De novo protein design. II. Plasticity in sequence space.

  title={De novo protein design. II. Plasticity in sequence space.},
  author={Patrice Koehl and Michael Levitt},
  journal={Journal of molecular biology},
  volume={293 5},
It is generally accepted that many different protein sequences have similar folded structures, and that there is a relatively high probability that a new sequence possesses a previously observed fold. An indirect consequence of this is that protein design should define the sequence space accessible to a given structure, rather than providing a single optimized sequence. We have recently developed a new approach for protein sequence design, which optimizes the complete sequence of a protein… CONTINUE READING
27 Citations
58 References
Similar Papers


Publications citing this paper.
Showing 1-10 of 27 extracted citations


Publications referenced by this paper.
Showing 1-10 of 58 references


  • TrEMBL in
  • Acid Res. 27, 49-54.
  • 1999
Highly Influential
11 Excerpts

2 . 2 AÊresolution structure analysis of two re ® ned Nacetylneuraminyllactose : wheat germagglutinin isolectin complexes

  • C. S. Wright
  • J . Mol . Biol .
  • 1990
Highly Influential
1 Excerpt

Similar Papers

Loading similar papers…