From: W. Trevor King <wking@tremily.us>
Date: Sat, 17 Nov 2012 14:07:42 +0000 (-0500)
Subject: root.bib: add roman12 entry for Marisa's thesis
X-Git-Tag: v1.0~298
X-Git-Url: http://git.tremily.us/?a=commitdiff_plain;h=8211f1d38178d238b98d990bae88a23eaadd71d9;p=thesis.git

root.bib: add roman12 entry for Marisa's thesis
---

diff --git a/src/root.bib b/src/root.bib
index 218b5cc..6915d81 100644
--- a/src/root.bib
+++ b/src/root.bib
@@ -223,6 +223,7 @@
 @string{LDougan = "Dougan, Lorna"}
 @string{LDoup = "Doup, L."}
 @string{TDrobek = "Drobek, T."}
+@string{Drexel = "Drexel University"}
 @string{OKDudko = "Dudko, Olga K."}
 @string{ADunham = "Dunham, A."}
 @string{DDunlap = "Dunlap, D."}
@@ -755,7 +756,7 @@
 @string{RRodriguez = "Rodriguez, R."}
 @string{YHRogers = "Rogers, Y. H."}
 @string{SRogic = "Rogic, S."}
-@string{MRoman = "Roman, Marisa"}
+@string{MRoman = "Roman, Marisa B."}
 @string{GRomano = "Romano, G."}
 @string{DRomblad = "Romblad, D."}
 @string{RRos = "Ros, Robert"}
@@ -7710,6 +7711,54 @@
   language =     "eng",
 }
 
+@phdthesis { roman12,
+  author = MRoman,
+  title = "Macromolecular crowding effects in the mechanical unfolding
+    forces of proteins",
+  school = Drexel,
+  year = 2012,
+  month = may,
+  url = "http://hdl.handle.net/1860/3854",
+  eprint = "http://idea.library.drexel.edu/bitstream/1860/3854/1/Roman_Marisa.pdf",
+  keywords = "Physics",
+  keywords = "Biophysics",
+  keywords = "Protein folding",
+  abstract = "Macromolecules can occupy a large fraction of the volume
+    of a cell and this crowded environment influences the behavior and
+    properties of the proteins, such as mechanical unfolding forces,
+    thermal stability and rates of folding and diffusion. Although
+    much is already known about molecular crowding, it is not well
+    understood how it affects a protein’s resistance to mechanical
+    stress in a crowded environment and how the size of the crowders
+    affect those changes. An atomic force microscope-based single
+    molecule method was used to measure the effects of the crowding on
+    the mechanical stability of a model protein, in this case I-27. As
+    proteins tend to aggregate, single molecule methods provided a way
+    to prevent aggregation because of the very low concentration of
+    proteins in the solution under study. Dextran was used as the
+    crowding agent with three different molecular weights 6kDa, 10 kDa
+    and 40 kDa, with concentrations varying from zero to 300 grams per
+    liter in a pH neutral buffer solution at room temperature. Results
+    showed that the forces required to unfold biomolecules were
+    increased when a high concentration of crowder molecules were
+    added to the buffer solution and that the maximum force required
+    to unfold a domain was when the crowder size was 10 kDa, which is
+    comparable to the protein size. Unfolding rates obtained from
+    Monte Carlo simulations showed that they were also affected in the
+    presence of crowders. As a consequence, the energy barrier was
+    also affected. These effects were most notable when the size of
+    the crowder was 10 kDa, comparable to the size of the protein. On
+    the other hand, distances to the transition state did not seem to
+    change when crowders were added to the solution. The effect of
+    Dextran on the energy barrier was modeled by using established
+    theories such as Ogston’s and scaled particle theory, neither of
+    which was completely convincing at describing the results. It can
+    be hypothesized that the composition of Dextran plays a role in
+    the deviation of the predicted behavior with respect to the
+    experimental data.",
+  language = "eng",
+} 
+
 @article { measey09,
   author =       TMeasey #" and "# KBSmith #" and "# SDecatur #" and "# 
                  LZhao #" and "# GYang #" and "# RSchweitzerStenner,