From: W. Trevor King Date: Thu, 27 Jun 2013 17:51:35 +0000 (-0400) Subject: salt/main.tex: Cite hofmeister88 and smith13 X-Git-Tag: v1.0~20 X-Git-Url: http://git.tremily.us/?a=commitdiff_plain;h=da9e44b020c16f22f65d5ef2a17e0fea4fcef48f;p=thesis.git salt/main.tex: Cite hofmeister88 and smith13 Additional background and CaCl2 motivation respectively. --- diff --git a/src/salt/main.tex b/src/salt/main.tex index 3befaec..512aa44 100644 --- a/src/salt/main.tex +++ b/src/salt/main.tex @@ -9,9 +9,11 @@ standard buffer, a buffer with additional calcium (from \CaCl\citep{fisher-CaCl}) was flushed into the fluid cell. After the new buffer equilibrated, unfolding experiments were continued. -Previous research on the effect of ions on unfolding forces is small, -although earlier experimental work on amyloid $\beta$ shows decreased -fibrillation with even small +Since \citet{hofmeister88}, there has been a lot of research on the +effect of ions on protein solubility. However, previous research on +the effect of ions on unfolding forces is small, but we do have some +material to work with. Earlier experimental work on amyloid $\beta$ +shows decreased fibrillation with even small \Ca\ concentrations\citep{chauhan97,itkin11}. The mechanism behind this weaker bonding is unclear\citep{chauhan97,zhang06}, although aspartic and glutamic acid groups tend to have a strong affinity for @@ -19,7 +21,11 @@ cations while arginine has a strong affinity for the \Cl\ anion\citep{friedman11}. Of these amino acids, only glutamic acid occurs in the key hydrogen bond regions responsible for I27 unfolding\citep{lu00b} (\cref{fig:I27:H-bonds}). \NaCl\ has also been -shown to decrease hydrogen bonding\citep{zidar11}. +shown to decrease internal hydrogen bonding in the +protein\citep{zidar11}. In molecular dynamics studies of amalyoid +$\beta$ fragments, the destabilizing effect of \CaCl\ is much greater +than the destabilizing effects of \MgCl, \NaCl, and +\KCl\citep{smith13}. \begin{figure} \begin{center}