rotation around the peptide bond. this makes the polypeptide chain relatively stiff and rigid