From owner-biophysics@net.bio.net Mon Oct 05 23:00:00 1998 Path: biosci!ihnp4.ucsd.edu!newsfeed.berkeley.edu!newsfeed.cwix.com!158.43.192.17!rill.news.pipex.net!pipex!bore.news.pipex.net!pipex!not-for-mail From: Simon Brocklehurst Newsgroups: bionet.biophysics Subject: Re: protein folding Date: Tue, 06 Oct 1998 11:27:31 +0100 Organization: Cambridge Antibody Technology Lines: 26 Message-ID: <3619F093.2E1A7048@camb-antibody.co.uk> References: <6v780i$1dn$1@nnrp1.dejanews.com> Reply-To: simon.brocklehurst@camb-antibody.co.uk NNTP-Posting-Host: pc106.camb-antibody.co.uk Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 4.07 [en] (WinNT; I) fromm@nauticom.net wrote: > Is this claim about protein folding, namely that the > proteins are a > [very small] subset of long polypeptides which are special > because they > have good folding properties, true? Most definitely yes. You might want to take a look at the literature in the field of de novo protein design. It is exceptionally difficult to design a sequence that folds into a structure that has the properties of a "natural" protein. Conversely it is easy to introduce just a few mutations into a natural sequence that prevent a polypeptide from folding. Simon -- Simon M. Brocklehurst, Ph.D. Head of Bioinformatics Cambridge Antibody Technology The Science Park, Melbourn, Cambridgeshire, UK http://www.catplc.co.uk/ mailto:simon.brocklehurst@camb-antibody.co.uk .