Please enable JavaScript.
Coggle requires JavaScript to display documents.
Proteins (Structure (Secondary (The protein folds itself, resulting in a…
Proteins
-
Structure
Primary
The basic sequence of amino acids, with no importance due to its 3D shape.
Its amino acids determine the shape of the other structures, due to their interactions.
Secondary
The protein folds itself, resulting in a different structure.
-
In beta-pleated sheets the AA connect themselves laterally until they make a twist at the end by using dipole-dipole interactions.
In the alpha helix, a helix is created through the use of hydrogen bonds.
Tertiary
The protein folds itself even more, taking a 3D shape.
-
-
Can also occur via Van der Waals forces, hydrogen bonds, salt briges or disulfate bonds, which are a type of covalent bond for when sulfur is present.
Quaternary
Several tertiary proteins come together through electrostatic interactions, forming a larger protein.
-
-
Characterization
Coloration
Ninhidrine
The alpha groups of the amino acids react with ninhidrine, creating a purple-coloured complex when heated.
The more amino acids, the stronger the colour of the purple.
-
-
Peptide bonds can also result in dipeptides, oligopeptides (3-10 aminoacids) and polypeptides.
There are other types of secondary structures, but these are the most common.
A-helixes are usually represented by coils, while b-p sheets are represented by arrows.
In tertiary structues, hydrophobic AA will hide in its interior.
-