Author: bugman
Date: Tue Jun 7 21:35:08 2011
New Revision: 12888
URL: http://svn.gna.org/viewcvs/relax?rev=12888&view=rev
Log:
Deleted my ancient Melbourne Uni email address from the MEDLINE info!
Modified:
1.3/info.py
Modified: 1.3/info.py
URL:
http://svn.gna.org/viewcvs/relax/1.3/info.py?rev=12888&r1=12887&r2=12888&view=diff
==============================================================================
--- 1.3/info.py (original)
+++ 1.3/info.py Tue Jun 7 21:35:08 2011
@@ -553,7 +553,7 @@
journal = "J. Biomol. NMR"
journal_full = "Journal of Biomolecular NMR"
abstract = "Investigation of protein dynamics on the ps-ns and
mus-ms timeframes provides detailed insight into the mechanisms of enzymes
and the binding properties of proteins. Nuclear magnetic resonance (NMR) is
an excellent tool for studying protein dynamics at atomic resolution.
Analysis of relaxation data using model-free analysis can be a tedious and
time consuming process, which requires good knowledge of scripting
procedures. The software relaxGUI was developed for fast and simple
model-free analysis and is fully integrated into the software package relax.
It is written in Python and uses wxPython to build the graphical user
interface (GUI) for maximum performance and multi-platform use. This software
allows the analysis of NMR relaxation data with ease and the generation of
publication quality graphs as well as color coded images of molecular
structures. The interface is designed for simple data analysis and
management. The software was tested and validated against the command line
version of relax."
- authoraddress = "Department of Biochemistry and Molecular Biology,
University of Melbourne, Melbourne, Victoria 3010, Australia.
ejdauv@xxxxxxxxxxxxxxxxxxxx"
+ authoraddress = "Department of Biochemistry and Molecular Biology,
University of Melbourne, Melbourne, Victoria 3010, Australia."
doi = "10.1007/s10858-011-9509-1"
pubmed_id = 21618018
status = "published"
@@ -606,7 +606,7 @@
number = "1"
pages = "25-39"
abstract = "Model-free analysis of NMR relaxation data, which is
widely used for the study of protein dynamics, consists of the separation of
the global rotational diffusion from internal motions relative to the
diffusion frame and the description of these internal motions by amplitude
and timescale. Five model-free models exist, each of which describes a
different type of motion. Model-free analysis requires the selection of the
model which best describes the dynamics of the NH bond. It will be
demonstrated that the model selection technique currently used has two
significant flaws, under-fitting, and not selecting a model when one ought to
be selected. Under-fitting breaks the principle of parsimony causing bias in
the final model-free results, visible as an overestimation of S2 and an
underestimation of taue and Rex. As a consequence the protein falsely appears
to be more rigid than it actually is. Model selection has been extensively
developed in other fields. The techniques known as Akaike's Information
Criteria (AIC), small sample size corrected AIC (AICc), Bayesian Information
Criteria (BIC), bootstrap methods, and cross-validation will be compared to
the currently used technique. To analyse the variety of techniques, synthetic
noisy data covering all model-free motions was created. The data consists of
two types of three-dimensional grid, the Rex grids covering single motions
with chemical exchange [S2,taue,Rex], and the Double Motion grids covering
two internal motions [S f 2,S s 2,tau s ]. The conclusion of the comparison
is that for accurate model-free results, AIC model selection is essential. As
the method neither under, nor over-fits, AIC is the best tool for applying
Occam's razor and has the additional benefits of simplifying and speeding up
model-free analysis."
- authoraddress = "Department of Biochemistry and Molecular Biology,
University of Melbourne, Melbourne, Victoria 3010, Australia.
ejdauv@xxxxxxxxxxxxxxxxxxxx"
+ authoraddress = "Department of Biochemistry and Molecular Biology,
University of Melbourne, Melbourne, Victoria 3010, Australia."
keywords = "Amines ; Diffusion ; *Models, Molecular ; Motion ;
Nuclear Magnetic Resonance, Biomolecular/*methods ; Proteins/*chemistry ;
Research Support, Non-U.S. Gov't ; Rotation"
doi = "10.1023/A:1021902006114"
pubmed_id = 12566997
r12888 - /1.3/info.py