Science, Aug 2nd

Iddo Friedberg (
Mon, 19 Aug 1996 15:01:44 +0300 (GMT+0300)


Better late than never...

For all those interested: Science, (1996) 273:545-708 (Aug. 2nd): a
special Bioinformatics issue. Of specific interest to PPSers: pages
610 (perspectives) and the accompanying article 666-669.

To summarize: the authors use a simplified model for examining protein
folding: a self-repelling 27 aa chain folded into a 3x3x3 cubic lattice.
"Amino acids" are of two kinds: hydrophobic (H) and polar (P). Instead of
looking at "foldability", that is selecting potentially functional
sequences, the authors look at "designability": starting from a given
structure, how many sequences may fold that way. Some structures are
*very* designable, while others are not. The highly designable structures
exhibit "proteinlike" secondary structures. Also, the sequnces for highly
designable structures exhibit well-conserved 'residues'. To quote
"...These results suggest that protein structures are selected in nature
because they are readily designed and stable against mutations, and that
such a selection simultaneously leads to thermodynamic stability".

Discussion, anyone?



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