Unfolding of Proteins: Thermal and Mechanical Unfolding
Abstract
Over the past few decades, researchers have sequenced the human genome which is a blueprint for proteins. However, given only the information of the sequence we cannot yet accurately predict specific structural information such as the secondary and tertiary structure of a given protein, let alone its functionality in biological processes. Recent theoretical and experimental findings have shown that the topology or conformation of the native structure of small proteins plays a critical role in determining its biological function (Baker 2000; Alm & Baker 1999). In order to carry out their biological function properly, proteins must assume a shape, assembling themselves into an ordered structure. It is now well known that depending on the topology of proteins, for example, when proteins do not fold correctly, there can be serious medical complications, such as Parkinson's disease, Alzheimers to name a few. Furthermore, more biophysical manifestations of protein-protein interactions are reflected in processes related to phase equilibria such as crystallization, and in the marked dependence of the diffusion coefficients of macromolecules on their concentration (Price et al. 1999). The latter aspect is currently becoming of much interest to biologists and chemists with advances in techniques for monitoring protein diffusion in the crowded cellular environment (Dayel et al. 1999). With ever increasing areas of interest in biomedical applications as mentioned above, much effort has been put into understanding the mechanism of protein folding. However, at present, there exists neither a simple and universally applicable theoretical framework nor an efficient and accurate computational framework that can account for many experimental findings.
Document Details
- Document Type
- Technical Report
- Publication Date
- Dec 01, 2003
- Accession Number
- ADP014823
Entities
People
- Eric F Darve
- Joe S. Hur
Organizations
- Stanford University