r25079 - in /trunk/docs/latex: bibliography.bib dispersion.tex -- August 19, 2014 - 16:22

Author: bugman
Date: Tue Aug 19 16:22:23 2014
New Revision: 25079

URL: http://svn.gna.org/viewcvs/relax?rev=25079&view=rev
Log:
Fixes for r25026 (http://thread.gmane.org/gmane.science.nmr.relax.scm/22775).

There were multiple formatting problems with the added bibtex item which have 
been fixed.  The
citation label and contents has also been standardised to match the rest of 
the bibliography.


Modified:
    trunk/docs/latex/bibliography.bib
    trunk/docs/latex/dispersion.tex

Modified: trunk/docs/latex/bibliography.bib
URL: 
http://svn.gna.org/viewcvs/relax/trunk/docs/latex/bibliography.bib?rev=25079&r1=25078&r2=25079&view=diff
==============================================================================
--- trunk/docs/latex/bibliography.bib   (original)
+++ trunk/docs/latex/bibliography.bib   Tue Aug 19 16:22:23 2014
@@ -6027,33 +6027,33 @@
   doi            = {10.1021/ja00012a001}
 }
 
-@InCollection{PalmerKroenkeLoria01,
-  Author         = {Palmer, 3rd, A. G. and Kroenke, C. D. and Loria, J. 
Patrick},
-  Editor         = {Thomas L. James, Volker Dötsch and Uli Schmitz},
+@InCollection{Palmer01,
+  Author         = {Palmer, 3rd, A. G. and Kroenke, C. D. and Loria, J. P.},
+  Editor         = {Thomas L. James, Volker D\:otsch and Uli Schmitz},
   Title          = {Nuclear magnetic resonance methods for quantifying 
microsecond-to-millisecond motions in biological macromolecules},
-  BookTitle      = [Nuclear Magnetic Resonance of Biological Macromolecules 
- Part B},
-  Series         = {Methods in Enzymology},
+  BookTitle      = {Nuclear Magnetic Resonance of Biological Macromolecules 
- Part B},
+  Series         = me,
   Pages          = {204-238},
-  Publisher      = {Academic Press},
-  Volume         = {339},
+  Publisher      = {Academic Press},
+  Volume         = {339},
   Address        = {Department of Biochemistry and Molecular Biophysics, 
Columbia University, New York, New York 10032, USA.},
   issn           = {0076-6879},
   doi            = {10.1016/S0076-6879(01)39315-1},
-  url            = {http://dx.doi.org/10.1016/S0076-6879%2801%2939315-1},
+  url            = {http://dx.doi.org/10.1016/S0076-6879\%2801\%2939315-1},
   abstract       = {Publisher Summary Intramolecular motions on ps-ns time 
scales in proteins in solution can be characterized by heteronuclear 
                     laboratory frame spin relaxation nuclear magnetic 
resonance (NMR) spectroscopy using established experimental protocols. 
                     The relaxation rate constants depend on the spectral 
density functions that quantify the frequency dependence of stochastic 
                     motions modulating the dipolar, chemical shift 
anisotropy (CSA), or quadrupolar interactions. The relaxation data are 
                     interpreted in terms of overall rotational diffusion of 
the molecule and intramolecular dynamics at specific atomic sites. 
                     Important applications of these methods have emerged for 
characterizing conformational entropy in proteins. 
-                    This chapter focuses on a subset of 13C and 15N 
heteronuclear ZZexchange, Carr–PurcellMeiboom–Gill (CPMG), and R1ρ15 
relaxation 
-                    techniques that are sensitive to molecular motions or 
chemical kinetic processes on μs–ms time scales. 
-                    Line-shape analysis or dynamic NMR is an established 
technique for investigating μs–ms time scale kinetic processes in 
solution. 
+                    This chapter focuses on a subset of 13C and 15N 
heteronuclear ZZ-exchange, Carr-Purcell-Meiboom-Gill (CPMG), and R1rho15 
relaxation 
+                    techniques that are sensitive to molecular motions or 
chemical kinetic processes on us-ms time scales. 
+                    Line-shape analysis or dynamic NMR is an established 
technique for investigating us-ms time scale kinetic processes in solution. 
                     However, heteronuclear 2H, 13C, and 15N spectra of 
macromolecules usually are recorded in an indirect dimension of 
multidimensional proton-detected 
                     NMR experiments and the limited digital resolution 
hinders line-shape analysis. 
                     Consequently, ZZ-exchange, CPMG, and R1ρ spin 
relaxation techniques are preferable for the investigation of dynamic 
processes 
-                    in proteins using heteronuclear NMR spectroscopy.}
-  year =         = 2001,
+                    in proteins using heteronuclear NMR spectroscopy.},
+  year           = 2001
 }
 
 @Article{PalmerMassi06,

Modified: trunk/docs/latex/dispersion.tex
URL: 
http://svn.gna.org/viewcvs/relax/trunk/docs/latex/dispersion.tex?rev=25079&r1=25078&r2=25079&view=diff
==============================================================================
--- trunk/docs/latex/dispersion.tex     (original)
+++ trunk/docs/latex/dispersion.tex     Tue Aug 19 16:22:23 2014
@@ -2050,7 +2050,7 @@
     \end{pmatrix},
 \end{equation}
 
-Reasonable limits for the exchange rate can be found in 
\citet{PalmerKroenkeLoria01}, p. 224.
+Reasonable limits for the exchange rate can be found in \citet{Palmer01}, p. 
224.
 ``In most cases of practical interest, CPMG experiments in proteins will be 
applicable to chemical exchange processes with values of $\kex < 1e^4$''.
 ``$\Ronerho$ experiments will be limited to values of $\kex < 1e5$, or 
approximately an order of magnitude faster than CPMG experiments.''
 The linear constraints for exchange rate is therefore set dependent on 
experiment type, and is set to