Proteins Flashcards

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1
Q

Size of proteins

A

Usually very large

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2
Q

Each organism…

A

Makes its own unique proteins. It’s proteins that give the organism their characteristics and allow key functions to occur

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3
Q

Proteins are key biological molecules - why?

A

The shape is highly specific and there fore different to other type of types

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4
Q

Monomers of proteins

A

Amino acids

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5
Q

Amino acids contain which elements?

A

Nitrogen (N), Carbon (C), Oxygen (O), Hydrogen (H) and sometimes sulphur (S)

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6
Q

Variety of proteins: Different roles

A

-Haemoglobin -> Transports oxygen by binding to it
-Antibodies -> Defends the body against infection
-Enzymes -> Biological catalysts
-Actin and myosin -> Involved in muscle contraction

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7
Q

Variety of proteins: Structural role

A

-Keratin -> Found in nails, hair and hooves
-Collagen -> Found in tendons

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8
Q

How many types of amino acids?

A

20 different types of amino acids, all with the same general structure

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9
Q

Essential and non-essential amino acids

A

You must ingest the essential amino acids in your diet, non-essential amino acids can be synthesised by your body

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10
Q

General amino acid structure

A

H H O
| | | |
H—-N—-C—-C—-OH
|
R

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11
Q

Each amino acid contains

A

A central carbon and 4 different chemical groups
-A nitrogen containing amine group (NH^2 or H^2N)
-A carboxyl group (COOH)
-A hydrogen atom (H)
-A ‘R’ variable side chain or group

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12
Q

What is different in amino acids in the general structure?

A

‘R’ variable side chain. Each R group has a different size and are grouped together by different properties e.g. charge and polarity

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13
Q

Formation of a peptide bond

A

Two amino acids joined together to form a dipeptide by a condensation reaction. The hydroxyl group (OH) from the carboxyl group of one amino acid reacts with a hydrogen (H) from the amine group of the second amino acid via a condensation reaction. The water is removed in the formation of a PEPTIDE BOND

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14
Q

Many (hundreds of) amino acids form what?

A

Form a polypeptide chai as a result of many condensation reactions

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15
Q

Important points of peptide bonds

A

-A peptide chain will always have an amine group at one end (N terminus) and a carboxyl at the other end (C terminus)
-Number of peptide bonds in the chain will be one less than the number of amino acids originally joined together

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16
Q

Proteins structure

A

Primary -> Secondary -> Tertiary -> Quaternary

17
Q

Primary structure

A

-The number and sequence of amino acids in a polypeptide chain. Because there is 20 amino acids, there is a limitless number of possible sequences
-Determines the positions of the bonds = Hydrogen, ionic and disulphide -> between R groups and final shape of protein
-Specific shape indicates it’s function

18
Q

Secondary structure

A

-The linked amino acids all have -NH and -C=O groups on either side of the polypeptide chain. NH group has overall positive charge and C=O has an overall negative charge.
-A hydrogen bond forms between the slight positive charge on the H and the slight negative charge on oxygen
-These 2 groups form weak hydrogen bonds through put the polypeptide but because there is so many they are strong
-Due to hydrogen bonding the chain coils into alpha helices or folds it’s beta pleated-sheets

19
Q

Tertiary structure

A

-This is the further folding of the secondary structure into a specific, complex 3D shape
-R groups on the amino acids determine how the chain folds into 3D specific shape.
-Held together by bonds and interactions between R groups of different amino acids
-Hydrogen bonds = weak bonds and easily broken with increasing temperature
-Ionic bonds = Weak but not as week as hydrogen. Bonds form between oppositely charged R groups and are broken by changes in pH