Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Organic chemistry and synthesis A2 > Amino acids > Flashcards

Amino acids Flashcards

You may prefer our related Brainscape-certified flashcards:
AP® Chemistry flashcards Periodic Table flashcards Chemistry 101 flashcards Organic Chemistry 101 flashcards
1
Q

What functional groups does an amino acid contain?

A

Amino group and carboxylic acid group

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

Amino acids can combine in what type of reaction?

A

A condensationreaction

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

If 2 amino acids combine what is produced?

A

A dipeptide

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

If 2 different types of amino acids combine what will be produced?

A

2 different types of dipeptide

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

What is produced when more than 2 amino acids combine?

A

A polypeptide which leads to protein formation

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

What does R represent in…
Glycine (2-aminoethanoicacid)
Alanine (2-aminopropanoicacid)
Serine (2-amino-3-hydroxypropanoicacid)

A

Glycine- H
Alanine- CH3
Serine- CH2OH

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

What is a primary protein structure?

A

The precise sequence of amino acids in the protein chain - many sequences with different amino acids

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

What is. Secondary protein structure

A

How parts of the protein fold up to form an alpha helix (held in shape by hydrogen bonds involving peptide link) or a beta pleated sheet (paper shape stabilised by hydrogen bonds between amino acids in different polypeptide chains)

Results in hydrogen bonding
Occurs between N-H and C=O groups of polypeptide chains

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

What is a tertiary protein structure

A

Proteins as a whole and the way in which alpha helices and beta pleated sheets of protein fold with respect to eachother

This structure is held together by interactions eg
Intramolecular- covalent and ionic bonds
Intermolecular - VDW and H bonds

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

Draw acids hydrolysis of peptide/amide link

A

..

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

Draw alkaline hydrolysis of peptide/amide link

A

..

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

What do amino acids predominantly exist as and what are these?

A

Zwitterions: these are internal sales and neutral molecules

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

Draw a zwitterion

A

..

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

Draw the zwitterionic nature of amino acids in acidic conditions

A

..

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

Draw the zwitterionic nature of amino acids in alkaline conditions

A

..

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

What are the properties of amino acids?

A

High melting points- have strong ionic bonding (IMF) lots of energy to overcome bonding and melt

Soluble in water due to ionic properties

17
Q

Reaction of amino acids with ethanoyl chloride

A

Has to be done in a fume cupboard as hydrogen chloride produced

Dry conditions

Produces:

CH3CONHCHRCOOH

18
Q

Structure of an amino acid

A

NH2CH(R)COOH

19
Q

How to make an amino acid into a zwitterion

A

Remove the far end H and put it into the N instead

20
Q

How does a secondary structure arise from a primary?

A

From hydrogen bonding between N-H groups in one part and C=O groups in Another part- this is due to parts of the protein folding to form an alpha helix or a beta pleated sheet

21
Q

Explain importance of proteins in living systems

A

Cotton fibres contain protein fibres

Essential in all living matter eg muscle

Enzymes are made up of them- biocatalysts in living cells carry out complex reactions. They’re sensitive to changes in Temp and pH

22
Q

Why do amino acids have high MPS?

A

They have strong ionic bonding(IMF) lots of energy needed to overcome bonding and melt them

23
Q

What happens to the structure of a zwitterion under acidic conditions?

Why?

A

The carboxyl group is removed and replaced with a hydroxy group (OH)

Because the zwitterion acts as a base under acidic conditions so accepts H+

24
Q

What does the zwitterion act as under acidic conditions?

A

A base- accepts H+

25
Q

What happens to the structure of zwitterion under alkaline conditions?

Why?

A

A H is removed

Because under alkaline conditions the zwitterion acts as a acid so donates H+

26
Q

What happens to structure of an amino acid in formation of a zwitterion?

A

a H is moved from the end to the N

Positive charge put in the N
Negative charge on the Oxygen that’s left on the end

27
Q

What is a zwitterion

A

An internal salt which is a neutral molecule

28
Q

If you have a secondary protein structure: what bonding will occur between molecules?

A

Hydrogen bonds

Organic chemistry and synthesis A2 (16 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions