< Back to previous page

Project

FoldMod: The role of local amino acid interactions in protein folding, fold stability and the location of post-translational modifications. (FWOAL796)

Proteins are molecular machines essential for the functioning of cells in all living organisms. Each protein is composed of a long chain of amino acids, connected to each other by a shared chemical structure (the protein backbone). Different proteins have a different sequence of amino acids, and this sequence determines how the protein backbone folds in space, how it can move, and how the protein functions.

Moreover, in cells some amino acids in proteins can be chemically modified, so altering the function or organization of the protein. Many protein sequences are known, but only for some experimental data on their fold, movements and chemical modifications is available.

There is therefore a need for fast computational approaches that can predict from the sequence what the protein is able to do. This project addresses the following questions from a computational angle: 1) can we find out where proteins start to fold, 2) does that help us to understand how proteins keep their fold and 3) can we then better identify where proteins become modified? We will also design new protein sequences based on our insights, which will be tested by experimental collaborators.
Date:1 Jan 2016 →  31 Dec 2019
Keywords:Proteins
Disciplines:Biomedical modelling