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 R1Ï 15
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 R1Ï 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
_______________________________________________
relax (http://www.nmr-relax.com)
This is the relax-commits mailing list
relax-commits@xxxxxxx
To unsubscribe from this list, get a password
reminder, or change your subscription options,
visit the list information page at
https://mail.gna.org/listinfo/relax-commits