Solvent dynamics strongly induce the fibrillation of an amyloidogenic system. Probing the solvation mechanism is crucial as it enables us to predict different proteins' functionalities, such as the aggregation propensity, structural flexibility, and toxicity. This work shows that a straightforward NMR method in conjunction with phenomenological models gives a global and qualitative picture of water dynamics at different concentrations and temperatures. Here, we study amyloid system A?40 and its...
[NMR paper] Monitoring protein ubiquitination and SUMOylation in real-time by NMR.
Monitoring protein ubiquitination and SUMOylation in real-time by NMR.
Monitoring protein ubiquitination and SUMOylation in real-time by NMR.
Chem Commun (Camb). 2020 May 19;:
Authors: Habibullah BI, Tripathi V, Surana P, Das R
Abstract
The covalent conjugation of ubiquitin (Ub), known as ubiquitination, is a multi-step reaction involving multiple enzymes. We report a real-time, tag-free method to monitor protein ubiquitination by NMR spectroscopy under physiological conditions. The approach is also applicable for monitoring...
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05-20-2020 05:17 PM
Real-time monitoring of enzyme-assisted animal protein hydrolysis by NMR spectroscopy – An NMR reactomics concept
Real-time monitoring of enzyme-assisted animal protein hydrolysis by NMR spectroscopy – An NMR reactomics concept
Publication date: Available online 23 April 2018
Source:LWT</br>
Author(s): Ulrik K. Sundekilde, Lise Jarno, Nina Eggers, Hanne Christine Bertram</br>
This study presents an application of proton (1H) NMR spectroscopy for monitoring of enzyme-assisted hydrolysis of muscle protein under both at-line and real-time conditions. Measurements were carried out on sample material >1 g, and two different enzymes (alcalase and papain) were examined. The...
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04-23-2018 05:00 PM
[NMR paper] Water Proton NMR-A Tool for Protein Aggregation Characterization.
Water Proton NMR-A Tool for Protein Aggregation Characterization.
Related Articles Water Proton NMR-A Tool for Protein Aggregation Characterization.
Anal Chem. 2017 Apr 25;:
Authors: Taraban MB, DePaz RA, Lobo B, Yu YB
Abstract
Formulation stability is a critical attribute of any protein-based biopharmaceutical drug due to a protein's inherent tendency to aggregate. Advanced analytical techniques currently used for characterization of protein aggregates are prone to a number of limitations, and usually require additional...
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04-26-2017 02:16 PM
ProbingConformational Exchange Dynamics in a Short-LivedProtein Folding Intermediate by Real-Time Relaxation–DispersionNMR
ProbingConformational Exchange Dynamics in a Short-LivedProtein Folding Intermediate by Real-Time Relaxation–DispersionNMR
Re?mi Franco, Sergio Gil-Caballero, Isabel Ayala, Adrien Favier and Bernhard Brutscher
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.6b12089/20170111/images/medium/ja-2016-12089u_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.6b12089
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/pEuEi5v6HRE
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01-12-2017 03:48 AM
[NMR paper] Probing Conformational Exchange Dynamics in a Short-Lived Protein Folding Intermediate by Real-Time Relaxation-Dispersion NMR.
Probing Conformational Exchange Dynamics in a Short-Lived Protein Folding Intermediate by Real-Time Relaxation-Dispersion NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Probing Conformational Exchange Dynamics in a Short-Lived Protein Folding Intermediate by Real-Time Relaxation-Dispersion NMR.
J Am Chem Soc. 2017 Jan 11;:
Authors: Franco R, Gil-Caballero S, Ayala I, Favier A, Brutscher B
Abstract
NMR spectroscopy is a powerful tool for studying...
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01-12-2017 03:48 AM
[NMR paper] Real-time NMR monitoring of protein-folding kinetics by a recycle flow system for temperature jump.
Real-time NMR monitoring of protein-folding kinetics by a recycle flow system for temperature jump.
Real-time NMR monitoring of protein-folding kinetics by a recycle flow system for temperature jump.
Anal Chem. 2013 Sep 12;
Authors: Yamasaki K, Obara Y, Hasegawa M, Tanaka H, Yamasaki T, Wakuda T, Okada M, Kohzuma T
Abstract
An NMR method was developed that allows for real-time monitoring of reactions (on the order of seconds) induced by temperature jump. In a recycle flow system, heating and cooling baths were integrated, with the latter...
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09-14-2013 03:02 PM
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy
Abstract It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all detectable species. The analysis was carried out using experimental data obtained during aggregation of the 10.4 kDa Crh protein, which has been shown to involve a partially unfolded intermediate...
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01-27-2011 04:31 AM
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy.
J Biomol NMR. 2011 Jan 21;
Authors: Etzkorn M, Böckmann A, Baldus M
It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all...
Solvent Relaxation NMR: A Tool for Real-Time Monitoring Water Dynamics in Protein Aggregation Landscape
Linear Mode
