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Wolfram Gronwald and Hans Robert Kalbitzer answers a
few questions about this month's fast breaking paper in the field of
Engineering.
From
•>>October 2005
Field:
Engineering
Article Title: Automated structure determination of proteins by NMR spectroscopy
Authors: Gronwald,
W;Kalbitzer, HR
Journal: PROG NUCL MAGN RESON SPECTROS
Volume: 44
Page: 33-96
Year: APR 16 2004
* Univ Regensburg, Inst Biophys & Phys Biochem, D-93040 Regensburg, Germany.
* Univ Regensburg, Inst Biophys & Phys Biochem, D-93040 Regensburg, Germany.
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 Why
do you think your paper is highly cited?
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“We describe in this review the advantages and limitations of the various methods in quite some detail which should enable the reader to select the most appropriate software for a specific problem.”
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There is currently a large need for computational approaches
to speed up the protein NMR structure determination process in
solution. During the last few years a quite divergent set of
methods has been published in order to tackle various aspects of
this problem, including optimized strategies for spectra
recording, automated NMR data evaluation and image analysis,
structure calculation, structure validation, and database
deposition. We describe in this review the advantages and
limitations of the various methods in quite some detail which
should enable the reader to select the most appropriate software
for a specific problem. In addition, we present our own
approaches to this problem which, in part, have not been
previously published.
Does
it describe a new discovery or a new methodology that's useful to
others?
A set of methodologies is reviewed that hopefully will be
useful to most researchers involved in NMR protein structure
determination in solution. In addition we provide information on
how the various software packages can be obtained.
Could
you summarize the significance of your paper in layman's terms?
Proteins play a fundamental role in almost all biological
processes and, due to various genome projects such as the Human
Genome Project, an enormous amount of protein sequence
information has become available. However, to fully make use of
the available information, e.g., to have a detailed knowledge of
how the various molecules function or interact with each other,
three-dimensional structural information of the encoded proteins
is required. At the moment, this information is mainly obtained
from two sources, namely X-ray crystallography and solution NMR
spectroscopy. Both approaches are presently relatively slow when
compared to the speed with which new sequence information can be
obtained. In NMR spectroscopy the time-limiting step is the
manual interpretation of the vast amount of experimental data
required to solve a single structure. Therefore, computational
methods to speed up this process are in high demand. In this
contribution we review recent advances in this area and discuss
them together with our own developments.
How
did you become involved in this research?
W. G.: It was during my diploma thesis at the University
of Braunschweig that I became interested in three-dimensional
protein structures. At that point I was mainly involved in the
development of new approaches in molecular modeling. During my
Ph.D. thesis at the "Gesellschaft für Biotechnologische
Forschung" (also in Braunschweig) I switched to the
experimental structure determination of proteins in solution
using NMR spectroscopy. In the research that followed, the
combination of NMR spectroscopy and computational approaches led
to the development of new methods for automated protein
structure determination in solution, initially in the group of
Prof. Brian Sykes in Edmonton, Canada, and now together with
Prof. Hans Robert Kalbitzer at the University of Regensburg in
Germany.
H. R. K.: Since 1983 when I was at the "Max-Planck-Institut
für Medizinische Forschung" in Heidelberg, one of my main
research topics has been the automated evaluation of NMR data. In
cooperation with Dr. Klaus-Peter Neidig
(Bruker Karlruhe) we wrote
the program package AURELIA, which is now succeeded by AUREMOL,
which was created when I obtained a professorship at the
University of Regensburg and Wolfram Gronwald joined my group. A
critical review of the achievements obtained by others is always
mandatory when you plan new projects.
Dr. Wolfram Gronwald and Prof. Dr. Hans Robert Kalbitzer
Institute for Biophysics and Physical Biochemistry
University of Regensburg
Regensburg, Germany
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ESI Special Topics,
October 2005
Citing URL - http://www.esi-topics.com/fbp/2005/october05-Gronwald_Kalbitzer.html
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