News - Revision history

imported>Mickey at 13:15, 21 February 2011

2011-02-21T13:15:53Z

← Older revision		Revision as of 13:15, 21 February 2011
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			[[#2011\|2011]]
	[[#2010\|2010]]		[[#2010\|2010]]
	[[#2009\|2009]]		[[#2009\|2009]]
	[[#2008\|2008]]		[[#2008\|2008]]
	[[#2007\|2007]]		[[#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 ==		== 2010 ==

imported>Mickey: /* BMRZ Seminar by Prof. Beat H. Meier and Dr. Anja Böckmann */

2010-11-22T09:25:03Z

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

← Older revision		Revision as of 09:25, 22 November 2010
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	=== BMRZ Seminar by Prof. Beat H. Meier and Dr. Anja Böckmann ===		=== BMRZ Seminar by Prof. Beat H. Meier and Dr. Anja Böckmann ===
			[[image:Meier_Boekmann.jpg\|thumb\|200px]]
	25.11.2010		25.11.2010

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

imported>Mickey: /* 2010 */

2010-11-22T09:24:16Z

2010

← Older revision		Revision as of 09:24, 22 November 2010
Line 6:		Line 6:
	== 2010 ==		== 2010 ==

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

	25.11.2010		25.11.2010
Line 18:		Line 18:
	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.		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.


	~~=== BMRZ Seminar by Dr. Anja Böckmann ===~~

	~~25.11.2010~~

	~~in room N100 0.15~~

	'''Solid-state NMR structural studies of prions'''		'''Solid-state NMR structural studies of prions'''

imported>Mickey: /* 2010 */

2010-11-22T09:18:24Z

2010

← Older revision		Revision as of 09:18, 22 November 2010
Line 17:		Line 17:

	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.		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.


	=== BMRZ Seminar by Dr. Anja Böckmann ===		=== BMRZ Seminar by Dr. Anja Böckmann ===

imported>Mickey: /* 2010 */

2010-11-22T09:18:03Z

2010

← Older revision		Revision as of 09:18, 22 November 2010
Line 9:		Line 9:

	25.11.2010		25.11.2010

	from 15:00 in room N100 0.15		from 15:00 in room N100 0.15

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	25.11.2010		25.11.2010

			in room N100 0.15

	'''Solid-state NMR structural studies of prions'''		'''Solid-state NMR structural studies of prions'''

imported>Mickey: /* BMRZ Seminar by Prof. Beat H. Meier */

2010-11-22T09:12:47Z

BMRZ Seminar by Prof. Beat H. Meier

← Older revision		Revision as of 09:12, 22 November 2010
Line 9:		Line 9:

	25.11.2010		25.11.2010
	15:00~		from 15:00 in room N100 0.15

	'''Protein structures by solid-state NMR: Recent progress'''		'''Protein structures by solid-state NMR: Recent progress'''

Line 15:		Line 16:

	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.		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.


	=== BMRZ Seminar by Dr. Anja Böckmann ===		=== BMRZ Seminar by Dr. Anja Böckmann ===

imported>Mickey: /* 2010 */

2010-11-22T09:12:00Z

2010

← Older revision		Revision as of 09:12, 22 November 2010
Line 9:		Line 9:

	25.11.2010		25.11.2010
			15:00~
	'''Protein structures by solid-state NMR: Recent progress'''		'''Protein structures by solid-state NMR: Recent progress'''

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	=== BMRZ Seminar by Anja Böckmann ===		=== BMRZ Seminar by Dr. Anja Böckmann ===

	25.11.2010		25.11.2010

imported>Guentert at 07:01, 19 November 2010

2010-11-19T07:01:21Z

← Older revision		Revision as of 07:01, 19 November 2010
Line 14:		Line 14:
	''Prof. Beat H. Meier, Physical Chemistry, ETH Zürich''		''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.		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.
	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.

	=== BMRZ Seminar by Anja ~~Boeckmann~~ ===
			=== BMRZ Seminar by Anja Böckmann ===

	25.11.2010		25.11.2010
Line 25:		Line 23:
	'''Solid-state NMR structural studies of prions'''		'''Solid-state NMR structural studies of prions'''

	''Dr. Anja ~~Boeckmann~~, CNRS-UMR, Lyon, France''		''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.		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.

imported>Mickey: /* 2010 */

2010-11-18T11:20:11Z

2010

← Older revision		Revision as of 11:20, 18 November 2010
Line 14:		Line 14:
	''Prof. Beat H. Meier, Physical Chemistry, ETH Zürich''		''Prof. Beat H. Meier, Physical Chemistry, ETH Zürich''

	~~===== Abstract: =====~~
	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.		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.		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.
Line 28:		Line 27:
	''Dr. Anja Boeckmann, CNRS-UMR, Lyon, France''		''Dr. Anja Boeckmann, CNRS-UMR, Lyon, France''

	~~===== Abstract: =====~~
	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.		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.

imported>Mickey: /* 2010 */

2010-11-18T11:17:25Z

2010

← Older revision		Revision as of 11:17, 18 November 2010
Line 30:		Line 30:
	===== Abstract: =====		===== Abstract: =====
	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.		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) ===		=== e-NMR - Extend-NMR Workshops in Vilnius (Lithuania) ===