introduction/main.tex: Cite dyson05 for unstructured proteins

This seems like an unambiguous reference ;).

diff --git a/src/introduction/main.tex b/src/introduction/main.tex
index ed9df9dd56ef9318b67b778dffa4ad518fff1807..e51088496874819f0a4e68d81e5c811f664e0b74 100644 (file)
--- a/src/introduction/main.tex
+++ b/src/introduction/main.tex
@@ -178,7 +178,7 @@ understanding to design drugs with a particular conformation, or
 predict the conformation of a biologically important receptor
 (\cref{sec:folding-problem}).  Understanding protein unfolding is less
 directly useful, because unfolded proteins are rarely biologically
-relevant (although it does happen\cref{TODO}).
+relevant (although it does happen\cref{dyson05}).
 
 The focus on unfolding is mainly because it's easier to unravel
 proteins by pulling on their ends (\cref{sec:procedure}) than it is to

diff --git a/src/root.bib b/src/root.bib
index 76416b1dbdb8e3cd24853cf1d5747fd919d02b3d..153af54b83a5e2a1d4e25aa153977e243685fed2 100644 (file)
--- a/src/root.bib
+++ b/src/root.bib
@@ -275,6 +275,7 @@
 @string{DDunlap = "Dunlap, D."}
 @string{PDunn = "Dunn, P."}
 @string{VDupres = "Dupres, Vincent"}
+@string{HJDyson = "Dyson, H.~Jane"}
 @string{EMBORep = "EMBO Rep"}
 @string{EMBO = "EMBO Rep."}
 @string{REckel = "Eckel, R."}
@@ -743,6 +744,7 @@
 @string{NAT = "Nature"}
 @string{NSB = "Nature Structural Biology"}
 @string{NSMB = "Nature Structural Molecular Biology"}
+@string{NRMCB = "Nature Reviews Molecular Cell Biology"}
 @string{SNaylor = "Naylor, S."}
 @string{CNeagoe = "Neagoe, Ciprian"}
 @string{BNeelam = "Neelam, B."}
@@ -1125,6 +1127,7 @@
 @string{TWoodage = "Woodage, T."}
 @string{GRWoodcock = "Woodcock, Glenna R."}
 @string{JRWortman = "Wortman, J. R."}
+@string{PEWright = "Wright, Peter E."}
 @string{DWu = "Wu, D."}
 @string{GAWu = "Wu, Guohong A."}
 @string{JWWu = "Wu, Jong-Wuu"}
@@ -10809,3 +10812,43 @@
     concentrations.  Interestingly, the binding is found to be both
     salt- and residue-specific.},
 }
+
+@article{ dyson05,
+  author = HJDyson #" and "# PEWright,
+  title = {Intrinsically unstructured proteins and their functions.},
+  journal = NRMCB,
+  year = 2005,
+  month = mar,
+  address = {Department of Molecular Biology and Skaggs Institute
+             for Chemical Biology, The Scripps Research Institute,
+             10550 North Torrey Pines Road, La Jolla, California
+             92037, USA. dyson@scripps.edu},
+  volume = 6,
+  number = 3,
+  pages = {197--208},
+  issn = {1471-0072},
+  doi = {10.1038/nrm1589},
+  url = {http://www.ncbi.nlm.nih.gov/pubmed/15738986},
+  language = {eng},
+  keywords = {CREB-Binding Protein},
+  keywords = {Humans},
+  keywords = {Nuclear Proteins},
+  keywords = {Nucleic Acids},
+  keywords = {Protein Binding},
+  keywords = {Protein Processing, Post-Translational},
+  keywords = {Protein Structure, Tertiary},
+  keywords = {Proteins},
+  keywords = {Trans-Activators},
+  keywords = {Tumor Suppressor Protein p53},
+  abstract = {Many gene sequences in eukaryotic genomes encode entire
+    proteins or large segments of proteins that lack a well-structured
+    three-dimensional fold. Disordered regions can be highly conserved
+    between species in both composition and sequence and, contrary to
+    the traditional view that protein function equates with a stable
+    three-dimensional structure, disordered regions are often
+    functional, in ways that we are only beginning to discover. Many
+    disordered segments fold on binding to their biological targets
+    (coupled folding and binding), whereas others constitute flexible
+    linkers that have a role in the assembly of macromolecular
+    arrays.},
+}