[NMR paper] Rapid Characterization of Structural and Behavioral Changes of Therapeutic Proteins by Relaxation and Diffusion (1)H-SOFAST NMR Experiments
Biologic drugs have emerged as a rapidly expanding and important modality, offering promising therapeutic solutions by interacting with previously "undruggable" targets, thus significantly expanding the range of modern pharmaceutical applications. However, the inherent complexity of these drugs also introduces liabilities and poses challenges in their development, necessitating efficient screening methods to evaluate the structural stability and behavior. Although nuclear magnetic resonance...
Simultaneous measurement of 1 H C/N -R 2 â?²s for rapid acquisition of backbone and sidechain paramagnetic relaxation enhancements (PREs) in proteins
Simultaneous measurement of 1 H C/N -R 2 â?²s for rapid acquisition of backbone and sidechain paramagnetic relaxation enhancements (PREs) in proteins
Abstract
Paramagnetic relaxation enhancements (PREs) are routinely used to provide long-range distance restraints for the determination of protein structures, to resolve protein dynamics, ligandâ??protein binding sites, and lowly populated species, using Nuclear Magnetic Resonance Spectroscopy (NMR). Here, we propose a simultaneous 1H-15Â*N, 1H-13C SESAME based pulse scheme for the rapid acquisition of...
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BEST and SOFAST experiments for resonance assignment of histidine and tyrosine side chains in 13 C/ 15 N labeled proteins
BEST and SOFAST experiments for resonance assignment of histidine and tyrosine side chains in 13 C/ 15 N labeled proteins
Abstract
Aromatic amino-acid side chains are essential components for the structure and function of proteins. We present herein a set of NMR experiments for time-efficient resonance assignment of histidine and tyrosine side chains in uniformly 13C/15N-labeled proteins. The use of band-selective 13C pulses allows to deal with linear chains of coupled spins, thus avoiding signal loss that occurs in branched spin systems during...
Measuring hydrogen exchange in proteins by selective water saturation in 1Hâ??15N SOFAST/BEST-type experiments: advantages and limitations
Measuring hydrogen exchange in proteins by selective water saturation in 1Hâ??15N SOFAST/BEST-type experiments: advantages and limitations
Abstract
HETex-SOFAST NMR (Schanda et al. in J Biomol NMR 33:199â??211, 2006) has been proposed some years ago as a fast and sensitive method for semi-quantitative measurement of site-specific amide-water hydrogen exchange effects along the backbone of proteins. Here we extend this concept to BEST readout sequences that provide a better resolution at the expense of some loss in sensitivity. We discuss the...
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[NMR paper] Rapid Characterization of Hydrogen Exchange in Proteins.
Rapid Characterization of Hydrogen Exchange in Proteins.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Rapid Characterization of Hydrogen Exchange in Proteins.
Angew Chem Int Ed Engl. 2013 Jan 22;
Authors: Thakur A, Chandra K, Dubey A, D'Silva P, Atreya HS
Abstract
Kinetics and thermodynamics of amide hydrogen exchange in proteins can be investigated with two-dimensional (13) CO-(15) N NMR correlation experiments. The spectra are...
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02-03-2013 10:19 AM
Magnetic resonance diffusion and relaxation characterization of water in the unfrozen vein network in polycrystalline ice and its response to microbial metabolic products
Magnetic resonance diffusion and relaxation characterization of water in the unfrozen vein network in polycrystalline ice and its response to microbial metabolic products
December 2012
Publication year: 2012
Source:Journal of Magnetic Resonance, Volume 225</br>
</br>
Polycrystalline ice, as found in glaciers and the ice sheets of Antarctica, is a low porosity porous media consisting of a complicated and dynamic pore structure of liquid-filled intercrystalline veins within a solid ice matrix. In this work, Nuclear Magnetic Resonance measurements of relaxation rates and...
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12-15-2012 09:51 AM
Magnetic resonance diffusion and relaxation characterization of water in the unfrozen vein network in polycrystalline ice and its response to microbial metabolic products
Magnetic resonance diffusion and relaxation characterization of water in the unfrozen vein network in polycrystalline ice and its response to microbial metabolic products
December 2012
Publication year: 2012
Source:Journal of Magnetic Resonance, Volume 225</br>
</br>
Polycrystalline ice, as found in glaciers and the ice sheets of Antarctica, is a low porosity porous media consisting of a complicated and dynamic pore structure of liquid-filled intercrystalline veins within a solid ice matrix. In this work, Nuclear Magnetic Resonance measurements of relaxation rates and...
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12-01-2012 06:10 PM
Magnetic Resonance Diffusion and Relaxation Characterization of Water in the Unfrozen Vein Network in Polycrystalline Ice and its Response to Microbial Metabolic Products
Magnetic Resonance Diffusion and Relaxation Characterization of Water in the Unfrozen Vein Network in Polycrystalline Ice and its Response to Microbial Metabolic Products
Publication year: 2012
Source:Journal of Magnetic Resonance</br>
Jennifer R. Brown, Timothy I. Brox, Sarah J. Vogt, Joseph D. Seymour, Mark Skidmore, Sarah L. Codd</br>
Polycrystalline ice, as found in glaciers and the ice sheets of Antarctica, is a low porosity porous media consisting of a complicated and dynamic pore structure of liquid-filled intercrystalline veins within a solid ice matrix. In...
Rapid Characterization of Structural and Behavioral Changes of Therapeutic Proteins by Relaxation and Diffusion (1)H-SOFAST NMR Experiments
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