The interaction among proteins is one of the most fundamental methods of information transfer in the living system. Many methods have been developed in order to identify the interaction pairs or groups either in vivo or in vitro. The in vitro pulldown/coprecipitation assay directly observes the protein that binds to the target. This method involves electrophoresis, which is a technique of a low resolution as well as a low throughput. As a better alternative, we wish to propose a new method that...
[NMR paper] AlphaFold 2 and NMR Spectroscopy: Partners to Understand Protein Structure, Dynamics and Function
AlphaFold 2 and NMR Spectroscopy: Partners to Understand Protein Structure, Dynamics and Function
The artificial intelligence program AlphaFold 2 is revolutionizing the field of protein structure determination as it accurately predicts the 3D structure of two thirds of the human proteome. Its predictions can be used directly as structural models or indirectly as aids for experimental structure determination using X-ray crystallography, CryoEM or NMR spectroscopy. Nevertheless, AlphaFold 2 can neither afford insight into how proteins fold, nor can it determine protein stability or...
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06-03-2022 07:40 PM
[NMR paper] NMR Spin Relaxation Theory of Biomolecules Undergoing Highly Asymmetric Exchange with Large Interaction Partners
NMR Spin Relaxation Theory of Biomolecules Undergoing Highly Asymmetric Exchange with Large Interaction Partners
The transient interactions of proteins and other molecules with much larger structures, such as synthetic or biological nanoparticles, lead to certain types of enhanced nuclear magnetic resonance (NMR) spin relaxation effects, which can be accurately measured by multidimensional solution NMR techniques. These relaxation effects provide new information about the nanostructures and the protein, their interactions, internal dynamics, and associated kinetic and thermodynamic...
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03-23-2021 07:56 PM
[ASAP] Comparative Analysis of the Conformation, Aggregation, Interaction, and Fibril Morphologies of Human a-, ß-, and ?-Synuclein Proteins
Comparative Analysis of the Conformation, Aggregation, Interaction, and Fibril Morphologies of Human a-, ß-, and ?-Synuclein Proteins
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00343/20180612/images/medium/bi-2018-00343q_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00343
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06-13-2018 05:09 PM
[NMR paper] Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.
Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.
Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.
Solid State Nucl Magn Reson. 2017 Oct 04;88:1-14
Authors: van der Wel PCA
Abstract
The aggregation of proteins and peptides into a variety of insoluble, and often non-native, aggregated states plays a central role in many devastating diseases. Analogous processes undermine the efficacy of polypeptide-based biological pharmaceuticals, but are also...
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10-17-2017 10:19 AM
Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy
Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy
Publication date: Available online 4 October 2017
Source:Solid State Nuclear Magnetic Resonance</br>
Author(s): Patrick C.A. van der Wel</br>
The aggregation of proteins and peptides into a variety of insoluble, and often non-native, aggregated states plays a central role in many devastating diseases. Analogous processes undermine the efficacy of polypeptide-based biological pharmaceuticals, but are also being leveraged in the design of biologically inspired self-assembling...
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10-05-2017 07:28 PM
[NMR paper] A Ligand-Based NMR Screening Approach for the Identification and Characterization of Inhibitors and Promoters of Amyloid Peptide Aggregation.
A Ligand-Based NMR Screening Approach for the Identification and Characterization of Inhibitors and Promoters of Amyloid Peptide Aggregation.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7315-19-Wiley_FullText_120x30_orange.png Related Articles A Ligand-Based NMR Screening Approach for the Identification and Characterization of Inhibitors and Promoters of Amyloid Peptide Aggregation.
ChemMedChem. 2017 Sep 07;12(17):1458-1463
Authors: Dalvit C, Santi S, Neier R
Abstract
Over the...
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09-24-2017 06:16 AM
[NMR paper] Site-specific identification of an a? fibril-heparin interaction site by using solid-state NMR spectroscopy.
Site-specific identification of an a? fibril-heparin interaction site by using solid-state 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 Site-specific identification of an a? fibril-heparin interaction site by using solid-state NMR spectroscopy.
Angew Chem Int Ed Engl. 2012 Dec 21;51(52):13140-3
Authors: Madine J, Pandya MJ, Hicks MR, Rodger A, Yates EA, Radford SE, Middleton DA
Abstract
At the...
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06-12-2013 11:42 AM
[NMR paper] Identification of the Archaeoglobus fulgidus endonuclease III DNA interaction surface
Identification of the Archaeoglobus fulgidus endonuclease III DNA interaction surface using heteronuclear NMR methods.
Related Articles Identification of the Archaeoglobus fulgidus endonuclease III DNA interaction surface using heteronuclear NMR methods.
Structure. 1999 Aug 15;7(8):919-30
Authors: Shekhtman A, McNaughton L, Cunningham RP, Baxter SM
BACKGROUND: Endonuclease III is the prototype for a family of DNA-repair enzymes that recognize and remove damaged and mismatched bases from DNA via cleavage of the N-glycosidic bond. Crystal...
Identification of interaction partners using protein aggregation and NMR spectroscopy
Linear Mode
