r25026 - /trunk/docs/latex/bibliography.bib -- August 15, 2014 - 15:11

Author: tlinnet
Date: Fri Aug 15 15:11:06 2014
New Revision: 25026

URL: http://svn.gna.org/viewcvs/relax?rev=25026&view=rev
Log:
Inserted Latex bibliography for reference to Linear Constraints of the 
exchange rate.

Modified:
    trunk/docs/latex/bibliography.bib

Modified: trunk/docs/latex/bibliography.bib
URL: 
http://svn.gna.org/viewcvs/relax/trunk/docs/latex/bibliography.bib?rev=25026&r1=25025&r2=25026&view=diff
==============================================================================
--- trunk/docs/latex/bibliography.bib   (original)
+++ trunk/docs/latex/bibliography.bib   Fri Aug 15 15:11:06 2014
@@ -6024,6 +6024,35 @@
   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},
+  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},
+  Pages          = {204-238},
+  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},
+  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. 
+                    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,
+}
+
 @Article{PalmerMassi06,
   Author         = {Palmer, 3rd, A. G. and Massi, F.},
   Title          = {Characterization of the dynamics of biomacromolecules