[NMR paper] Structure determination of uniformly (13)C, (15)N labeled protein using qualitative distance restraints from MAS solid-state (13)C-NMR observed paramagnetic relaxation enhancement.
Structure determination of uniformly (13)C, (15)N labeled protein using qualitative distance restraints from MAS solid-state (13)C-NMR observed paramagnetic relaxation enhancement.
Related Articles Structure determination of uniformly (13)C, (15)N labeled protein using qualitative distance restraints from MAS solid-state (13)C-NMR observed paramagnetic relaxation enhancement.
J Biomol NMR. 2016 Jan 4;
Authors: Tamaki H, Egawa A, Kido K, Kameda T, Kamiya M, Kikukawa T, Aizawa T, Fujiwara T, Demura M
Abstract
Magic angle spinning...
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01-07-2016 08:36 AM
Comparison of backbone dynamics of the type III antifreeze protein and antifreeze-like domain of human sialic acid synthase
Comparison of backbone dynamics of the type III antifreeze protein and antifreeze-like domain of human sialic acid synthase
Abstract
Antifreeze proteins (AFPs) are found in a variety of cold-adapted (psychrophilic) organisms to promote survival at subzero temperatures by binding to ice crystals and decreasing the freezing temperature of body fluids. The type III AFPs are small globular proteins that consist of one α-helix, three 310-helices, and two β-strands. Sialic acids play important roles in a variety of biological functions, such as...
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01-09-2015 03:58 PM
[NMR paper] Dynamic Interaction Between Membrane-Bound Full-Length Cytochrome P450 and Cytochrome b5 Observed by Solid-State NMR Spectroscopy.
Dynamic Interaction Between Membrane-Bound Full-Length Cytochrome P450 and Cytochrome b5 Observed by Solid-State NMR Spectroscopy.
Dynamic Interaction Between Membrane-Bound Full-Length Cytochrome P450 and Cytochrome b5 Observed by Solid-State NMR Spectroscopy.
Sci Rep. 2013 Aug 29;3:2538
Authors: Yamamoto K, Dürr UH, Xu J, Im SC, Waskell L, Ramamoorthy A
Abstract
Microsomal monoxygenase enzymes of the cytochrome-P450 family are found in all biological kingdoms, and play a central role in the breakdown of metabolic as well as...
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08-30-2013 04:35 PM
[NMR paper] Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
Related Articles Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
J Biomol NMR. 2005 Jul;32(3):195-207
Authors: Böckmann A, Juy M, Bettler E, Emsley L, Galinier A, Penin F, Lesage A
We report site-resolved observation of hydrogen exchange in the micro-crystalline protein Crh. Our approach is based on the use of proton T2' -selective 1H-13C-13C correlation spectra for...
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12-01-2010 06:56 PM
Protein-ice interaction of an antifreeze protein observed with solid-state NMR [Chemi
Protein-ice interaction of an antifreeze protein observed with solid-state NMR
Siemer, A. B., Huang, K.-Y., McDermott, A. E....
Date: 2010-10-12
NMR on frozen solutions is an ideal method to study fundamental questions of macromolecular hydration, because the hydration shell of many biomolecules does not freeze together with bulk solvent. In the present study, we present previously undescribed NMR methods to study the interactions of proteins with their hydration shell and the ice lattice in frozen solution. We applied these methods to compare solvent interaction of an ice-binding...
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10-13-2010 04:10 AM
Protein-ice interaction of an antifreeze protein observed with solid-state NMR.
Protein-ice interaction of an antifreeze protein observed with solid-state NMR.
Related Articles Protein-ice interaction of an antifreeze protein observed with solid-state NMR.
Proc Natl Acad Sci U S A. 2010 Sep 30;
Authors: Siemer AB, Huang KY, McDermott AE
NMR on frozen solutions is an ideal method to study fundamental questions of macromolecular hydration, because the hydration shell of many biomolecules does not freeze together with bulk solvent. In the present study, we present previously undescribed NMR methods to study the interactions...
Protein–ice interaction of an antifreeze protein observed with solid-state NMR - pnas.org
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