amino acids, proteins and DNA Flashcards

1
Q

at nuetral pH and in solid state amino acids exist as

A

zwitterions
H from COOH removed so COO- and added to NH2 forming +NH3

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

structure of amino acid

A

H2N-CHR-COOH

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

at low pH amino acids exist as

A

+NH3-CHR-COOH gained h has more acidic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

at high pH amoni acids exist as

A

NH2-CRH-COO- as more alkaline so loses H

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

proteins are

A

condensation polymers of amino acids joined by peptide links

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

the importance of hydrogen bonding and disulphite bonds in proteins

A

hold proteins in shape ,
hydrogen bonding exist between polar groups(-OH and -NH2) stabilize the secondary and tertiary structure of protein
disulphite bonding between cysteine, link diff part of protein chain together help to stabilise the tertiary strucutre

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

primary structure of protiens

A

number and order of amino acids in polypepetide chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

seconday structure of protiens

A

peptide links form hydrogen bonds with each other resulting in alpha helix or beta pleated sheets

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

tertiary structure of proteins

A

3D tertiary structure
disulphite bonds
hyrogen bonds
ionic bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

hydrolysis of the peptide link produces

A

the constituent amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

how can amino acids be sperated and identified

A

thin layer chromotgraphy
used developing agents such as ninhydrin or UV light to locate then caluculate Rf values

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

enzymes are

A

proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

action of enzymes as catalysts

A

substrate fit exactly into the active site that is stereospecific so only bond to one enantiomer of a substrate.
enzyme substrate complex forms reducing the Ea to break bonds within the molecule and catalyses’ the reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

principle of a drug acting as an enzyme inhibitor

A

similar shape to sunstrate so compete with the substrate to bond to the active site but no reaction follows instead they block the active site so no sunstrate can fit in

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

how can drugs’ acting as enzymes inhibitor be deigned

A

computers
if an undesirable biological process occurs which is catalyzed by and enzyme a computer is used to determine the shape of an active site and design another molecule that will fit into the active site (must be correct enantiomers)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

explain why a stereospecific active site can only bind to one enantiomeric form of a substrate of drug

A

as active site made up of amino acids so contain chiral centers

17
Q

a nucleotide is made up from

A

a phosphate ion bonded to 2-deoxyribose which is bonded to one of the 4 bases (adenine, cytosine, guanine and thymine)

18
Q

a single strand of DNA is a polymer of

A

nucleotides are phosphate group of one nucleotide bonded to the 2-deoxyribose of another nucleotide, this results in a sugar-phosphate-sugar-phosphate polymer chain with baes attached to the sugars in the chain

19
Q

DNA exist as

A

2 complemtnetory strands arranged in the form of double helix

20
Q

explain how the hydrogen bonding between base pairs leads to the two complemtnetory stands of DNA

A

complementary base pairing exists in DNA helix where adenine always pairs with thymine with 2 hydrogen bonds and guanine always pairs with cytosine with 3 hydrogen bonds

21
Q

expample of anti-cancer drug and how it works

A

cisplatin
prevents DNA replication in cancer cells by a ligand replacement reaction with DNA in which a bond is formed between platinum and nitrogen atom on guanine. this prevents DNA from unwinding so cancerous cell cannot replicate

22
Q

consisderations of cisplatin

A

will also bind to the DNA in healthy cells which can cause unwanted side effects
the drug can be targeted straight to the cancer cells to reduce the effect on healthy tissue
can also be used in minimal amounts