amino acids, proteins & DNA Flashcards

1
Q

How many bonds does a and t form

A

2 hydrogen bonds

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2
Q

How many bonds does c and g form

A

3 hydrogen bonds

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3
Q

What is the monomer, nucleotide of DNA made from

A

A phosphate
A sugar
A base

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4
Q

What is an example of an anti-cancer drug

A

cis-platin.

This has the formula [PtCl2(NH3)2]

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5
Q

How does cis platin prevent DNA replication

A

The CIS isomer has 2 Cl ligands adjacent to each other, and 2 NH3 ligands. It works by binding to the DNA in cancerous cells.

This prevents the DNA from unwinding and so the cancer cell cannot replicate.

This prevents the growth and spreading of cancerous cells.

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6
Q

What are the considerations of cis platin

A

-Cis-platin will also bind to the DNA in healthy cells.
- This can cause unwanted side effects.
- The cis-platin drug can be targeted straight to the cancer cells to reduce the effect on healthy tissue.
- It can also be used in minimal amounts.

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7
Q

How is a zwitterion formed in acidic conditions

A

If the ‘R’ group contains an amine group, this can also get protonated.

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8
Q

How is a zwitterion formed in acidic conditions

A

If the ‘R’ group contains a COOH group, this can also get deprotonated.

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9
Q

What are proteins

A

Proteins are sequences of amino acids joined by peptide links

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10
Q

What is the primary structure of proteins

A

The sequence of amino acids in a protein is called the primary structure

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11
Q

What is the secondary structure of proteins

A

The secondary structure is only held in place by H-bonds. These are approximately 1/10th the strength of a covalent bond, and so can be broken by gentle heating or changes in pH.

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12
Q

What is the tertiary structure and what is it held in place by

A

The α-helix or β-pleated sheet can itself be folded into a 3D shape called a tertiary structure.

The tertiary structure can be held in place by:
- Hydrogen bonds
- Some ionic interactions (i.e. the COO- on one amino acid, and the NH3+ on another)
- Disulfide bonds

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13
Q

What can two cysteine amino acids can form

A

a disulphide bond

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14
Q

What are enzymes

A

Proteins

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15
Q

What is stereo specific

A

The shape of the active site is so specific to the substrate that in many cases one optical isomer may fit whereas another optical isomer may not fit

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16
Q

Describe enzyme inhibition - how drugs work

A

(1) An undesirable biological process occurs which is catalysed by an enzyme.

(2) A computer is used to determine the shape of the active site, and design another molecule which will fit into the active site. This must be the correct enantiomer.

(3) The new molecule is called the inhibitor. This fits into the active site and prevents the substrate from reacting in the active site.