Skip to main content
Search

Protein folding

Published on December 31, 2025   22 min

A selection of talks on Biochemistry

Please wait while the transcript is being prepared...
0:00
I'm Ivan Campeotto, assistant professor in microbial biotechnology at the University of Nottingham, and today, I will give you an overview of a key process in microbiology called protein folding.
0:15
This lecture aims to introduce protein architectures to you, discuss the driving forces leading to protein folding, explain the folding problem on the computational and conceptual point of use, and discuss the folding problem and the ways to solve it both computationally and experimentally.
0:35
There are several levels of protein structure. The primary structure on the top left is the simple composition of amino acids of a protein. In this example, in the single-letter code, A for alanine and so on, K for lysine, valine, W for tryptophan, Y for tyrosine, H for histidine. And this primary structure already contains all the chemical and physical properties that dictate further levels of organization. But there is no function yet. The second level of organization is the secondary structure in which the primary structure adopts secondary structure elements, like here in orange β strands in these arrows or a helical form called an alpha helix. These secondary structure elements come further together to form a tertiary structure. This is the structure or organization which leads to function and is essential for function. Some proteins also have a quaternary structure where tertiary structure elements come together, in this case four of them, and have another level of organization. They can be independent in their own function, or they can affect each other's function, like in the case of hemoglobin in a process, for instance, called cooperativity.

Quiz available with full talk access. Request Free Trial or Login.