SEM1(68-107) is a peptide corresponding to the region of semenogelin 1 protein from 68 to 107 amino acid position. SEM1(68-107) is an abundant component of semen, which participates in HIV infection enhanced by amyloid fibrils forming. To understand the causes influencing amyloid fibril formation, it is necessary to determine the spatial structure of SEM1(68-107). It was shown that the determination of SEM1(68-107) structure is complicated by the non-informative NMR spectra due to the high...
[NMR paper] NMR Studies of the Ion Channel-Forming Human Amyloid-beta with Zinc Ion Concentrations
NMR Studies of the Ion Channel-Forming Human Amyloid-beta with Zinc Ion Concentrations
Alzheimer's disease (AD) is classified as an amyloid-related disease. Amyloid beta (A?) is a transmembrane protein known to play a major role in the pathogenesis of AD. These A? proteins can form ion channels or pores in the cell membrane. Studies have elucidated the structure of the transmembrane domain of A? ion channels. In addition, various studies have investigated substances that block or inhibit the formation of A? ion channels. Zinc ions are considered as potential inhibitors of AD. In...
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[NMR paper] Exploring interactions between lipids and amyloid-forming proteins: a review for applying fluorescence and NMR techniques
Exploring interactions between lipids and amyloid-forming proteins: a review for applying fluorescence and NMR techniques
A hallmark of Alzheimer's, Parkinson's, and other amyloid diseases is the assembly of amyloid proteins into amyloid aggregates or fibrils. In many cases, the formation and cytotoxicity of amyloid assemblies are associated with their interaction with cell membranes. Despite studied for many years, the characterization of the interaction is challenged for reasons on the multiple aggregation states of amyloid-forming proteins, transient and weak interactions in the complex...
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02-24-2021 05:50 AM
[NMR paper] Exploring interactions between lipids and amyloid-forming proteins: a review for applying fluorescence and NMR techniques.
Exploring interactions between lipids and amyloid-forming proteins: a review for applying fluorescence and NMR techniques.
Related Articles Exploring interactions between lipids and amyloid-forming proteins: a review for applying fluorescence and NMR techniques.
Chem Phys Lipids. 2021 Feb 15;:105062
Authors: Chang Z, Deng J, Zhao W, Yang J
Abstract
A hallmark of Alzheimer's, Parkinson's, and other amyloid diseases is the assembly of amyloid proteins into amyloid aggregates or fibrils. In many cases, the formation and cytotoxicity...
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02-20-2021 07:45 PM
[NMR paper] Conformational Stability Study of a Therapeutic Peptide Plectasin Using Molecular Dynamics Simulations in Combination with NMR.
Conformational Stability Study of a Therapeutic Peptide Plectasin Using Molecular Dynamics Simulations in Combination with NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Conformational Stability Study of a Therapeutic Peptide Plectasin Using Molecular Dynamics Simulations in Combination with NMR.
J Phys Chem B. 2019 06 13;123(23):4867-4877
Authors: Indrakumar S, Zalar M, Pohl C, Nørgaard A, Streicher W, Harris P, Golovanov AP, Peters GHJ
Abstract
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07-18-2020 10:53 AM
[NMR paper] High pressure NMR reveals conformational perturbations by disease-causing mutations in amyloid ?-peptide.
High pressure NMR reveals conformational perturbations by disease-causing mutations in amyloid ?-peptide.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles High pressure NMR reveals conformational perturbations by disease-causing mutations in amyloid ?-peptide.
Chem Commun (Camb). 2018 May 01;54(36):4609-4612
Authors: Rosenman DJ, Clemente N, Ali M, García AE, Wang C
Abstract
Here we present the high pressure NMR characterization of A?42 and two...
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[NMR paper] Distinct conformational states of the Alzheimer ?-amyloid peptide can be detected by high-pressure NMR spectroscopy.
Distinct conformational states of the Alzheimer ?-amyloid peptide can be detected by high-pressure NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Distinct conformational states of the Alzheimer ?-amyloid peptide can be detected by high-pressure NMR spectroscopy.
Angew Chem Int Ed Engl. 2013 Aug 19;52(34):8943-7
Authors: Munte CE, Beck Erlach M, Kremer W, Koehler J, Kalbitzer HR
PMID: 23843225
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[NMR paper] An Ensemble of Rapidly Interconverting Orientations in Electrostatic Protein-Peptide Complexes Characterized by NMR Spectroscopy.
An Ensemble of Rapidly Interconverting Orientations in Electrostatic Protein-Peptide Complexes Characterized by NMR Spectroscopy.
Related Articles An Ensemble of Rapidly Interconverting Orientations in Electrostatic Protein-Peptide Complexes Characterized by NMR Spectroscopy.
Chembiochem. 2014 Feb 6;
Authors: Guan JY, Foerster JM, Drijfhout JW, Timmer M, Blok A, Ullmann GM, Ubbink M
Abstract
Protein complex formation involves an encounter state in which the proteins are associated in a nonspecific manner and often stabilized by...
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NMR-Based Explicit Ensemble Dynamics Simulations of Membrane Protein
NMR-Based Explicit Ensemble Dynamics Simulations of Membrane Protein
Publication date: 28 January 2014
Source:Biophysical Journal, Volume 106, Issue 2, Supplement 1</br>
Author(s): Xi Cheng , Wonpil Im</br>
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Conformational ensemble of amyloid-forming semenogelin 1 peptide SEM1(68-107) by NMR spectroscopy and MD simulations
Linear Mode
