Nitrogen Compounds revision

interactions that holds these structures in their native

PCl5, reflux conformation
then KCN (alc),
heat
6. β-pleated sheet

Carboxylic
Acid/
NaOH (aq)
Excess conc NH3 reflux
HCl/H2SO4
Sealed tube, ethanol,
(aq)
reflux
reflux

1. Steps to transform:
• Methylbenzene to 4-aminobenzoic acid

i. Conc HNO , conc H SO , 30’C

3 2 4

ii.KMnO , acidified with H SO

4 2 4

iii. Reflux with Sn, followed bt NaOH

• CH3CH2CH2OH to CH3CH2CH(OH)COOH

i. K Cr O
2 2 7 (aq), heat, immediate distillation
ii. HCN in small amount of KCN
iii. HCl (aq), reflux

2. Amines are weak bases

• Due to the availability of a lone pair of electrons on the

nitrogen atom able to form a dative bond with a proton (H+)

• R-NH2 + H2O → R-NH3+ + OH-

3. Relative basicities
• Ammonia < 1° Amine < 2° Amine
Increasing base strength, decreasing pKb →
• Electron-donating R groups increase the basicity by
i. Increasing the electron density of the lone pair
electrons on N, making it more available to
accept a proton, and
ii.Lowering the positive charge on N in the
conjugate and so stabilises it, therefore favouring
• Stabilized by hydrogen-bonds between CO and NH groups
in adjacent strands
• May be antiparallel or parallel
• Side chains on successive AA residues appear on opposite
sides of the sheet
7. α-helix
• Right-hand screw
• NH group in each peptide link is hydrogen-bonded to the
CO group of the fourth following peptide link
• 3.6 amino acids per turn

the forward reaction to produce more OH-

8. The tertiary structure of a protein refers to its three-dimensional
structure of the polypeptide.
4. Acid-base properties of amino acids • Hydrogen bonding
• Amino acids are less acidic than most carboxylic acids, and i. Between polar side chains (-OH, -NH, =O, =NR
less basic than most amines groups)
• van der Waals forces
• Acidic part is the –NH3+ group, basic part is the –COO- group i. Electrostatic interactions among permanent or
• Forms dipolar ions called zwitterions induced dipoles
ii. Hydrophobic interactions – contributed by
• Amphoteric nonpolar side chains which cluster away from
• Pre-dominant form depends on the pH of the solution water to avoid destabilisation of side chains (a
hydrophobic core is formed)
5. Define: • Ionic interactions
i. Between two oppositely charged side chains (e.g.
• Peptide bond – When two amino acids join together Asp and Lys) – usually groups that ionize in water
• Disulphide bridges
• Tripeptide – Three amino acids join together i. Between cysteine residues with the thiol (-SH)
• Primary structure – Sequence of amino acids in the side chain
polypeptide chain ii.R-SH + HS-R’ + [O] → R-S-S-R + H O2

• Secondary structure – Segments of the polypeptide

backbone orientate into a regular pattern through hydrogen 9.
bonding
• Tertiary structure – Three-dimensional structure of the
polypeptide
10. Denaturation of proteins by
• Quaternary structure - Characteristic manner in which the
individually folded polypeptide subunits are grouped
• Denaturation – Disruption in the secondary, tertiary and
quaternary structures by the breaking of the non-covalent
The quaternary structure of protein refers to the spatial arrangements
and association of the polypeptide subunits of proteins.
• Haemoglobin as an example
i. Formed from four polypeptide chains
• Effect of Temperature
i. Heating causes an increase in the thermal
vibration of the molecule

http://education.helixated.com
An Open Source Education Project
2 | Page

ii. Hydrogen bonding is disrupted

iii.Proteins denature and thus unfold
• Effect of pH
i. If pH is lowered far below pI, the protein will only
contain positive charges
ii. Like charges repel each other and cause the
denaturation of proteins
iii. Likewise for high pH

• Effect of Heavy Metal Ions

i. Heavy metal ions (Pb2+, Cd2+, etc) are
positively charged
ii. Compete with positively charged groups for
attraction with negatively charged groups
iii. Also bond with –SH groups (especially Hg2+) and
disrupt disulphide bridges
iv. Resident metal ions in certain proteins may also
be displaced

11. Phenomena of denaturation:

• In denaturation, solubility is drastically decreased, as
occurs when egg white is cooked and the albumins unfold
and coagulate to an insoluble white mass.
• Milk is curdled by bacteria when it sours as the pH is
changed