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Chemistry > Biochemistry > Flashcards

Biochemistry Flashcards

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1
Q

Structure of an amino acid

A

Amino group (NH2), alpha carbon, hydrogen, carboxylic acid group (COOH), variable side chain (R)

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2
Q

Functional groups of an amino acid

A

An amine group (-NH2) and a carboxylic acid acid (COOH)

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3
Q

How do naturally occurring amino acids differ

A

The R group

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4
Q

Which amino acid isn’t optically active

A

Glycine

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5
Q

Why are amino acids optically active

A

They have a chiral carbon

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6
Q

Which which optical isomer naturally occurs and what is the effect on plane polarised light

A

L-isomer rotates plane polarised light anti-clockwise (the left)

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7
Q

Can amino acid acids act as a base or an acid

A

Both an acid and a base

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8
Q

Does an amino acid act as an acid or a base in a solution of acid

A

Base

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9
Q

Does an amino acid act as an acid or a base in a solution of base

A

Acid

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10
Q

Does an amino acid act as an acid or a base in a solution of isoelectric pH

A

Zwitterion so both

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11
Q

Which part of an amino acid accepts a proton

A

The lone pair on the NH2

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12
Q

Which part of the amino acid donates a proton

A

Carboxylic acid

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13
Q

What is the isoelectric point

A

pH at which is has no net charge. Midway between two pKa of its two functional groups

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14
Q

Which amino acid has the variable group H

A

Glycine

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15
Q

Charge on an amino acid in a acidic solution

A

Positive

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16
Q

Are cations positive or negative

A

Positive

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17
Q

What binds join amino acids in a protein

A

Peptide

18
Q

What sort of polymers are proteins

A

Condensation polymers

19
Q

Define fibrous proteins

A

Long chains of polypeptides found in bundles and insoluble in water

20
Q

Define globular proteins

A

Polypeptide chains folded into roughly spherical shapes that are soluble in water

21
Q

Example of globular protein

A

Haemoglobin

22
Q

Example of fibrous protein

A

Keratin

23
Q

Define primary structure

A

The order of alpha-amino acids in a protein

24
Q

How do you determine the order of amino acids in a protein

A

Systematically hydrolyse the protein chain and identify each amino acid

25
Q

How do you separate amino acids

A

TLC or paper chromatography

26
Q

What is a proteins secondary structure caused by

A

Caused by hydrogen bonding between the N-H and the C=O groups of the peptide links along the protein chain causing alpha helix and beta pleated sheets

27
Q

Define alpha helix

A

Hydrogen bonds formed every four amino acids forcing the chain into a cylindrical formation. Elastic and flexible.

28
Q

Define beta pleated sheets

A

Parallel regions of the protein line up allowing hydrogen bonds to form between them, leading to a flat sheet like structure.

29
Q

Where do you find beta pleated sheet proteins

A

In association with Alzheimer’s

30
Q

Define tertiary structure

A

The overall 3D shape of a protein. Maintained by hydrogen bonds, ionic interactions and disulphides bonds between R groups of amino acids

31
Q

What is the tertiary structure necessary for

A

Biochemical activity

32
Q

What is broken when a protein is denatured

A

Tertiary structure

33
Q

What are disulphides bonds

A

Between two -SH variable groups. Form strong S-S bonds

34
Q

How can sulphide bonds be broken

A

They are destroyed by heat, reduction or reaction with a base

35
Q

Define enzyme

A

Proteins that act as biological catalysts, providing an alternative reactions of lower Eact

36
Q

How do enzymes works

A

Substrates bond in an active site.

37
Q

Define lock and key hypothesis

A

Only molecules that have the right shape can fit into the active site

38
Q

What determines how a substrate will bind

A

The size and orientation of an amino acid

39
Q

How does a substrate bind to the active site

A

Hydrogen bonding, ionic bonding, and van der waals forces

40
Q

What does a stereospecific active site cause

A

An active site which bonds to only one enantiomer of a racemate

41
Q

Define enzyme inhibitor

A

A molecule that binds to an enzyme active site and decrease its activity is called an enzyme inhibitor

Chemistry (24 decks)

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