Related ArticlesNMR characterization of theinteraction of GroEL with amyloid ? as a model ligand.
FEBS Lett. 2013 Apr 18;
Authors: Yagi-Utsumi M, Kunihara T, Nakamura T, Uekusa Y, Makabe K, Kuwajima K, Kato K
Abstract
Here we report an NMR study on the substrate interaction modes of GroEL using amyloid?(A?) as a model ligand. We found that GroEL could suppress A?(1-40) amyloid formation by interacting with its two hydrophobic segments Leu17-Ala21 and Ala30-Val36, which involve key residues in fibril formation. The binding site of A?(1-40) wasmapped on a pair of ?-helices located in the GroEL apical domain. These resultsprovide insights intochaperonin recognition of amyloidogenic proteins of pathological interest. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: A?(1-40)andA?(1-40)bindbyfluorescence technology(View interaction) A?(1-40)andA?(1-40)bindbynuclear magnetic resonance(View interaction) GroELandA?(1-40)bindbynuclear magnetic resonance(View interaction).
PMID: 23603391 [PubMed - as supplied by publisher]
NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: insights on the role of methionine.
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Chem Commun (Camb). 2011 Jun 14;47(22):6407-9
Authors: Shoshan MS, Shalev DE, Adriaens W, Merkx M, Hackeng TM, Tshuva EY
Abstract
The first NMR structure of a Cu(I)-bound metallochaperone model with the conserved sequence MT/HCXXC revealed that at pH ~3.0 and ~6.8 Cu(I) binds through one Cys and the Met...
[NMR paper] Characterization of protein-ligand interactions by high-resolution solid-state NMR sp
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J Am Chem Soc. 2004 Nov 3;126(43):13948-53
Authors: Zech SG, Olejniczak E, Hajduk P, Mack J, McDermott AE
A novel approach for detection of ligand binding to a protein in solid samples is described. Hydrated precipitates of the anti-apoptotic protein Bcl-xL show well-resolved (13)C-(13)C 2D solid-state NMR spectra that allow...
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[NMR paper] NMR-based structural characterization of large protein-ligand interactions.
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J Biomol NMR. 2002 Feb;22(2):165-73
Authors: Pellecchia M, Meininger D, Dong Q, Chang E, Jack R, Sem DS
Genomic research on target identification and validation has created a great need for methods that rapidly provide detailed structural information on protein-ligand interactions. We developed a suite of NMR experiments as rapid and efficient tools to provide descriptive...
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[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.
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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...
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Structural Characterization of GNNQQNY Amyloid Fibrils by Magic Angle Spinning NMR
Structural Characterization of GNNQQNY Amyloid Fibrils by Magic Angle Spinning NMR
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi100077x/aop/images/medium/bi-2010-00077x_0004.gif
Biochemistry
DOI: 10.1021/bi100077x
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[NMR paper] NMR techniques for characterization of ligand binding: utility for lead generation an
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Biopolymers. 1999;51(3):221-43
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Over the last ten years, nmr spectroscopy has evolved into an important discipline in drug discovery....
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Structural Characterization of GNNQQNY Amyloid Fibrils by Magic Angle Spinning NMR.
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Structural Characterization of GNNQQNY Amyloid Fibrils by Magic Angle Spinning NMR.
Biochemistry. 2010 Aug 9;
Authors: van der Wel PC, Lewandowski JR, Griffin RG
Various human diseases feature the formation of amyloid aggregates, but experimental characterization of these amyloid fibrils and their oligomeric precursors has remained challenging. Experimental...
NMR characterization of theinteraction of GroEL with amyloid ? as a model ligand.
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