2 Proteins and enzymes Flashcards

1
Q

What monomers are proteins made up of?

A

amino acids

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2
Q

Fibrous proteins form long _______ chains and have _______ functions, such as collagen

A

fibrous proteins have long parallel chains and have structural functions, such as collagen

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3
Q

Globular proteins are ______ and have many _______ functions (e.g., enzymes)

A

globular proteins are spherical and have many metabolic functions (e.g., enzymes)

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4
Q

What are the 2 groups common to all amino acid molecules?

A

amine group and carboxyl group

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5
Q

What does the R group on an amino acid represent?

A

a side group/ chain

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6
Q

What type of bond is formed when 2 amino acids join?

A

peptide bond

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7
Q

What is a molecule called that is made up of 2 amino acids?

A

dipeptide

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8
Q

What is a molecule called that is made up of many amino acids?

A

polypeptide

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9
Q

What is a molecule called that contains one or more polypeptides?

A

functional protein

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10
Q

What does a protein with a primary structure look like?

A

a polypeptide chain, no extra bonding

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11
Q

Describe the primary structure of a protein

A

sequence of amino acids in polypeptide chain

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12
Q

What 2 forms can secondary structures of a protein take?

A

alpha helix or beta-pleated sheet

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13
Q

What type of bond is involved in secondary structure formation of proteins?

A

hydrogen bond

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14
Q

Which 3 bonds can form between polypeptides in tertiary protein structures creating their shape?

A

hydrogen, ionic, disulfide bonds

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15
Q

Describe the quaternary structure of a protein

A

separate polypeptides linked together

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16
Q

Where does the reaction take place in an enzyme?

A

active site

17
Q

What is formed when the substrate has attached to an enzyme?

A

enzyme-substrate complex

18
Q

Enzymes are biological _______

A

enzymes are biological catalysts

19
Q

Enzymes are ________ to a particular substrate

A

enzymes are specific to a particular substrate

20
Q

The active site has a specific 3D shape, which is ____________ to the substrate

A

the active site has a specific 3D shape, which is complimentary to the substrate

21
Q

Each enzyme lowers the ___________ energy of its reaction

A

each enzyme lowers the activation energy of its reaction

22
Q

What test is used to identify proteins, and what results are shown when a protein is present?

A

biuret test- pale blue to lilac

23
Q

What can be carried out to identify the components of a mixture of unknown amino acids?

A

chromatography

24
Q

What will happen to the rate of an enzyme-controlled reaction if the concentration of enzyme is increased?

A

it will increase, provided there is enough substrate (more enzyme-substrate complexes)

25
What will happen to the rate of enzyme-controlled reaction if the temperature is increased?
it will increase, until the temperature denatures the enzyme
26
What is a competitive inhibitor?
a non-substrate molecule that fits in the active site of an enzyme
27
Which type of protein structure does haemoglobin have?
quaternary
28
What is a non-competitive inhibitor?
non-substrate molecule that binds to non-functional part of enzyme and changes specific shape of active site
29
What is the accepted model of enzyme action called?
induced-fit model
30
Describe the induced-fit model of enzyme action
- shape of active site of enzyme not fully complementary to substrate molecule - when substrate collides with active site, enzyme changes shape to fit active site around substrate --> enzyme-substrate complex --> reaction