Srinivasan, R. ; Balasubramanian , R. ; Rajan , S. S. (1976) Extended helical conformation newly observed in protein folding Science, 194 (4266). pp. 720-722. ISSN 0036-8075
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Official URL: http://www.sciencemag.org/content/194/4266/720.sho...
Related URL: http://dx.doi.org/10.1266/science.982035
Abstract
A new secondary structure, which shows regularity within the experimental error, is noticed in alpha-chymotrypsin, and considering its extended nature, the name epsilon-helix has been suggested for the same. The average observed values of phi and psi for this conformation are -93 degrees and +146 degrees, respectively. The helical parameters turn out to be n=2.7 and h=3.3 angstroms.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to American Association for the Advancement of Science. |
| ID Code: | 36616 |
| Deposited On: | 12 Apr 2011 10:23 |
| Last Modified: | 12 Apr 2011 10:23 |
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