Hi Rob, Hyunchul Kim and Miguel, I was just about to write a comment on this, but Rob was quicker..
Rob is right, our dataset of hen egg-white lysozymes does not contain any structures with resolution lower than 2.3 A....one may say that these are all relatively high-resolution structures, therefore we can not claim there is no correlation between ASA and resolution in general. Nevertheless, we cannot see any correlation in our (limited) dataset.
On the other hand, we also saw that two structures of the same protein differed by hundreds of sq A in their ASA just because a few residues could not be seen in one of these two structures. The conclusion of our paper was identical with Rob's last paragraph (although we forget to use the word "biodegradable"), and it is even more true when one look at individual residues.
I think that The EDS server can provide some hints concerning the reliability of ASA values for individual residues...it allows to check how well are individual residues supported by experimental data, so if a deposited residue conformation is well supported by its electron density map, then its ASA can be quite reliable regardless resolution of a whole structure. However, proteins are dynamic and therefore ASA for individual residues will fluctuate substantially during time (regardless of resolution).
best regards, --marian ############################################################ Marian Novotny Department of Animal Physiology and Developmental Biology Faculty of Natural Sciences Charles University in Prague Vinicna 7 Praha 2 128 43 Czech Republic GPS: 50¡4'20.07"N,14¡25'27.02"E mail: [EMAIL PROTECTED] tel: +420221951766 #############################################################
