[ASAP] Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes As Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations
Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes As Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00195/20180430/images/medium/bi-2018-001959_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00195
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05-01-2018 10:57 PM
[NMR paper] Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes as Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations.
Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes as Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations.
Related Articles Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes as Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations.
Biochemistry. 2018 Apr 17;:
Authors: Baird-Titus JM, Thapa M, Doerdelmann T, Combs KA, Rance M
Abstract
An important but poorly characterized contribution to the thermodynamics of protein-DNA interactions is...
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04-18-2018 01:41 PM
[NMR paper] Site-Resolved Backbone and Side-Chain Intermediate Dynamics in a Carbohydrate-Binding Module Protein Studied by Magic-Angle Spinning NMR Spectroscopy.
Site-Resolved Backbone and Side-Chain Intermediate Dynamics in a Carbohydrate-Binding Module Protein Studied by Magic-Angle Spinning NMR Spectroscopy.
Site-Resolved Backbone and Side-Chain Intermediate Dynamics in a Carbohydrate-Binding Module Protein Studied by Magic-Angle Spinning NMR Spectroscopy.
Chemistry. 2015 Jun 12;
Authors: Ivanir-Dabora H, Nimerovsky E, Madhu PK, Goldbourt A
Abstract
Magic-angle spinning solid-state NMR spectroscopy has been applied to study the dynamics of CBM3b-Cbh9A from Clostridium thermocellum...
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06-16-2015 07:24 PM
[NMR paper] Effective strategy to assign (1)H- (15)N heteronuclear correlation NMR signals from lysine side-chain NH3 (+) groups of proteins at low temperature.
Effective strategy to assign (1)H- (15)N heteronuclear correlation NMR signals from lysine side-chain NH3 (+) groups of proteins at low temperature.
Related Articles Effective strategy to assign (1)H- (15)N heteronuclear correlation NMR signals from lysine side-chain NH3 (+) groups of proteins at low temperature.
J Biomol NMR. 2014 Aug 17;
Authors: Esadze A, Zandarashvili L, Iwahara J
Abstract
Recent studies have shown that lysine side-chain NH3 (+) groups are excellent probes for NMR investigations of dynamics involving...
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08-19-2014 11:21 AM
Effective strategy to assign 1H-15N heteronuclear correlation NMR signals from lysine side-chain NH3 + groups of proteins at low temperature
Effective strategy to assign 1H-15N heteronuclear correlation NMR signals from lysine side-chain NH3 + groups of proteins at low temperature
Abstract
Recent studies have shown that lysine side-chain NH3 + groups are excellent probes for NMR investigations of dynamics involving hydrogen bonds and ion pairs relevant to protein function. However, due to rapid hydrogen exchange, observation of 1H-15N NMR cross peaks from lysine NH3 + groups often requires use of a relatively low temperature, which...
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08-16-2014 10:26 PM
[NMR paper] Investigation of Lysine Side Chain Interactions of Interleukin-8 with Heparin and other Glycosaminoglycans Studied by a Methylation-NMR Approach.
Investigation of Lysine Side Chain Interactions of Interleukin-8 with Heparin and other Glycosaminoglycans Studied by a Methylation-NMR Approach.
Investigation of Lysine Side Chain Interactions of Interleukin-8 with Heparin and other Glycosaminoglycans Studied by a Methylation-NMR Approach.
Glycobiology. 2013 Aug 27;
Authors: Möbius K, Nordsieck K, Pichert A, Samsonov SA, Thomas L, Schiller J, Kalkhof S, Pisabarro MT, Beck-Sickinger AG, Huster D
Abstract
Although the interaction between interleukin-8 (IL-8) and glycosaminoglycans (GAG) is...
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08-29-2013 01:53 PM
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
J Am Chem Soc. 2010 Dec 27;
Authors: Esadze A, Li DW, Wang T, Bru?schweiler R, Iwahara J
Despite their importance in macromolecular interactions and functions, the dynamics of lysine side-chain amino groups in proteins are not well understood. In this study, we have developed the methodology for the investigations of the dynamics...
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12-29-2010 04:04 PM
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear 1H-15N NMR Spectroscopy
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear 1H-15N NMR Spectroscopy
Alexandre Esadze, Da-Wei Li, Tianzhi Wang, Rafael Bru?schweiler and Junji Iwahara
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja107847d/aop/images/medium/ja-2010-07847d_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja107847d
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Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear 1H-15N NMR Spectroscopy - ACS Publications
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