Protein structure and enzymes Flashcards

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1
Q

Amino acids

A

Monomers of proteins

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2
Q

Bond formed when amino acids bond together

A

Dipeptide bond

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3
Q

Polypeptide

A

When more than two amino acids join together

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4
Q

Condensation reaction to form polypeptides

A

Amino acids are joined together with a peptide bond forming between Carbon of a carboxyl group and Nitrogen of an amine group. Water is formed as product

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5
Q

Primary structure

A

The sequence of amino acids in a polypeptide chain held together by peptide bonds

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6
Q

Secondary structure

A

Hydrogen bonds from between amino acids in the chain and makes it coil into an alpha or fold into a beta pleated sheet

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7
Q

Tertiary structure

A

The coiled or folded amino acids go further into their final 3D structure with more bonds forming between different parts of the polypeptide chain including hydrogen, disulfide bridges ionic bonds and hydrophobic/philic interactions

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8
Q

Quaternary structure

A

When polypeptide chains are assembled together

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9
Q

Globular proteins

A

Round, compact proteins made up of multiple polypeptide chains
Hydrophobic parts of the chain face inwards and hydrophilicface outwards making it soluble

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10
Q

Adaptations of haemoglobin

A

It is a globular protein so it is soluble and can be easily transported in the blood
Contains iron containing haem groups to bind to oxygen

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11
Q

Fibrous proteins

A

Long molecules made of insoluble peptide chains that are tightly coiled together
Lots of bonds between the chains make it a strong molecule, so they are often found in supportive tissue q

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12
Q

Collagen adaptions

A

Strong fibrous protein found in connective tissue in animals

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13
Q

Enzymes

A

Biological catalysts which lower the activation energy of chemical reactions

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14
Q

Where are enzymes found

A

Everywhere, intracellular and extracellular

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15
Q

Enzyme substrate complex

A

When a substrate binds to the active site of an enzyme

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16
Q

How do enzymes reduce activation energy

A

Holds substrate molecules close together reducing any repulsion so they can bond more easily
Puts strain on bonds in a substrate so it breaks up more easily

17
Q

Induced fit model

A

Active site changes shape when he substrate binds

18
Q

Properties of enzymes

A

Specific so only one complementary substrate will fit onto active site
Each different enzyme has a different tertiary structure so different shaped active site

19
Q

Active site shape

A

Determined by the tertiary structure of the enzyme, which is determine by primary structure

20
Q

How is tertiary shape of enzyme altered

A

Temperature or pH

21
Q

Saturation point

A

When the concentration of enzymes becomes the limiting factor, so adding more sublates doesn’t change anything

22
Q

Why is initial rate of reaction the highest

A

Substrate concentration decreases over time so rate of reaction decreases as well