r17361 - /trunk/docs/latex/bibliography.bib -- August 28, 2012 - 17:28

Author: bugman
Date: Tue Aug 28 17:28:52 2012
New Revision: 17361

URL: http://svn.gna.org/viewcvs/relax?rev=17361&view=rev
Log:
Added the Fushman 1999 reference and a few formatting fixes in other 
references.


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=17361&r1=17360&r2=17361&view=diff
==============================================================================
--- trunk/docs/latex/bibliography.bib (original)
+++ trunk/docs/latex/bibliography.bib Tue Aug 28 17:28:52 2012
@@ -426,7 +426,7 @@
 @Article{Bieri11,
    Author = {Bieri, Michael and d’Auvergne, Edward and Gooley, Paul},
    Affiliation = {Department of Biochemistry and Molecular Biology, Bio21 
Molecular Science and Biotechnology Institute, The University of Melbourne, 
Parkville, VIC 3010, Australia},
-   Title = {relaxGUI: a new software for fast and simple NMR relaxation data 
analysis and calculation of ps-ns and μs motion of proteins},
+   Title = {relax{GUI}: a new software for fast and simple {NMR} relaxation 
data analysis and calculation of ps-ns and $\mu$s motion of proteins},
    Journal = jbnmr,
    Publisher = {Springer Netherlands},
    issn = {0925-2738},
@@ -1807,7 +1807,7 @@
 }
 
 
-@article{Erdelyi11,
+@Article{Erdelyi11,
 Author = {Erdelyi, Mate and d'Auvergne, Edward and Navarro-Vazquez, Armando 
and
    Leonov, Andrei and Griesinger, Christian},
 Title = {{Dynamics of the Glycosidic Bond: Conformational Space of Lactose}},
@@ -2181,6 +2181,20 @@
   medline-stat   = {MEDLINE},
   url            = 
{http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?cmd=prlinks\&dbfrom=pubmed\&retmode=ref\&id=9054979},
   year           = 1997
+}
+
+@article{Fushman99,
+  author = {Fushman, D. and Tjandra, N. and Cowburn, D.},
+  title = {An Approach to Direct Determination of Protein Dynamics from 
{15N} {NMR} Relaxation at Multiple Fields, Independent of Variable {15N} 
Chemical Shift Anisotropy and Chemical Exchange Contributions},
+  journal = jacs,
+  volume = {121},
+  number = {37},
+  pages = {8577-8582},
+  year = {1999},
+  doi = {10.1021/ja9904991},
+  URL = {http://pubs.acs.org/doi/abs/10.1021/ja9904991},
+  eprint = {http://pubs.acs.org/doi/pdf/10.1021/ja9904991},
+  abstract = { An approach to protein dynamics analysis from 15N relaxation 
data is demonstrated, based on multiple-field relaxation data. This provides 
a direct, residue-specific determination of both the spectral density 
components, the 15N chemical shift anisotropy (CSA) and the conformational 
exchange contribution to the 15N line width. Measurements of R1, R2, and 
15N{1H} NOE are used. The approach is free from any assumption about the 
values of the CSA or of the conformational exchange. Using this approach, the 
spectral densities, the values of 15N CSA, and the conformational exchange 
contribution to the 15N line width are directly determined from the 
relaxation data for human ubiquitin, collected at 360, 500, and 600 MHz. The 
spectral densities are analyzed in terms of the order parameter and the 
correlation time of local motion, using an axially symmetric overall 
rotational diffusion model. The residue-specific values of 15N CSA and the 
spectral densities obtained using this approach are in agreement with those 
derived previously [Fushman, Tjandra, and Cowburn. J. Am. Chem. Soc. 1998, 
120, 10947−10952] from CSA/dipolar cross-correlation analysis. Accurate 
determination of spectral densities and order parameters from 15N relaxation 
may be accomplished by analysis of multiple-field data without assumption of 
constant CSA or zero chemical exchange contributions. }
 }
 
 @Article{Gagne98,