Development Of Free-Energy Based Models For Chaperonin Containing TCP-1 Mediated Folding Of Actin

Main Category: Biology / Biochemistry
Also Included In: Cancer / Oncology
Article Date: 13 Aug 2008 - 10:00 PDT

email to a friend   printer friendly   opinions  

Molecular chaperones are proteins that help other proteins fold into their characteristic 3D shape. The chaperone CCT (Chaperonin Containing TCP-1) plays a vital role in folding cellular cytoskeletal proteins that are intimately involved in cell structure, division and locomotion.

The mechanism of CCT action is important to current cancer research and is not fully understood. This article introduces a novel theoretical perspective, using a free-energy basis to assess the CCT-mediated folding of actin, the major cytoskeletal protein of all cells.

Such an approach provides a universal platform to address this folding problem, from which two hypothetical folding mechanisms are developed.

Journal of the Royal Society Interface

The Journal of the Royal Society Interface is the Society's cross-disciplinary publication promoting research at the interface between the physical and life sciences. It offers rapidity, visibility and high-quality peer review and is ranked fifth in JCR's multidisciplinary category. The journal also incorporates Interface Focus, a peer-reviewed, themed supplement, each issue of which concentrates on a specific cross-disciplinary subject.

Journal of the Royal Society Interface

• Additional
• References
• Citations