## Abstract We compare folding trajectories of chymotrypsin inhibitor (CI2) using a dynamic Monte Carlo scheme with Goβtype potentials. The model considers the four backbone atoms of each residue and a sphere centered around C^Ξ²^ the diameter of which is chosen according to the type of the side gro
Optimizing protein folding to the native state in bacteria
β Scribed by Catherine H. Schein
- Publisher
- Elsevier Science
- Year
- 1991
- Tongue
- English
- Weight
- 447 KB
- Volume
- 2
- Category
- Article
- ISSN
- 0958-1669
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β¦ Synopsis
A correctly folded protein is usually both active and soluble. This review focuses on novel ways to improve the folding of recombinant proteins during production in bacteria and includes a few tips for refolding proteins. Major results in correlating protein primary structure with proper folding and stability, and the production of viral antigens and antibodies in bacteria are also discussed.
π SIMILAR VOLUMES
## Background: We present a simple method to train a potential function for the protein folding problem which, even though trained using a small number of proteins, is able to place a significantly large number of native conformations near a local minimum. the training relies on generating decoys b