Hi, There are some problems with this entry which prevent the manual from compiling. I'll fix this problem.
Regards, Edward On 15 August 2014 15:11, <[email protected]> wrote: > 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 > [email protected] > > 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 _______________________________________________ relax (http://www.nmr-relax.com) This is the relax-devel mailing list [email protected] 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-devel
