[NMR paper] Direct Observation of CH/CH van der Waals Interactions in Proteins by NMR.
Direct Observation of CH/CH van der Waals Interactions in Proteins by NMR.
Direct Observation of CH/CH van der Waals Interactions in Proteins by NMR.
J Am Chem Soc. 2018 Feb 26;:
Authors: Li J, Wang Y, An L, Chen J, Yao L
Abstract
van der Waals interactions are important to protein stability and function. These interactions are usually identified empirically based on protein 3D structures. In this work, we performed a solution nuclear magnetic resonance (NMR) spectroscopy study of van der Waals interactions by detecting the...
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02-27-2018 12:30 PM
[NMR paper] "Rules of Engagement" of Protein-Glycoconjugate Interactions: A Molecular View Achievable by using NMR Spectroscopy and Molecular Modeling.
"Rules of Engagement" of Protein-Glycoconjugate Interactions: A Molecular View Achievable by using NMR Spectroscopy and Molecular Modeling.
"Rules of Engagement" of Protein-Glycoconjugate Interactions: A Molecular View Achievable by using NMR Spectroscopy and Molecular Modeling.
ChemistryOpen. 2016 Aug;5(4):274-96
Authors: Marchetti R, Perez S, Arda A, Imberty A, Jimenez-Barbero J, Silipo A, Molinaro A
Abstract
Understanding the dynamics of protein-ligand interactions, which lie at the heart of host-pathogen recognition,...
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08-23-2016 01:22 PM
[NMR paper] The "long tail" of the protein tumbling correlation function: observation by (1)H NMR relaxometry in a wide frequency and concentration range.
The "long tail" of the protein tumbling correlation function: observation by (1)H NMR relaxometry in a wide frequency and concentration range.
Related Articles The "long tail" of the protein tumbling correlation function: observation by (1)H NMR relaxometry in a wide frequency and concentration range.
J Biomol NMR. 2015 Nov 18;
Authors: Roos M, Hofmann M, Link S, Ott M, Balbach J, Rössler E, Saalwächter K, Krushelnitsky A
Abstract
Inter-protein interactions in solution affect the auto-correlation function of Brownian tumbling not...
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11-20-2015 06:29 PM
[NMR900 blog] CSC 2013 symposium - "Halogen Bonding and other Non-Covalent Interactions"
CSC 2013 symposium - "Halogen Bonding and other Non-Covalent Interactions"
David Bryce (Ottawa) and Mark Taylor (Toronto) are organizing a symposium on "Halogen Bonding and other Non-Covalent Interactions" to be held as part of the Canadian Chemistry Conference in Quebec City, May 26-30, 2013. International experts including Prof. Pierangelo Metrangolo (Milan, Italy), Prof. Giuseppe Resnati (Milan, Italy), Prof. P. Shing Ho (Colorado State, USA), and Prof. Duncan Bruce (York, UK) have already agreed to give oral presentations at the meeting. Although this is not an NMR-focussed symposium,...
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10-22-2012 09:07 PM
Detecting the "Afterglow" of (13)C NMR in Proteins Using Multiple Receivers.
Detecting the "Afterglow" of (13)C NMR in Proteins Using Multiple Receivers.
Related Articles Detecting the "Afterglow" of (13)C NMR in Proteins Using Multiple Receivers.
J Am Chem Soc. 2010 Dec 2;
Authors: Kupc?e E, Kay LE, Freeman R
We show that the weak signal that remains after (13)C-detected experiments (the (13)C "afterglow") can still be measured with high sensitivity by proton detection. This is illustrated by the incorporation of two experiments, 2D (HA)CACO and 3D (HA)CA(CO)NNH, into a single pulse sequence that makes use of two receivers...
Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholi
Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholipid Bilayers Give Equivalent Angular Constraints for NMR Structure Determination.
Related Articles Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholipid Bilayers Give Equivalent Angular Constraints for NMR Structure Determination.
J Phys Chem B. 2010 Oct 20;
Authors: Park SH, Das BB, De Angelis AA, Scrima M, Opella SJ
The native environment for membrane proteins is the highly asymmetric phospholipid bilayer, and this has a large...
Correction to "Direct Observation of CH/CH van der Waals Interactions in Proteins by NMR"
Linear Mode
