Folding and Unfolding of Two Mixed α/β Peptides
✍ Scribed by Dongqi Wang; Bernhard Jaun; Wilfred F. van Gunsteren
- Publisher
- John Wiley and Sons
- Year
- 2009
- Tongue
- English
- Weight
- 714 KB
- Volume
- 10
- Category
- Article
- ISSN
- 1439-4227
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📜 SIMILAR VOLUMES
## Abstract A systematic analysis of the substituent influence on the formation of the unique secondary structure type of “mixed” helices in the homologous α‐, β‐, and γ‐peptides was performed on the basis of ab initio molecular orbital theory. Contrary to the common periodic peptide helices, mixed
## Abstract Stopped flow CD (SFCD) kinetic studies of self–assembly of coiled coils of rabbit αα–tropomyosin and of nonpolymerizable αα–tropomyosin (NPTm) are reported. The protein was denatured in 6__M__ urea buffer, then renatured by 10‐fold dilution into benign saline buffer. Folding was monitor