Author: bugman
Date: Wed Nov 6 14:22:39 2013
New Revision: 21394
URL: http://svn.gna.org/viewcvs/relax?rev=21394&view=rev
Log:
Added the Korzhnev et al., 2005 reference to the bibliography file for the
manual.
Modified:
branches/relax_disp/docs/latex/bibliography.bib
Modified: branches/relax_disp/docs/latex/bibliography.bib
URL:
http://svn.gna.org/viewcvs/relax/branches/relax_disp/docs/latex/bibliography.bib?rev=21394&r1=21393&r2=21394&view=diff
==============================================================================
--- branches/relax_disp/docs/latex/bibliography.bib (original)
+++ branches/relax_disp/docs/latex/bibliography.bib Wed Nov 6 14:22:39 2013
@@ -3865,6 +3865,76 @@
year = 2004
}
+@Article{Korzhnev05,
+ Author = {Korzhnev, D. M. and Neudecker, P. and Mittermaier, A.
+ and Orekhov, V. Y. and Kay, L. E.},
+ Title = {Multiple-site exchange in proteins studied with a
+ suite of six {NMR} relaxation dispersion experiments:
+ an application to the folding of a {F}yn {SH}3 domain
+ mutant.},
+ Journal = jacs,
+ Volume = {127},
+ Number = {44},
+ Pages = {15602-15611},
+ abstract = {The three-site exchange folding reaction of an
+ (15)N-labeled, highly deuterated Gly48Met mutant of the
+ Fyn SH3 domain has been characterized at 25 degrees C
+ using a suite of six CPMG-type relaxation dispersion
+ experiments that measure exchange contributions to
+ backbone (1)H and (15)N transverse relaxation rates in
+ proteins. It is shown that this suite of experiments
+ allows the extraction of all the parameters of this
+ multisite exchange process in a robust manner,
+ including chemical shift differences between exchanging
+ states, from a data set recorded at only a single
+ temperature. The populations of the exchanging folded,
+ intermediate, and unfolded states that are fit are 94,
+ 0.7, and 5\%, respectively. Despite the small fraction
+ of the intermediate, structural information is obtained
+ for this state that is consistent with the picture of
+ SH3 domain folding that has emerged from other studies.
+ Taken together, the six dispersion experiments
+ facilitate the complete reconstruction of (1)H-(15)N
+ correlation spectra for the unfolded and intermediate
+ states that are "invisible" in even the most sensitive
+ of NMR experiments.},
+ authoraddress = {Departments of Medical Genetics, Biochemistry, and
+ Chemistry, The University of Toronto, Toronto, Ontario
+ M5S 1A8, Canada.},
+ keywords = {Deuterium Exchange Measurement ; Magnetic Resonance
+ Spectroscopy/*methods ; Mutation ; Nitrogen Isotopes ;
+ *Protein Folding ; Proteins/*chemistry ; Proto-Oncogene
+ Proteins c-fyn/*chemistry/genetics ; src Homology
+ Domains},
+ language = {eng},
+ medline-aid = {10.1021/ja054550e [doi]},
+ medline-crdt = {2005/11/03 09:00},
+ medline-da = {20051102},
+ medline-dcom = {20060208},
+ medline-edat = {2005/11/03 09:00},
+ medline-fau = {Korzhnev, Dmitry M ; Neudecker, Philipp ; Mittermaier,
+ Anthony ; Orekhov, Vladislav Yu ; Kay, Lewis E},
+ medline-is = {0002-7863 (Print) ; 0002-7863 (Linking)},
+ medline-jid = {7503056},
+ medline-jt = {Journal of the American Chemical Society},
+ medline-lr = {20120605},
+ medline-mhda = {2006/02/09 09:00},
+ medline-own = {NLM},
+ medline-pl = {United States},
+ medline-pmid = {16262426},
+ medline-pst = {ppublish},
+ medline-pt = {Journal Article ; Research Support, Non-U.S. Gov't},
+ medline-rn = {0 (Nitrogen Isotopes) ; 0 (Proteins) ; EC 2.7.10.2
+ (FYN protein, human) ; EC 2.7.10.2 (Proto-Oncogene
+ Proteins c-fyn)},
+ medline-sb = {IM},
+ medline-so = {J Am Chem Soc. 2005 Nov 9;127(44):15602-11.},
+ medline-stat = {MEDLINE},
+ url =
{http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?cmd=prlinks&dbfrom=pubmed&retmode=ref&id=16262426},
+ doi = {10.1021/ja054550e},
+ year = 2005
+}
+
@Article{KullbackLeibler51,
Author = {Kullback, S. and Leibler, R. A.},
Title = {On information and sufficiency},
r21394 - /branches/relax_disp/docs/latex/bibliography.bib