Protein Structure And Function Flashcards

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1
Q

What are proteins made up of?

A

Polypeptide chains made up of amino acids

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2
Q

What are the 4 main groups of an amino acid?

A

An amino group, a carboxyl group, a hydrogen atom and a side chain.

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3
Q

What is an amino acid called when it has been joined by a peptide bond to make a protein?

A

An amino acid residue

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4
Q

Name 3 basic amino acids and 2 acidic.

A

Basic - Lysine, Arginine, Histidine

Acidic - Aspartate and Glutamate

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5
Q

Which groups lies at the N terminal of a protein and which at the C terminal?

A

N - Amino group

C - carboxyl group

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6
Q

What is the basic principle regarding whether the ph of a solution is smaller / bigger that the pk of an amino group?

A

If an amino acid is BASIC then it is PROTONATED, if the ph of a solution is smaller than the pk value of the aa, it is positively charged. This is because the solution is forced to the right, so there are more H+ions.
If an amino acid is ACIDIC then it will be DEPROTONATED - negatively charged. the opposite of what you think it is.

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7
Q

Explain the four different sized structure of proteins.

A

Primary - amino acids arranged like beads on a string.
Secondary - a polypeptide backbone, an alpha helix structure.
Tertiary - 3D configuration of the alpha helix, starts to move a unique structure affecting its function.
Quarternary - A multiple peptide sub-unit - the largest

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8
Q

Where are peptide bonds formed? And what is produced in the process?

A

Formed between the N and C terminals, between the amino group of one aa and carboxyl group of the next. An H20 molecule is produced.

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9
Q

Describe 3 characteristics of peptide bonds.

A

PLANAR - all lie in the same plane
RIGID - They have partial double bond characteristics which make them less flexible.
TRANS CONFIRMATION - This means the bonds form on opposite sides.

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10
Q

What type of bonds stabilise the alpha helix structure?

A

Hydrogen bonds

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11
Q

What amino acid is a helix breaker and why?

A

PROLINE - Makes rotation impossible, stops formation.

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12
Q

What is it could when lots of alpha helixes are put together?

A

A Beta sheet

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13
Q

Name the two tertiary structures for a group of proteins and give an example of each.

A

Fibrous e.g. Collagen - 3 alpha helixes wrapped together.

Globular - a big bundle e/g/ myoglobin.

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14
Q

How would you know an amino acid is neutral? Example?

A

No negative or positive charges on the side chain. E.g. Serine, cysteine.

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15
Q

How would you know if an amino acid is acidic? Example?

A

There would be a negative charge e.g. A COO- group e.g Aspartic acid

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16
Q

How would you know an amino acid is basic? Example?

A

It would have a positive charge, an NH3+ group e.g. Histidine, Lysine, Arginine.

17
Q

What makes an amino acids alkyl?

A

Contains a carbon and hydrogen in its side chain e.g. CH3

18
Q

How would you know an amino acid is aromatic?

A

Big aromatic ring on its side chain