hi all, we are writing up the structure determination of a dimeric human enzyme. while going through the model (~750 residues per monomer), i noticed that the protein contains rather few lysines (1.8%) and isoleucines (2.7%), and rather many prolines (7.5%) and phenylalanines (6.5%). (if i remember correctly, there are no low-complexity regions in the sequence.) i would be grateful for any clues or literature references that might tell us if this is statistically to be expected or unusual and -if the latter- what could explain it, and whether or not it might have any significance. also, a pointer to a table of the average amino-acid composition of soluble human proteins (or enzymes) would be useful. thanks in advance for any input ! --gerard ****************************************************************** Gerard J. Kleywegt [Research Fellow of the Royal Swedish Academy of Sciences] Dept. of Cell & Molecular Biology University of Uppsala Biomedical Centre Box 596 SE-751 24 Uppsala SWEDEN http://xray.bmc.uu.se/gerard/ mailto:gerard at xray.bmc.uu.se ****************************************************************** The opinions in this message are fictional. Any similarity to actual opinions, living or dead, is purely coincidental. ******************************************************************