PROTEINS Flashcards

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1
Q

amino acids contain

A

amino group
acid group

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2
Q

General structure of an amino acid

A

hydrogen
amino central carboxyl acid carbon group
group
R group

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3
Q

How many R groups and amino acids

A

20

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4
Q

What reaction / bond joins amino acids

A

peptide bond
condensation reaction

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5
Q

What does a peptide bond look like

A

O=C-N-H

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6
Q

2 amino acids

A

Dipeptide

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7
Q

Many amino acids

A

polypeptide

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8
Q

the beginning and end of a polypeptide chain is called

A

N terminus - H2N
C terminus - COOH

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9
Q

A sequence of amino acids is based of

A

The sequence of bases in DNA

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10
Q

Primary structure

A

The sequence of amino acids in the polypeptide chains which determine the structure
sequence
number and
type
NOT number oreder type

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11
Q

Secondary structure

A

The structure held together by hydrogen bonds between carboxyl groups and amino acid groups in the polypeptide backbone
These are Alpha helix spirals and Beta [pleated] sheets

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12
Q

Alpha helix

A

H bonds are formed between non-adjacent amino acids forming into a helix spiral
Alpha helix is very strong and stable structure

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13
Q

What elements in which groups have H bonds between them

A

The O in the carboxyl group and one of the H in the amino group

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14
Q

Beta [pleated] sheet

A

polypeptide chains are zigzagged forming a sheet of antiparallel strands held together by hydrogen bonds

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15
Q

Tertiary structure

A

The compact globular structure is formed by folding a polypeptide chain
They are responsible for the functions and properties of the proteins eg. active sit of the enzyme

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16
Q

How is the tertiary structure held together

A

By bonds between the R groups of amino acids, so the shape of the protein is dependant on the order of the amino acids and the type of amino acid

17
Q

What are the 3 bonds that make the globular structure

A

Weak H bonds
Ionic bonds
Strong Sulphur bridges (covalent S-S bonds between two cysteine amino acids)

18
Q

What causes inwards and outwards protein folding

A

Hydrophobic interactions (inward)
Hydrophilic interactions (outward)

19
Q

Quaternary structure

A

the interactions and numbers of polypeptide chains in a protein

20
Q

Examples of quaternary structure

A

ATP
Hemoglobin
Collagen

21
Q

Globular and Fibrous proteins

A

The final 3D shape of a protein

22
Q

globular protein examples

A

Most proteins
-enzymes
-membrane proteins
-receptors
-storage proteins

23
Q

fibrous proteins roles

A

long and thin usually with structural roles

24
Q

fibrous proteins examples

A

-collagen
-keratin
-cytoskeleton

25
Q

What bonds and structures are broken when an enzyme denatures and what remains

A

-Secondary,tertiary and quaternary structures are broken due to the breaking of Hydrogen bonds
-Primary structure remains intact along with the covalent bonds and disulphide bridges

26
Q

What is the biochemical test for proteins

A

1-Add equal volumes of sodium hydroxide to an aqueous protein sample
2-Add a few drops of aqueous copper sulfate
3-When mixed the solution turns purple when the proteins present
-NaH + H2O
-add CuSO4 + H2O
-purple

27
Q
A