News

From GuentertWiki
(Difference between revisions)
Jump to: navigation, search
(Seminar by Prof. Koichi Kato (03.07.2008))
 
(89 intermediate revisions by 5 users not shown)
Line 1: Line 1:
 +
[[#2011|2011]]
 +
[[#2010|2010]]
 +
[[#2009|2009]]
 +
[[#2008|2008]]
 +
[[#2007|2007]]
 +
 +
== 2011 ==
 +
 +
=== BMRZ Seminar by Prof. Alexander Arseniev === 
 +
3.3.2011
 +
 +
from 15:00 in room H2
 +
 +
'''NMR study of membrane protein helix-helix interactions'''
 +
 +
''Prof. Alexander Arseniev, Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow''
 +
 +
 +
== 2010 ==
 +
 +
=== BMRZ Seminar by Prof. Beat H. Meier and Dr. Anja Böckmann === 
 +
[[image:Meier_Boekmann.jpg|thumb|200px]]
 +
25.11.2010
 +
 +
from 15:00 in room N100 0.15
 +
 +
'''Protein structures by solid-state NMR: Recent progress'''
 +
 +
''Prof. Beat H. Meier, Physical Chemistry, ETH Zürich''
 +
 +
Structure determination from solid-state NMR spectra is still a challenge. While a handful of proteins have indeed been solved at atomic resolution, structure determination of completely unknown proteins and of larger proteins (>150 residues) is still difficult and prone to error. The talk will describe some of the problems and pitfalls and sketch or describe some recipes that promise to advance the field in the future. These include better and more efficient pulse sequences, enhanced spectral resolution, four-dimensional spectroscopy, and improved computational processes to arrive at the correct structure form a set of given solid-state spectra. The principles will be illustrated using microcrystalline proteins as well as fibrils.
 +
 +
 +
'''Solid-state NMR structural studies of prions'''
 +
 +
''Dr. Anja Böckmann, CNRS-UMR, Lyon, France''
 +
 +
Prions are infectious, self-propagating polymers of otherwise soluble, host-encoded proteins. The structural basis of prion infectivity remains largely elusive today; this issue is a technical challenge as prion oligomers are heterogeneous high molecular weight particles that are neither suitable for protein crystallography nor classical NMR studies. Moreover, it has long been believed that misfolded proteins like prions and amyloids give poorly resolved NMR spectra. We show that the spectra of full-length prion fibrils from Ure2p and HET-s interestingly lead to very highly resolved solid-state NMR spectra, at least for parts of the proteins. Ure2p and HET-s are of similar architecture, with a compactly folded globular domain and an in solution flexible prion domain. Comparing the NMR spectra of the full-length protein fibrils reveals however surprising features and stresses the structural diversity underlying prion propagation suggesting that no unique mode exists for the assembly of these proteins into fibrils.
 +
 +
=== e-NMR - Extend-NMR Workshops in Vilnius (Lithuania) ===
 +
 +
04-08.10.2010
 +
 +
'''NMR structure calculation - GRID applications and integrated tools '''
 +
 +
For more information, please see the following webpage of the [http://www.enmr.eu/eNMR-news-events Workshop].
 +
 +
 +
=== BMRZ Seminar by Prof. Masatsune Kainosho ===
 +
 +
02.07.2010
 +
 +
'''Recent progress in SAIL-NMR methods for studying Protein Structure and Dynamics'''
 +
 +
''Prof. Masatsune Kainosho, Nagoya University and Tokyo Metropolitan University''
 +
 +
 +
=== e-NMR - Extend-NMR Workshops in Vilnius (Lithuania) ===
 +
 +
07-11.06.2010
 +
 +
'''NMR structure calculation - GRID applications and integrated tools '''
 +
 +
For more information, please see the following webpage of the [http://www.enmr.eu/eNMR-news-events Workshop].
 +
 +
 +
=== 4<sup>th</sup>BMRZ-CEF Workshop ===
 +
 +
16.04.2010
 +
 +
4<sup>th</sup>BMRZ-CEF Workshop will be held on 16 April 2010 in Forschungskolleg Humanwissenschaften in Bad Homburg. For details, see the [http://www.bmrz.uni-frankfurt.de/wiki/index.php/BMRZ_meeting_2010 Meeting website].
 +
 
== 2009 ==
 
== 2009 ==
  
===== Seminar by Dr. Hélène Van Melckebeke (16.01.2009) =====
+
=== BMRZ Seminar by Prof. Vladislav Orekhov ===
  
:'''High resolution structure of the HET-s(218-289) prion amyloid fibrils using solid-state NMR'''
+
10.12.2009, 16:00, Biocenter Lecture Hall B2
  
:''Dr. Hélène Van Melckebeke, Physical Chemistry, ETH Zürich, Switzerland''
+
'''Co-processing NMR spectra with multi-dimensional decomposition: 4D NOESYs of the human membrane protein VDAC-1 and other applications'''
  
:Prions and amyloid fibrils are associated with several animal and human diseases. Despite the paramount importance of the structural aspects, no atomic resolution structure of a prion in its fibrillar state has been reported yet. Solid-state NMR is to date the only technique capable of obtaining the structure of such non-crystalline and non-soluble compounds. We have obtained the structure of amyloid fibrils produced in vitro from the prion-forming domain (residues 218-289) of the HET-s prion from the filamentous fungus Podospora anserina using solid-state NMR techniques. These results give a structural explanation of the stability of the HET-s(218-289) fibrils. In the presentation, both methodological and structural aspects will be discussed.
+
''Prof. Vladislav Orekhov, Swedish NMR Centre, University of Gothenburg, Sweden''
  
:Wasmer, C. Lange, A., Van Melckebeke, H., Siemer, A. B., Riek, R. & Meier, B. H. (2008). Amyloid fibrils of the HET-s(218–289) prion form a β solenoid with a triangular hydrophobic core. Science 319, 1523–1526.
+
The analysis of typical sets of multidimensional NMR experiments for signal assignment, structure calculations, and metabolomic studies relies on matching of signal frequencies between several experiments. By simultaneous processing of the spectra, this intrinsic reoccurrence of signal frequencies and line-shapes is exploited to enhance the quality and efficiency of the data analysis. We use multi-dimensional decomposition (MDD) for co-processing of any combination of experiments and non-uniform sampling for optimizing spectra resolution and sensitivity. The approach has been successfully demonstrated for several essentially different situations: processing of 4D NOESY spectra for the de novo structure determination of the 31 kDa integral human membrane protein VDAC-1 in detergent micelles with an effective molecular weight of 70–90 kDa; rapid real-time data collection and automated backbone assignments of a 13 kDa naturally disordered cytoplasmic part of the zeta-chain of the T-cell receptor system; a metabolomic study on food-deprived fish.
 +
 
 +
* Hiller, S., Garces, R.G., Malia, T.J., Orekhov, V.Y., Colombini, M. & Wagner, G. Solution structure of the integral human membrane protein VDAC-1 in detergent micelles. [http://dx.doi.org/10.1126/science.1161302 Science 321, 1206-1210 (2008)]
 +
* Jaravine, V.A. and Orekhov, V.Y. Targeted acquisition for real-time NMR spectroscopy. [http://dx.doi.org/10.1021/ja062146p J. Am. Chem. Soc. 128, 13421-13426 (2006)]
 +
 
 +
 
 +
=== Job announcement  ===
 +
 
 +
22.6.2009
 +
 
 +
'''Ph.D. and postdoctoral positions in "Hyper-dimensional NMR spectroscopy for automated protein structure determination"
 +
 
 +
[[Ph.D. and postdoctoral positions in hyper-dimensional NMR| Read more...]]
 +
 
 +
 
 +
[[image:BMRZ-CEFPoster3small.jpg|thumb|100px]]
 +
=== BMRZ-CEF Workshop 2009 ===
 +
 
 +
04.05.2009
 +
 
 +
The BMRZ and the [http://www.cef-mc.de/ Cluster of Excellence Macromolecular Complexes] at the Goethe University Frankfurt (CEF) held a joint [http://www.bmrz.uni-frankfurt.de/wiki/index.php/BMRZ-CEF_Workshop_2009 BMRZ-CEF Workshop 2009] on '''Magnetic Resonance and Complementary Techniques for Macromolecular Systems''' in Kronberg on May 4, 2009. For details, see the [http://www.bmrz.uni-frankfurt.de/wiki/index.php/BMRZ-CEF_Workshop_2009 BMRZ-CEF Workshop 2009 Workshop webpage].
 +
 
 +
 
 +
=== BMRZ Seminar by Prof. Yuichiro Maéda ===
 +
 
 +
24.04.2009
 +
 
 +
'''Towards understanding the basic properties of F-actin based on high resolution structures'''
 +
 
 +
''Prof. Dr. Yuichiro Maéda, Structural Biology Research Center and Department of Biology, Nagoya University, Japan''
 +
 
 +
Actin plays various important cellular roles, among others, in muscle contraction, cell motility, neuron network formation, and cell division. In muscle, the actin filament plays the central roles in muscle contraction and its regulation. In non-muscle cells, actin is highly dynamic through transition between monomeric G-actin and filamentous F-actin. Movement is driven and force is exerted by “tread-milling”; simultaneous polymerization at the B-end and depolymerization at the P-end of F-actin. F-actin elongation is not controllable so that F-actin cannot be crystallized. Therefore a high- resolution structure of F-actin has never been known. Recently, we have made progress in the structural elucidation of F-actin. First, we have obtained a high-resolution structure of F-actin (Oda et al., 2009), which is based upon X-ray fiber diffractions obtained from highly oriented F-actin sols. Second, we have established a method for knowing cryo-EM structures at the ends of F-actin, and by employing this method, we have obtained the structure of a capping protein bound to the B-end of F-actin. Third, we have challenged a long-lasting problem and we have established a Sf9 based actin expression system to prepare actin variants. This enables us to know more details of how actin works. By combining these results, we are beginning to understand how actin works.
 +
 
 +
* Oda, T., Iwasa, M., Aihara, T., Maéda, Y., Narita, A. The nature of the globular- to fibrous-actin transition. Nature 457, 441-446 (2009).
 +
 
 +
 
 +
=== BMRZ CCPN Workshop ===
 +
 
 +
17-18.02.2009
 +
 
 +
A two day [http://www.ccpn.ac.uk/ccpn CCPN] (Collaborative Computing Project for NMR) workshop will take place February 17-18 (2009), right here at the BMRZ (rooms to be announced). It is free. The workshop will consist of a full Analysis workshop on day 1, and an integration workshop on day 2 (which would be more specialised, and/or possibly answering specific other questions that people might have (e.g. left over from day 1).For those of you who have not heard of this software, it is for assigning and analysing NMR spectra, and one of many nice features is that it can read many file list formats (Xeasy, pdb, NMRStar, Bruker, Cara, Sparky, nmrPipe...), making it easy to incorporate results obtained elsewhere into a project.The software has enjoyed a huge growth in the last years, and is very well supported. It is free to download, and runs on Windows, Linux and Apple PCs. There is an emailing list which is very lively, and the programmers even take suggestions to add to the software package. Furthermore, a nice [http://www.protein-nmr.org.uk/ web page] which goes through NMR experiments and assignments, by Vicky Higman, is oriented towards CCPN software.
 +
 
 +
 
 +
[[image:InCellStructure.jpg|thumb|130px]]
 +
=== "Proteinstruktur in der lebenden Zelle bestimmt - NMR-Experimente erstmals in natürlicher Umgebung möglich" ===
 +
 
 +
05.03.2009
 +
 
 +
[http://www.muk.uni-frankfurt.de/pm/pm2009/0309/041/ Pressemitteilung] by the [http://www.uni-frankfurt.de/ Goethe University Frankfurt am Main].
 +
 
 +
* Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. & Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy. [http://dx.doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]
 +
 
 +
 
 +
=== "Proteine bei der Arbeit beobachten" ===
 +
 
 +
05.03.2009
 +
 
 +
[http://www.volkswagenstiftung.de/service/aktuelles/archiv/period/1240329274///article/145/proteine-bei.html Pressemitteilung] by the [http://www.volkswagenstiftung.de/ Volkswagen Foundation].
 +
 
 +
* Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. & Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy. [http://dx.doi.org/10.1038/nature07814 Nature 458, 102-105 (2009)]
 +
 
 +
 
 +
=== BMRZ Seminar by Dr. Hélène Van Melckebeke ===
 +
 
 +
16.01.2009
 +
 
 +
'''High resolution structure of the HET-s(218-289) prion amyloid fibrils using solid-state NMR'''
 +
 
 +
''Dr. Hélène Van Melckebeke, ETH Zürich''
 +
 
 +
Prions and amyloid fibrils are associated with several animal and human diseases. Despite the paramount importance of the structural aspects, no atomic resolution structure of a prion in its fibrillar state has been reported yet. Solid-state NMR is to date the only technique capable of obtaining the structure of such non-crystalline and non-soluble compounds. We have obtained the structure of amyloid fibrils produced in vitro from the prion-forming domain (residues 218-289) of the HET-s prion from the filamentous fungus Podospora anserina using solid-state NMR techniques. These results give a structural explanation of the stability of the HET-s(218-289) fibrils. In the presentation, both methodological and structural aspects will be discussed.
 +
 
 +
* Wasmer, C. Lange, A., Van Melckebeke, H., Siemer, A. B., Riek, R. & Meier, B. H. (2008). Amyloid fibrils of the HET-s(218–289) prion form a β solenoid with a triangular hydrophobic core. Science 319, 1523–1526.
  
 
== 2008 ==
 
== 2008 ==
  
===== Seminar by Prof. Masatsune Kainosho (14.10.2008) =====
+
=== BMRZ Seminar by Prof. Masatsune Kainosho ===
  
:'''Recent progress in the SAIL approach to study side-chain conformations of proteins and protein complexes'''
+
14.10.2008
  
:''Prof. Dr. Masatsune Kainosho, Nagoya University and Tokyo Metropolitan University, Japan
+
'''Recent progress in the SAIL approach to study side-chain conformations of proteins and protein complexes'''
  
===== Seminar by Dr. Hideo Iwai (15.09.2008) =====
+
''Prof. Dr. Masatsune Kainosho, Nagoya University and Tokyo Metropolitan University, Japan''
  
:'''Segmental and fractional isotopic labelling of proteins'''
 
  
:''Dr. Hideo Iwai, University of Helsinki, Finland''
+
=== BMRZ Seminar by Dr. Hideo Iwai ===
  
:Dr. Iwai will present two new approaches of segmental isotopic labelling and fractional 13C labelling for NMR assignments of proteins. Recently, he has developed a robust approach for segmental isotopic labelling using protein trans-splicing, which could open possibilities to study a domain of intact proteins without dissecting into smaller globular domains. He will also present a novel concept to classify residue types in NMR spectra by the use of fractional labeling, which is distinct from routinely used chemical shifts and spin topologies for identifying residue types.
+
15.09.2008
  
:Dr. Hideo Iwai graduated from the Graduate School of Pharmaceutical Sciences of the University of Tokyo with Prof. Yoji Arata, and received his Ph.D. in 1998 at ETH Zürich, Switzerland, with Prof. Kurt Wüthrich. He then worked as a postdoctoral researcher at ETH Zürich, at the University of Zürich with Prof. Andreas Plückthun, and at RIKEN Genomic Sciences Center in Yokohama, Japan. In 2003 he became Assistant Professor of Chemistry at the University of Saskatchewan in Saskatoon, Canada. Since 2005 he is an Academy Research Fellow at the Institute of Biotechnology of the University of Helsinki in Finland.
+
'''Segmental and fractional isotopic labelling of proteins'''
  
===== Seminar by Prof. Koichi Kato (03.07.2008) =====
+
''Dr. Hideo Iwai, University of Helsinki, Finland''
 +
 
 +
Dr. Iwai will present two new approaches of segmental isotopic labelling and fractional <sup>13</sup>C labelling for NMR assignments of proteins. Recently, he has developed a robust approach for segmental isotopic labelling using protein trans-splicing, which could open possibilities to study a domain of intact proteins without dissecting into smaller globular domains. He will also present a novel concept to classify residue types in NMR spectra by the use of fractional labeling, which is distinct from routinely used chemical shifts and spin topologies for identifying residue types.
 +
 
 +
 
 +
[[image:Pannenhelfer.jpg|thumb|200px]]
 +
=== "Pannenhilfe der Antibiotikumproduktion entschlüsselt" ===
 +
 
 +
11.08.2008
 +
 
 +
[http://www.volkswagenstiftung.de/service/aktuelles/archiv/period/1233149134///article/145/pannenhilfe.html Pressemitteilung] by the [http://www.volkswagenstiftung.de/ Volkswagen Foundation].
 +
 
 +
[http://www.muk.uni-frankfurt.de/pm/pm2008/0808/148/ Pressemitteilung] by the [http://www.uni-frankfurt.de/ Goethe University Frankfurt am Main].
 +
 
 +
* Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. & Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase. [http://dx.doi.org/10.1038/nature07161 Nature 454, 907–911 (2008)]
 +
 
 +
 
 +
=== BMRZ Seminar by Prof. Koichi Kato ===
 +
 
 +
03.07.2008
  
 
'''NMR and sugar library approaches for structural glycomics'''
 
'''NMR and sugar library approaches for structural glycomics'''
  
:''Prof. Dr. Koichi Kato, Nagoya City University, Nagoya, and Institute of Molecular Science, Okazaki, Japan''
+
''Prof. Dr. Koichi Kato, Nagoya City University, Nagoya, and Institute of Molecular Science, Okazaki, Japan''
 +
 
 +
Many proteins in the living systems are covalently linked to carbohydrate moieties. NMR spectroscopy can potentially provide information on the structure and dynamics of glycoproteins in solution but has also been hampered by spectral overlap and low sensitivity. To cope with this difficulty, we have been developing a systematic method for structural glycobiology by combined use of stable-isotope-assisted NMR spectroscopy and multi-dimensional HPLC techniques for glycosylation profiling and sugar library construction. Our projects address the underlying mechanisms of
 +
* Glycoform-dependent effector functions of immunoglobulin G glycoproteins as therapeutic antibodies
 +
* Glycoprotein-fate determination in cells through the interactions with a variety of intracellular lectins
 +
 
 +
 
 +
== 2007 ==
 +
 
 +
[[image:NewNMRinStructuralBiology2007Poster.jpg|thumb|150px]]
 +
=== Symposium on New NMR in Structural Biology 2007 ===
 +
 
 +
16-17.11.2007
  
:Many proteins in the living systems are covalently linked to carbohydrate moieties. NMR spectroscopy can potentially provide information on the structure and dynamics of glycoproteins in solution but has also been hampered by spectral overlap and low sensitivity. To cope with this difficulty, we have been developing a systematic method for structural glycobiology by combined use of stable-isotope-assisted NMR spectroscopy and multi-dimensional HPLC techniques for glycosylation profiling and sugar library construction. Our projects address the underlying mechanisms of
+
For details, please see the [http://www.uni-frankfurt.de/fb/fb14/BiochemieH/BPC/AK_Guentert/SymposiumNov2007/index.html conference web site].
:* Glycoform-dependent effector functions of immunoglobulin G
+
glycoproteins as therapeutic antibodies
+
:* Glycoprotein-fate determination in cells through the interactions with a
+
variety of intracellular lectins
+

Latest revision as of 14:15, 21 February 2011

2011 2010 2009 2008 2007

Contents

2011

BMRZ Seminar by Prof. Alexander Arseniev

3.3.2011

from 15:00 in room H2

NMR study of membrane protein helix-helix interactions

Prof. Alexander Arseniev, Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow


2010

BMRZ Seminar by Prof. Beat H. Meier and Dr. Anja Böckmann

Meier Boekmann.jpg

25.11.2010

from 15:00 in room N100 0.15

Protein structures by solid-state NMR: Recent progress

Prof. Beat H. Meier, Physical Chemistry, ETH Zürich

Structure determination from solid-state NMR spectra is still a challenge. While a handful of proteins have indeed been solved at atomic resolution, structure determination of completely unknown proteins and of larger proteins (>150 residues) is still difficult and prone to error. The talk will describe some of the problems and pitfalls and sketch or describe some recipes that promise to advance the field in the future. These include better and more efficient pulse sequences, enhanced spectral resolution, four-dimensional spectroscopy, and improved computational processes to arrive at the correct structure form a set of given solid-state spectra. The principles will be illustrated using microcrystalline proteins as well as fibrils.


Solid-state NMR structural studies of prions

Dr. Anja Böckmann, CNRS-UMR, Lyon, France

Prions are infectious, self-propagating polymers of otherwise soluble, host-encoded proteins. The structural basis of prion infectivity remains largely elusive today; this issue is a technical challenge as prion oligomers are heterogeneous high molecular weight particles that are neither suitable for protein crystallography nor classical NMR studies. Moreover, it has long been believed that misfolded proteins like prions and amyloids give poorly resolved NMR spectra. We show that the spectra of full-length prion fibrils from Ure2p and HET-s interestingly lead to very highly resolved solid-state NMR spectra, at least for parts of the proteins. Ure2p and HET-s are of similar architecture, with a compactly folded globular domain and an in solution flexible prion domain. Comparing the NMR spectra of the full-length protein fibrils reveals however surprising features and stresses the structural diversity underlying prion propagation suggesting that no unique mode exists for the assembly of these proteins into fibrils.

e-NMR - Extend-NMR Workshops in Vilnius (Lithuania)

04-08.10.2010

NMR structure calculation - GRID applications and integrated tools

For more information, please see the following webpage of the Workshop.


BMRZ Seminar by Prof. Masatsune Kainosho

02.07.2010

Recent progress in SAIL-NMR methods for studying Protein Structure and Dynamics

Prof. Masatsune Kainosho, Nagoya University and Tokyo Metropolitan University


e-NMR - Extend-NMR Workshops in Vilnius (Lithuania)

07-11.06.2010

NMR structure calculation - GRID applications and integrated tools

For more information, please see the following webpage of the Workshop.


4thBMRZ-CEF Workshop

16.04.2010

4thBMRZ-CEF Workshop will be held on 16 April 2010 in Forschungskolleg Humanwissenschaften in Bad Homburg. For details, see the Meeting website.

2009

BMRZ Seminar by Prof. Vladislav Orekhov

10.12.2009, 16:00, Biocenter Lecture Hall B2

Co-processing NMR spectra with multi-dimensional decomposition: 4D NOESYs of the human membrane protein VDAC-1 and other applications

Prof. Vladislav Orekhov, Swedish NMR Centre, University of Gothenburg, Sweden

The analysis of typical sets of multidimensional NMR experiments for signal assignment, structure calculations, and metabolomic studies relies on matching of signal frequencies between several experiments. By simultaneous processing of the spectra, this intrinsic reoccurrence of signal frequencies and line-shapes is exploited to enhance the quality and efficiency of the data analysis. We use multi-dimensional decomposition (MDD) for co-processing of any combination of experiments and non-uniform sampling for optimizing spectra resolution and sensitivity. The approach has been successfully demonstrated for several essentially different situations: processing of 4D NOESY spectra for the de novo structure determination of the 31 kDa integral human membrane protein VDAC-1 in detergent micelles with an effective molecular weight of 70–90 kDa; rapid real-time data collection and automated backbone assignments of a 13 kDa naturally disordered cytoplasmic part of the zeta-chain of the T-cell receptor system; a metabolomic study on food-deprived fish.


Job announcement

22.6.2009

Ph.D. and postdoctoral positions in "Hyper-dimensional NMR spectroscopy for automated protein structure determination"

Read more...


BMRZ-CEFPoster3small.jpg

BMRZ-CEF Workshop 2009

04.05.2009

The BMRZ and the Cluster of Excellence Macromolecular Complexes at the Goethe University Frankfurt (CEF) held a joint BMRZ-CEF Workshop 2009 on Magnetic Resonance and Complementary Techniques for Macromolecular Systems in Kronberg on May 4, 2009. For details, see the BMRZ-CEF Workshop 2009 Workshop webpage.


BMRZ Seminar by Prof. Yuichiro Maéda

24.04.2009

Towards understanding the basic properties of F-actin based on high resolution structures

Prof. Dr. Yuichiro Maéda, Structural Biology Research Center and Department of Biology, Nagoya University, Japan

Actin plays various important cellular roles, among others, in muscle contraction, cell motility, neuron network formation, and cell division. In muscle, the actin filament plays the central roles in muscle contraction and its regulation. In non-muscle cells, actin is highly dynamic through transition between monomeric G-actin and filamentous F-actin. Movement is driven and force is exerted by “tread-milling”; simultaneous polymerization at the B-end and depolymerization at the P-end of F-actin. F-actin elongation is not controllable so that F-actin cannot be crystallized. Therefore a high- resolution structure of F-actin has never been known. Recently, we have made progress in the structural elucidation of F-actin. First, we have obtained a high-resolution structure of F-actin (Oda et al., 2009), which is based upon X-ray fiber diffractions obtained from highly oriented F-actin sols. Second, we have established a method for knowing cryo-EM structures at the ends of F-actin, and by employing this method, we have obtained the structure of a capping protein bound to the B-end of F-actin. Third, we have challenged a long-lasting problem and we have established a Sf9 based actin expression system to prepare actin variants. This enables us to know more details of how actin works. By combining these results, we are beginning to understand how actin works.

  • Oda, T., Iwasa, M., Aihara, T., Maéda, Y., Narita, A. The nature of the globular- to fibrous-actin transition. Nature 457, 441-446 (2009).


BMRZ CCPN Workshop

17-18.02.2009

A two day CCPN (Collaborative Computing Project for NMR) workshop will take place February 17-18 (2009), right here at the BMRZ (rooms to be announced). It is free. The workshop will consist of a full Analysis workshop on day 1, and an integration workshop on day 2 (which would be more specialised, and/or possibly answering specific other questions that people might have (e.g. left over from day 1).For those of you who have not heard of this software, it is for assigning and analysing NMR spectra, and one of many nice features is that it can read many file list formats (Xeasy, pdb, NMRStar, Bruker, Cara, Sparky, nmrPipe...), making it easy to incorporate results obtained elsewhere into a project.The software has enjoyed a huge growth in the last years, and is very well supported. It is free to download, and runs on Windows, Linux and Apple PCs. There is an emailing list which is very lively, and the programmers even take suggestions to add to the software package. Furthermore, a nice web page which goes through NMR experiments and assignments, by Vicky Higman, is oriented towards CCPN software.


InCellStructure.jpg

"Proteinstruktur in der lebenden Zelle bestimmt - NMR-Experimente erstmals in natürlicher Umgebung möglich"

05.03.2009

Pressemitteilung by the Goethe University Frankfurt am Main.

  • Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. & Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy. Nature 458, 102-105 (2009)


"Proteine bei der Arbeit beobachten"

05.03.2009

Pressemitteilung by the Volkswagen Foundation.

  • Sakakibara, D., Sasaki, A., Ikeya, T., Hamatsu, J., Hanashima, T., Mishima, M., Yoshimasu, M., Hayashi, N., Mikawa, T., Wälchli, M., Smith, B. O., Shirakawa, M., Güntert, P. & Ito, Y. Protein structure determination in living cells by in-cell NMR spectroscopy. Nature 458, 102-105 (2009)


BMRZ Seminar by Dr. Hélène Van Melckebeke

16.01.2009

High resolution structure of the HET-s(218-289) prion amyloid fibrils using solid-state NMR

Dr. Hélène Van Melckebeke, ETH Zürich

Prions and amyloid fibrils are associated with several animal and human diseases. Despite the paramount importance of the structural aspects, no atomic resolution structure of a prion in its fibrillar state has been reported yet. Solid-state NMR is to date the only technique capable of obtaining the structure of such non-crystalline and non-soluble compounds. We have obtained the structure of amyloid fibrils produced in vitro from the prion-forming domain (residues 218-289) of the HET-s prion from the filamentous fungus Podospora anserina using solid-state NMR techniques. These results give a structural explanation of the stability of the HET-s(218-289) fibrils. In the presentation, both methodological and structural aspects will be discussed.

  • Wasmer, C. Lange, A., Van Melckebeke, H., Siemer, A. B., Riek, R. & Meier, B. H. (2008). Amyloid fibrils of the HET-s(218–289) prion form a β solenoid with a triangular hydrophobic core. Science 319, 1523–1526.

2008

BMRZ Seminar by Prof. Masatsune Kainosho

14.10.2008

Recent progress in the SAIL approach to study side-chain conformations of proteins and protein complexes

Prof. Dr. Masatsune Kainosho, Nagoya University and Tokyo Metropolitan University, Japan


BMRZ Seminar by Dr. Hideo Iwai

15.09.2008

Segmental and fractional isotopic labelling of proteins

Dr. Hideo Iwai, University of Helsinki, Finland

Dr. Iwai will present two new approaches of segmental isotopic labelling and fractional 13C labelling for NMR assignments of proteins. Recently, he has developed a robust approach for segmental isotopic labelling using protein trans-splicing, which could open possibilities to study a domain of intact proteins without dissecting into smaller globular domains. He will also present a novel concept to classify residue types in NMR spectra by the use of fractional labeling, which is distinct from routinely used chemical shifts and spin topologies for identifying residue types.


Pannenhelfer.jpg

"Pannenhilfe der Antibiotikumproduktion entschlüsselt"

11.08.2008

Pressemitteilung by the Volkswagen Foundation.

Pressemitteilung by the Goethe University Frankfurt am Main.

  • Koglin, A., Löhr, F., Bernhard, F., Rogov, V. R., Frueh, D. P., Strieter, E. R., Mofid, M. R., Güntert, P., Wagner, G., Walsh, C. T., Marahiel, M. A. & Dötsch, V. Structural basis for the selectivity of the external thioesterase of the surfactin-synthetase. Nature 454, 907–911 (2008)


BMRZ Seminar by Prof. Koichi Kato

03.07.2008

NMR and sugar library approaches for structural glycomics

Prof. Dr. Koichi Kato, Nagoya City University, Nagoya, and Institute of Molecular Science, Okazaki, Japan

Many proteins in the living systems are covalently linked to carbohydrate moieties. NMR spectroscopy can potentially provide information on the structure and dynamics of glycoproteins in solution but has also been hampered by spectral overlap and low sensitivity. To cope with this difficulty, we have been developing a systematic method for structural glycobiology by combined use of stable-isotope-assisted NMR spectroscopy and multi-dimensional HPLC techniques for glycosylation profiling and sugar library construction. Our projects address the underlying mechanisms of

  • Glycoform-dependent effector functions of immunoglobulin G glycoproteins as therapeutic antibodies
  • Glycoprotein-fate determination in cells through the interactions with a variety of intracellular lectins


2007

NewNMRinStructuralBiology2007Poster.jpg

Symposium on New NMR in Structural Biology 2007

16-17.11.2007

For details, please see the conference web site.

Personal tools
Intranet
Create Account