Protein folding is the process by which a protein structure assumes its functional shape or conformation. All protein molecules are heterogeneous unbranched chains of amino acids. By coiling and folding into a specific three-dimensional shape they are able to perform their biological function.
The reverse of this process is protein denaturation, whereby a native protein is caused to lose its functional conformation, and become an amorphous, and non-functional amino acid chain. Denatured proteins may lose their solubility, and precipitate, becoming insoluble solids. In some cases, denaturation is reversible, and proteins may refold. In many other cases, however, denaturation is irreversible.
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Folderol - An open-sourced distributed computing client for exploring the results of the Human Genome Project.
Meta Description: [ The world's largest development and download repository of Open Source code and applications ]
Predictor@home - Distributed project to predict protein folding using the BOINC (Berkeley Open Infrastructure for Network Computing) client.
500The Blueprint Initiative - Blueprint develops, hosts and maintains public biological databases and Bioinformatics software tools such as BIND, SeqHound and Distributed Folding.
A short video about protein primary, secondary, tertiary, and quaternary structure. ...