proteins Flashcards

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1
Q

how are polypeptides made?

A

amino acids are the basic monomer units that combine to make up a polymer called a polypeptide

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2
Q

what do polypeptides combine to form

A

proteins

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3
Q

what provides indirect evidence for evolution

A

the fact that the same 20 amino acids occur in a living organism provides indirect evidence for evolution

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4
Q

what does every amino acid have

A

a central carbon atom to which is attached to four different chemical groups

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5
Q

what are the four different chemical groups amino acids can be attached to

A

amino group NH2

Carboxyl group COOH

hydrogen atom H

R side group

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6
Q

define amino groups

A

a basic group from which the amino part of the name amino acid is derived

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7
Q

define carboxyl groups

A

an acidic group which gives the amino acid the acid part of its name

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8
Q

define the R (side) group

A

a variety of different chemical groups.

these 20 naturally occurring amino acids differ only in their R (side) group

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9
Q

draw the general structure of an amino acid

A
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10
Q

what do two amino acid monomers combine to form

A

a dipeptide

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11
Q

explain a condensation reaction between two amino monomers

A

the water is made by combining an OH from the carboxyl group of one amino acid with an H from the amino group of another amino acid

the two amino acids then become linked by a new peptide bond between the carbon atom of one amino acid and the nitrogen atom of the other

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12
Q

what breaks peptide bonds

A

a hydrolysis reaction

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13
Q

what do we call a chain with many amino acids

A

a polypeptide

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14
Q

define polymerisation in terms of amino acids

A

through a series of condensation reactions, many amino acid monomers can be joined together in a process called polymerisation

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15
Q

what forms the primary structure of any protein
and what is this determined by

A

the sequence of amino acids in a polypeptide chain.

this sequence is determined by DNA

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16
Q

what determines the shape and function of a protein
what does this mean

A

its primary structure

this means that a change in just a single amino acid in this primary sequence can lead to a change in just a single amino acid in the primary sequence that may stop it from carrying out its function

17
Q

define hydrogen bonds

A

the hydrogen of the NH group has an overall positive charge while the O of the C=O group has an overall negative charge

these two groups therefore readily form weak bonds called hydrogen bonds

18
Q

what do hydrogen bonds cause

A

the long polypeptide chain to be twisted into a 3d shape, such as the coil known as an a-helix

19
Q

what can a-helices do

A

the a-helices of the secondary protein structure can be twisted and folded even more to give the complex, and often specific, 3-D structure of each protein

this is known as the tertiary structure

20
Q

how are tertiary structures maintained

A

by a number of different bonds

where the bonds occur depends on the primary structure of the protein.

21
Q

what bonds maintain the tertairy structure

A

disulfide bridges

ionic bonds

hydrogen bonds

22
Q

describe disulfide bridges

A

they are fairly strong and therefore not easily broken

23
Q

describe ionic bonds

A

they are formed between any carboxyl and amino groups that are not involved in forming peptide bonds.

they are groups that are not involved in forming peptide bonds.

they are weaker than disulfide bonds and are easily broken by changes in PH

24
Q

describe hydrogen bonds

A

they are numerous but easily broken

25
Q

explain why the 3-d shape of a protein is important

A

the 3-d shape of a protein is important when it comes to how it functions

it makes each protein distinctive and allows it to recognise, and be recognised by, other molecules.

it can then interact with them in a very specific way

26
Q

describe the primary structure of a protein

A

the primary structure of a protein is the sequence of amino acids found in its polypeptide chains.

this sequence determines its properties and shape

following the elucidation of the amino acid sequence of the hormone insulin by Frederick sanger in 1954, the primary structure of many other proteins is now known

27
Q

describe the secondary structure of a protein

A

the secondary structure is the shape that the polypeptide chain forms as a result of hydrogen bonding.

this is most often a spiral known as the a-helix, although other configurations occur

28
Q

describe the tertiary structure of a protein

A

the tertiary structure is due to the bending and twisting of the polypeptide helix into a compact structure.

All three types of bond, disulfide, ionic and hydrogen, contribute to the maintenance of the tertiary structure

29
Q

describe the quaternary structure of a protein

A

the quaternary structure arises from the combination of a number of different polypeptide chains and associated non-protein groups into a large, complex protein molecule

30
Q

explain how we perform a test for proteins

A

place a sample of the solution to be tested in a test tube and add an equal volume of sodium hydroxide solution at room temperature

add a few drops of very dilute 0.05% copper(II) sulfate solution and mix gently

a purple coloration indicates the presence of peptide bonds and hence a protein.

if no protein is preset the solution remains blue