[NMR paper] Identification of interaction partners using protein aggregation and NMR spectroscopy
Identification of interaction partners using protein aggregation and NMR spectroscopy
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...
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nmrlearner
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09-11-2022 10:03 PM
[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
[ASAP] Dissecting the Protein Dynamics Coupled Ligand Binding with Kinetic Models and Single-Molecule FRET
Dissecting the Protein Dynamics Coupled Ligand Binding with Kinetic Models and Single-Molecule FRET
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.1c00771/20220228/images/medium/bi1c00771_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.1c00771
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03-02-2022 01:13 PM
Binding and Energetics of Electron Transfer betweenan Artificial Four-Helix Mn-Protein and Reaction Centers from Rhodobacter sphaeroides
Binding and Energetics of Electron Transfer betweenan Artificial Four-Helix Mn-Protein and Reaction Centers from Rhodobacter sphaeroides
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00978/20171128/images/medium/bi-2017-00978p_0011.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00978
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/BzbxrJbQOg0
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11-29-2017 09:22 AM
[NMR paper] Acceleration of protein backbone NMR assignment by combinatorial labeling: Application to a small molecule binding study.
Acceleration of protein backbone NMR assignment by combinatorial labeling: Application to a small molecule binding study.
Acceleration of protein backbone NMR assignment by combinatorial labeling: Application to a small molecule binding study.
Biopolymers. 2016 Dec 30;:
Authors: Hein C, Löhr F, Schwarz D, Dötsch V
Abstract
Selective labeling with stable isotopes has long been recognized as a valuable tool in protein NMR to alleviate signal overlap and sensitivity limitations. In this study, combinatorial (15) N-, (13) C(?) -,...
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12-31-2016 12:18 PM
NMRMethod for Characterizing Microsecond-to-MillisecondChemical Exchanges Utilizing Differential Multiple-Quantum Relaxationin High Molecular Weight Proteins
NMRMethod for Characterizing Microsecond-to-MillisecondChemical Exchanges Utilizing Differential Multiple-Quantum Relaxationin High Molecular Weight Proteins
Yuki Toyama, Masanori Osawa, Mariko Yokogawa and Ichio Shimada
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.5b12954/20160208/images/medium/ja-2015-12954n_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.5b12954
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/p9bBsJBEoDE
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02-09-2016 04:21 AM
[NMR paper] TROSY NMR with a 52 kDa sugar transport protein and the binding of a small-molecule inhibitor.
TROSY NMR with a 52 kDa sugar transport protein and the binding of a small-molecule inhibitor.
Related Articles TROSY NMR with a 52 kDa sugar transport protein and the binding of a small-molecule inhibitor.
Mol Membr Biol. 2014 May 7;
Authors: Kalverda AP, Gowdy J, Thompson GS, Homans SW, Henderson PJ, Patching SG
Abstract
Abstract Using the sugar transport protein, GalP, from Escherichia coli, which is a homologue of human GLUT transporters, we have overcome the challenges for achieving high-resolution - and -methyl-TROSY NMR...
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05-09-2014 07:01 PM
Scientists Paint New Picture of Dance Between Protein and Binding Partners - Science Daily (press release)
Scientists Paint New Picture of Dance Between Protein and Binding Partners - Science Daily (press release)
<img alt="" height="1" width="1" />
Scientists Paint New Picture of Dance Between Protein and Binding Partners
Science Daily (press release)
The new study -- which used a number of complementary technologies including NMR spectroscopy and hydrogen/deuterium exchange (HDX) coupled to mass spectrometery, combined with previous x-ray crystallography analyses -- provides detailed insights into ...
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Artificial Protein Crosstalk with a Molecule that Exchanges Binding Partners
Linear Mode
