[NMR paper] Direct NMR detection of bifurcated hydrogen bonding in the ?-helix N-caps of ankyrin repeat proteins.
Direct NMR detection of bifurcated hydrogen bonding in the ?-helix N-caps of ankyrin repeat proteins.
Direct NMR detection of bifurcated hydrogen bonding in the ?-helix N-caps of ankyrin repeat proteins.
J Am Chem Soc. 2015 Jan 12;
Authors: Preimesberger MR, Majumdar A, Aksel T, Sforza K, Lectka T, Barrick D, Lecomte JT
Abstract
In biomolecules, bifurcated hydrogen bonds typically involve the interaction of two donor protons with the two lone pairs of oxygen. Here, we present direct NMR evidence for a bifurcated H-bonding...
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01-13-2015 02:31 PM
[NMR paper] NMR-Based Detection of Hydrogen/Deuterium Exchange in Liposome-Embedded Membrane Proteins.
NMR-Based Detection of Hydrogen/Deuterium Exchange in Liposome-Embedded Membrane Proteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png Related Articles NMR-Based Detection of Hydrogen/Deuterium Exchange in Liposome-Embedded Membrane Proteins.
PLoS One. 2014;9(11):e112374
Authors: Yao X, Dürr UH, Gattin Z, Laukat Y, Narayanan RL, Brückner AK, Meisinger C, Lange A, Becker S, Zweckstetter M
Abstract
Membrane proteins play key roles in biology. Determination of...
[NMR paper] Use of H/D isotope effects to gather information about hydrogen bonding and hydrogen exchange rates
Use of H/D isotope effects to gather information about hydrogen bonding and hydrogen exchange rates
Publication date: Available online 11 October 2013
Source:Journal of Magnetic Resonance</br>
Author(s): Mitsuhiro Takeda , Yohei Miyanoiri , Tsutomu Terauchi , Chin-Jiun Yang , Masatsune Kainosho</br>
Polar side-chains in proteins play important roles in formingand maintaining three-dimensional structures, and thus participate invarious biological functions. Until recently, most protein NMR studieshave focused onthe non-exchangeable protons of amino acid...
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10-11-2013 10:43 AM
[NMR paper] An empirical backbone-backbone hydrogen-bonding potential in proteins and its applica
An empirical backbone-backbone hydrogen-bonding potential in proteins and its applications to NMR structure refinement and validation.
Related Articles An empirical backbone-backbone hydrogen-bonding potential in proteins and its applications to NMR structure refinement and validation.
J Am Chem Soc. 2004 Jun 16;126(23):7281-92
Authors: Grishaev A, Bax A
A new multidimensional potential is described that encodes for the relative spatial arrangement of the peptidyl backbone units as observed within a large database of high-resolution X-ray...
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11-24-2010 09:51 PM
[NMR paper] NMR detection of side chain-side chain hydrogen bonding interactions in 13C/15N-label
NMR detection of side chain-side chain hydrogen bonding interactions in 13C/15N-labeled proteins.
Related Articles NMR detection of side chain-side chain hydrogen bonding interactions in 13C/15N-labeled proteins.
J Biomol NMR. 2000 Aug;17(4):305-10
Authors: Liu A, Hu W, Majumdar A, Rosen MK, Patel DJ
We describe the direct observation of side chain-side chain hydrogen bonding interactions in proteins with sensitivity-enhanced NMR spectroscopy. Specifically, the remote correlation between the guanidinium nitrogen 15Nepsilon of arginine 71,...
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11-19-2010 08:29 PM
[NMR paper] Detection of very weak side chain-main chain hydrogen bonding interactions in medium-
Detection of very weak side chain-main chain hydrogen bonding interactions in medium-size 13C/15N-labeled proteins by sensitivity-enhanced NMR spectroscopy.
Related Articles Detection of very weak side chain-main chain hydrogen bonding interactions in medium-size 13C/15N-labeled proteins by sensitivity-enhanced NMR spectroscopy.
J Biomol NMR. 2000 May;17(1):79-82
Authors: Liu A, Hu W, Majumdar A, Rosen MK, Patel DJ
We describe the direct observation of very weak side chain-main chain hydrogen bonding interactions in medium-size 13C/15N-labeled...
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11-18-2010 09:15 PM
Hydrogen-bonding potential to refine NMR structure
An Empirical Backbone-Backbone Hydrogen-Bonding Potential in Proteins and Its Applications to NMR Structure Refinement and Validation
Alexander Grishaev and Ad Bax
J. Am. Chem. Soc.; 2004; 126(23) pp 7281 - 7292
http://pubs.acs.org./isubscribe/journals/jacsat/126/i23/figures/ja0319994n00001.gif
Abstract:
A new multidimensional potential is described that encodes for the relative spatial arrangement of the peptidyl backbone units as observed within a large database of high-resolution X-ray structures. The detailed description afforded by such an analysis provides an opportunity to study...
DirectNMR Detection of Bifurcated Hydrogen Bonding in the ?-HelixN-Caps of Ankyrin Repeat Proteins
Linear Mode
