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<div style="direction: ltr;font-family: Tahoma;color: #000000;font-size: 10pt;">Hi Christine-<br>
In general, their contribution will be roughly proportional to the inverse of the metal density in the computation of vbar from composition. The confounding part is that their ionization will cause electrostriction of water, if they remain charged when bound.
If the ions are bound in such a way to be neutral (i.e. they are chelated by charged residues), then the approximation using their density will not be as much in error as it would be if they remain charged.<br>
Best wishes,<br>
Tom<br>
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<div style="direction: ltr;" id="divRpF202434"><font color="#000000" face="Tahoma" size="2"><b>From:</b> rasmb-bounces@list.rasmb.org [rasmb-bounces@list.rasmb.org] on behalf of EBEL Christine [christine.ebel@ibs.fr]<br>
<b>Sent:</b> Thursday, February 27, 2014 4:45 AM<br>
<b>To:</b> rasmb@list.rasmb.org<br>
<b>Subject:</b> [RASMB] vbar of protein binding zinc and cupper ions<br>
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<h1><font size="-1">Dear all, </font></h1>
<h1><font size="-1">Does somebody know how bound Zn++ or Cu++ ions affect vbar of proteins?</font></h1>
<h1><font size="-1">Thank you in advance <br>
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<h1><font size="-1">Christine</font><br>
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<pre class="moz-signature" cols="72">--
Institut de Biologie Structurale
UMR 5075 CEA - CNRS - Univ. Grenoble Alpes
EPN Campus, 6 rue Jules Horowitz, F-38000 Grenoble
Tel.: +33 (0)4 5742 8570; Fax: +33 (0)4 7650 1890
E mail: <a class="moz-txt-link-abbreviated" href="mailto:Christine.Ebel@ibs.fr" target="_blank">Christine.Ebel@ibs.fr</a> <a class="moz-txt-link-freetext" href="http://www.ibs.fr" target="_blank">http://www.ibs.fr</a>
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