r21006 - /branches/relax_disp/docs/latex/bibliography.bib -- October 07, 2013 - 15:41

Author: bugman
Date: Mon Oct  7 15:41:52 2013
New Revision: 21006

URL: http://svn.gna.org/viewcvs/relax?rev=21006&view=rev
Log:
Added Tollinger reference.

Progress sr #3071: https://gna.org/support/index.php?3071 - Implementation of 
Tollinger/Kay dispersion model (2001)
Following the guide at: 
http://wiki.nmr-relax.com/Tutorial_for_adding_relaxation_dispersion_models_to_relax

Troels E. Linnet provided this patch. Commit by: tlinnet _aaattt_ 
gmail_dot_com

Signed-off-by: Edward d'Auvergne <edward@xxxxxxxxxxxxx>

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=21006&r1=21005&r2=21006&view=diff
==============================================================================
--- branches/relax_disp/docs/latex/bibliography.bib (original)
+++ branches/relax_disp/docs/latex/bibliography.bib Mon Oct  7 15:41:52 2013
@@ -6211,6 +6211,47 @@
   year           = 1996
 }
 
+@Article{Tollinger01,
+  Author         = {Tollinger, M. and Skrynnikov, N.R. and Mulder, F.A.A. 
and Forman-Kay, J.D. and Kay, L.E.},
+  Title          = {Slow Dynamics in Folded and Unfolded States of an SH3 
Domain},
+  Journal        = jacs,
+  Volume         = {123},
+  Pages          = {11341-11352},
+  Number         = {46},
+  abstract       = {15N relaxation dispersion experiments were applied to 
the isolated
+                   N-terminal SH3 domain of the Drosophila protein drk (drkN 
SH3) to
+                   study microsecond to second time scale exchange 
processes. The drkN
+                   SH3 domain exists in equilibrium between folded (Fexch) 
and unfolded
+                   (Uexch) states under nondenaturing conditions in a ratio 
of 2:1 at
+                   20 °C, with an average exchange rate constant, kex, of 
2.2 s-1 (slow
+                   exchange on the NMR chemical shift time scale). 
Consequently a discrete
+                   set of resonances is observed for each state in NMR 
spectra. Within
+                   the Uexch ensemble there is a contiguous stretch of 
residues undergoing
+                   conformational exchange on a μs/ms time scale, likely 
due to local,
+                   non-native hydrophobic collapse. For these residues both 
the Fexch
+                   ↔ Uexch conformational exchange process and the μs/ms 
exchange
+                   event within the Uexch state contribute to the 15N line 
width and
+                   can be analyzed using CPMG-based 15N relaxation 
dispersion measurements.
+                   The contribution of both processes to the apparent 
relaxation rate
+                   can be deconvoluted numerically by combining the 
experimental 15N
+                   relaxation dispersion data with results from an 15N 
longitudinal
+                   relaxation experiment that accurately quantifies exchange 
rates in
+                   slow exchanging systems (Farrow, N. A.; Zhang, O.; 
Forman-Kay, J.
+                   D.; Kay, L. E. J. Biomol. NMR 1994, 4, 727−734). A 
simple, generally
+                   applicable analytical expression for the dependence of 
the effective
+                   transverse relaxation rate constant on the pulse spacing 
in CPMG
+                   experiments has been derived for a two-state exchange 
process in
+                   the slow exchange limit, which can be used to fit the 
experimental
+                   data on the global folding/unfolding transition. The 
results illustrate
+                   that relaxation dispersion experiments provide an 
extremely sensitive
+                   tool to probe conformational exchange processes in 
unfolded states
+                   and to obtain information on the free energy landscape of 
such systems.},
+  doi            = {10.1021/ja011300z},
+  eprint         = {http://pubs.acs.org/doi/pdf/10.1021/ja011300z},
+  url            = {http://dx.doi.org/10.1021/ja011300z},
+  year           = 2001
+}
+
 @Article{TrottPalmer02,
        pmid = {11820837},
        author = {Trott, O. and Palmer, A. G.},