HELIX v. 1.5
© 1994-97
Andersen Research
Group
Department of Chemistry, University of Washington
This program simulates the alpha-helix/random
coil transition in the secondary structures of peptides and proteins
using a two-state matrix algorithm based upon the Lifson-Roig model.
The abstract of the
research paper which has been submitted to Protein Science.
Here is a demostration of the program.
- The minimum length of the sequence is 13, the maximum is 60.
- The charge is assigned automatically according to the pH.
- Checkout which residues have been defined.
You can also view or download individual source
files and compile them using Makefile (requires gcc).
Supporting files (you must have these two files in order
to run the program) |
|
Other secondary structure predition web sites
can be found at NIH.
Last updated 3/10/97
htong@u.washington.edu
