Loading
Apuntes
Study Reminders
Support
Text Version

Nucleic Acids, Proteins and Lipids - Lesson Summary

Set your study reminders

We will email you at these times to remind you to study.
  • Monday

    -

    7am

    +

    Tuesday

    -

    7am

    +

    Wednesday

    -

    7am

    +

    Thursday

    -

    7am

    +

    Friday

    -

    7am

    +

    Saturday

    -

    7am

    +

    Sunday

    -

    7am

    +

Page 1
An amino acid molecule has an amine group and a carboxylic acid group.
The isoelectronic point or isoionic point is the pH at which the amino acid does not migrate in an electric field. This means it is the pH at which the amino acid is neutral, i.e. the zwitterion form is dominant.
Ninhydrin test is a very sensitive test to detect the presence of amino acids or proteins in any substance.
Proteins are large biological macromolecules composed of amino acids.
An amino acid sequence has two types of bonds - the phi (φ)and psi (ψ) bonds, which are in different planes.
The Secondary Structure of a protein molecule can either assume alpha helix or beta-sheet forms depending on the rotation around the Phi bond or the Psi bond.
By making a Ramachandran plot, protein structural scientists can determine which torsional angles are permitted and can obtain insight into the structure of peptides.
When a protein assumes its Tertiary Structure, it becomes a functional protein.
The Quaternary Structure of a protein is formed when it has many peptide subunits.
Unfolding or denaturation of a protein implies breaking all the bonding interactions present in the tertiary structure to bring it back to a primary form.
There are primarily three types of interactions that dictate the formation of the tertiary structure of a protein: Electrostatic interaction, Hydrophobic interactions and formation of the disulfide bond.

Page 2
A classic study of how proteins fold and unfold was done by Professor Anfinsen, who won the Nobel Prize for his work.
Anfinsen found out that urea can be used to denature a protein.
After denaturation with urea, the disulfide bonds remain; these can be broken with the reagent beta-mercaptoethanol.
Slow removal of urea (by dialysis) is the first step of the protein refolding process.
The formation of the tertiary structure of a protein is a thermodynamically favourable process.
Apart from DNA and RNA, other kinds of biomolecules also contain nucleobases and if we can develop similar compounds in the laboratory, they will be useful as drugs to treat various diseases.
If we know how to break the molecules depending upon the structure, we can work the process backwards to synthesize the same molecules in the laboratory. This process is known as Retrosynthesis.
A faster and higher-yielding method of producing pyrimidine-base compounds is by the use of Lewis acid in a microwave reaction.