PHYS: Protein folding progress
Max More (maxmore@primenet.com)
Thu, 23 Oct 1997 12:11:36 -0700
>6. A NEW APPROACH TO THE DE NOVO DESIGN OF PROTEINS
>An argument can be made that the unraveling of the mysteries of
>enzymes and other proteins will depend on the possibility of
>tinkering systematically with structure. Certainly that has been
>the thrust of much research aimed at relating structure to
>function. Until now, the primary method of tinkering has been
>genetic alteration, changing the gene that codes for a specific
>protein, hopefully in a manner such that the specific change in
>the protein is known, and then examining the effect of the change
>in protein structure on protein function. This is good tinkering,
>but not the best sort of tinkering. Ideally, one would want to be
>able to design and synthesize proteins, and then systematically
>examine the functions of various structural designs. Twenty years
>ago, that was a dream. These days, the dreams of molecular
>biologists are turning into reality at a breathtaking pace.
>Bassil I. Dahiyat and Stephen L. Mayo (California Institute of
>Technology, US) report the first fully automated folding design
>and experimental validation of a novel sequence for an entire
>protein. They used a computational design algorithm based on
>physico-chemical potential functions and stereochemical
>constraints to screen a combinatorial library of (1.9)10exp(27)
>possible amino acid sequences for compatibility with a particular
>folding design target. The authors suggest this result demonstr-
>ates that unbiased computational methods can successfully be used
>for protein design. QY: S. Mayo <steve@mayo.caltech.edu>
>(Science 3 Oct 1997)
>
Max More, Ph.D.
more@extropy.org
http://www.primenet.com/~maxmore
President, Extropy Institute: exi-info@extropy.org, http://www.extropy.org