De Novo Design of Helical Bundles as Models for Understanding Protein Folding and Function
β Scribed by Hill, R. Blake; Raleigh, Daniel P.; Lombardi, Angela; DeGrado, William F.
- Book ID
- 120444391
- Publisher
- American Chemical Society
- Year
- 2000
- Tongue
- English
- Weight
- 446 KB
- Volume
- 33
- Category
- Article
- ISSN
- 0001-4842
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## Abstract Stereochemistry could be a powerful variable for conformational tune up of polypeptides for de novo design. It may be also useful probe of possible role of interamide energetics in selection and stabilization of conformation. The homopolypeptides AcβXxx~30~βNHMe, with Xxx = Ala, Val, an
The solution to the protein folding problem lies in defining the relative energetic contributions of short-range and long-range interactions. In other words, the tendency of a stretch of amino acids to adopt a final secondary structural fold is context dependent. Our approach to this problem is to a