Solid-state NMR spectroscopic investigation of A? protofibrils: implication of a ?-sheet remodeling upon maturation into terminal amyloid fibrils.

		BioNMR > Educational resources > Journal club
Solid-state NMR spectroscopic investigation of A? protofibrils: implication of a ?-sheet remodeling upon maturation into terminal amyloid fibrils.

Webservers

NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

Thread Tools

Search this Thread

Rate Thread

Display Modes

07-02-2011, 04:03 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,777

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

Solid-state NMR spectroscopic investigation of A? protofibrils: implication of a ?-sheet remodeling upon maturation into terminal amyloid fibrils.

Solid-state NMR spectroscopic investigation of A? protofibrils: implication of a ?-sheet remodeling upon maturation into terminal amyloid fibrils.

Solid-state NMR spectroscopic investigation of A? protofibrils: implication of a ?-sheet remodeling upon maturation into terminal amyloid fibrils.

Angew Chem Int Ed Engl. 2011 Mar 14;50(12):2837-40

Authors: Scheidt HA, Morgado I, Rothemund S, Huster D, Fändrich M

PMID: 21387500 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid ?-protein fibrils. Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid ?-protein fibrils. Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid ?-protein fibrils. Bioorg Med Chem. 2011 Aug 27; Authors: Masuda Y, Fukuchi M, Yatagawa T, Tada M, Takeda K, Irie K, Akagi KI, Monobe Y, Imazawa T, Takegoshi K Abstract Aggregation of 42-residue amyloid ?-protein (A?42) plays a pivotal role in the etiology of Alzheimer's disease (AD). Curcumin, the yellow pigment in the rhizome of turmeric, attracts...	nmrlearner	Journal club	0	09-20-2011 03:10 PM
Intermolecular Alignment in Y145Stop Human Prion Protein Amyloid Fibrils Probed by Solid-State NMR Spectroscopy Intermolecular Alignment in Y145Stop Human Prion Protein Amyloid Fibrils Probed by Solid-State NMR Spectroscopy Jonathan J. Helmus, Krystyna Surewicz, Marcin I. Apostol, Witold K. Surewicz and Christopher P. Jaroniec http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja206469q/aop/images/medium/ja-2011-06469q_0003.gif Journal of the American Chemical Society DOI: 10.1021/ja206469q http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/e9F1wuu5168	nmrlearner	Journal club	0	08-16-2011 03:17 AM
Intermolecular Alignment in Y145Stop Human Prion Protein Amyloid Fibrils Probed by Solid-State NMR Spectroscopy. Intermolecular Alignment in Y145Stop Human Prion Protein Amyloid Fibrils Probed by Solid-State NMR Spectroscopy. Intermolecular Alignment in Y145Stop Human Prion Protein Amyloid Fibrils Probed by Solid-State NMR Spectroscopy. J Am Chem Soc. 2011 Aug 10; Authors: Helmus JJ, Surewicz K, Apostol MI, Surewicz WK, Jaroniec CP The Y145Stop mutant of human prion protein, huPrP23-144, has been linked to PrP cerebral amyloid angiopathy, an inherited amyloid disease, and also serves as a valuable in vitro model for investigating the molecular basis of...	nmrlearner	Journal club	0	08-11-2011 12:32 PM
Molecular-Level Examination of Cu2+ Binding Structure for Amyloid Fibrils of 40-Residue Alzheimer’s ? by Solid-State NMR Spectroscopy Molecular-Level Examination of Cu2+ Binding Structure for Amyloid Fibrils of 40-Residue Alzheimer’s ? by Solid-State NMR Spectroscopy Sudhakar Parthasarathy, Fei Long, Yifat Miller, Yiling Xiao, Dan McElheny, Kent Thurber, Buyong Ma, Ruth Nussinov and Yoshitaka Ishii http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1072178/aop/images/medium/ja-2010-072178_0006.gif Journal of the American Chemical Society DOI: 10.1021/ja1072178 http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA ...	nmrlearner	Journal club	0	02-22-2011 11:06 PM
Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy. Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy. Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy. J Am Chem Soc. 2010 Oct 6;132(39):13765-75 Authors: Van Melckebeke H, Wasmer C, Lange A, Ab E, Loquet A, Böckmann A, Meier BH We present a strategy to solve the high-resolution structure of amyloid fibrils by solid-state NMR and use it to determine the atomic-resolution structure of the prion domain of the fungal prion HET-s...	nmrlearner	Journal club	0	01-21-2011 12:00 PM
Probing water-accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR. Probing water-accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR. Probing water-accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR. J Mol Biol. 2010 Nov 18; Authors: Van Melckebeke H, Schanda P, Gath J, Wasmer C, Verel R, Lange A, Meier BH, Böckmann A Despite its importance in the context of conformational diseases, structural information is still sparse for protein fibrils. Hydrogen/deuterium exchange measurements of backbone amides allow to identify hydrogen-bonding patterns and reveal pertinent information about...	nmrlearner	Journal club	0	11-26-2010 05:32 PM
[NMR paper] A 2H solid-state NMR spectroscopic investigation of biomimetic bicelles containing ch A 2H solid-state NMR spectroscopic investigation of biomimetic bicelles containing cholesterol and polyunsaturated phosphatidylcholine. Related Articles A 2H solid-state NMR spectroscopic investigation of biomimetic bicelles containing cholesterol and polyunsaturated phosphatidylcholine. Chem Phys Lipids. 2004 Nov;132(1):55-64 Authors: Minto RE, Adhikari PR, Lorigan GA Deuterium solid-state NMR spectroscopy was used to qualitatively study the effects of both 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphatidylcholine (PLiPC) and cholesterol on...	nmrlearner	Journal club	0	11-24-2010 10:03 PM
[NMR paper] An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed by cold shock protein A. Related Articles An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed by cold shock protein A. Pac Symp Biocomput. 2001;:67-78 Authors: Alexandrescu AT Acid-denatured cold shock protein A (CspA) self-assembles into polymers with properties typical of amyloid fibrils. In the present work, a quenched hydrogen exchange experiment was used to probe the interactions of CspA fibrils with solvent. Exchange...	nmrlearner	Journal club	0	11-19-2010 08:32 PM

« Previous Thread | Next Thread »

Posting Rules
You may not post new threads You may not post replies You may not post attachments You may not edit your posts BB code is On Smilies are On [IMG] code is On HTML code is On Trackbacks are Off Pingbacks are Off Refbacks are Off