Combination of NMR spectroscopy and X-ray crystallography offers unique advantages for elucidation of the structural basis of protein complex assembly.
Combination of NMR spectroscopy and X-ray crystallography offers unique advantages for elucidation of the structural basis of protein complex assembly.
Combination of NMR spectroscopy and X-ray crystallography offers unique advantages for elucidation of the structural basis of protein complex assembly.
Sci China Life Sci. 2011 Feb;54(2):101-11
Authors: Feng W, Pan L, Zhang M
NMR spectroscopy and X-ray crystallography are two premium methods for determining the atomic structures of macro-biomolecular complexes. Each method has unique strengths and weaknesses. While the two techniques are highly complementary, they have generally been used separately to address the structure and functions of biomolecular complexes. In this review, we emphasize that the combination of NMR spectroscopy and X-ray crystallography offers unique power for elucidating the structures of complicated protein assemblies. We demonstrate, using several recent examples from our own laboratory, that the exquisite sensitivity of NMR spectroscopy in detecting the conformational properties of individual atoms in proteins and their complexes, without any prior knowledge of conformation, is highly valuable for obtaining the high quality crystals necessary for structure determination by X-ray crystallography. Thus NMR spectroscopy, in addition to answering many unique structural biology questions that can be addressed specifically by that technique, can be exceedingly powerful in modern structural biology when combined with other techniques including X-ray crystallography and cryo-electron microscopy.
NMR as a Unique Tool in Assessment and Complex Determination of Weak Protein-Protein Interactions.
NMR as a Unique Tool in Assessment and Complex Determination of Weak Protein-Protein Interactions.
NMR as a Unique Tool in Assessment and Complex Determination of Weak Protein-Protein Interactions.
Top Curr Chem. 2011 Aug 2;
Authors: Vinogradova O, Qin J
Protein-protein interactions are crucial for a wide variety of biological processes. These interactions range from high affinity (K (d) < nM) to very low affinity (K (d) > mM). While much is known about the nature of high affinity protein complexes, our knowledge about structural characteristics...
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08-03-2011 12:00 PM
[NMR images] The basis of NMR spectroscopy
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The basis of NMR spectroscopy
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02-01-2011 06:40 PM
Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy
Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy
Abstract Long-range structural information derived from paramagnetic relaxation enhancement observed in the presence of a paramagnetic nitroxide radical is highly useful for structural characterization of globular, modular and intrinsically disordered proteins, as well as protein�??protein and protein-DNA complexes. Here we characterized the conformation of a spin-label attached to the homodimeric protein CylR2 using a combination of X-ray crystallography, electron...
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01-31-2011 06:03 AM
Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy.
Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy.
Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy.
J Biomol NMR. 2011 Jan 28;
Authors: Gruene T, Cho MK, Karyagina I, Kim HY, Grosse C, Giller K, Zweckstetter M, Becker S
Long-range structural information derived from paramagnetic relaxation enhancement observed in the presence of a paramagnetic nitroxide radical is highly useful for structural characterization of...
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01-29-2011 12:35 PM
[NMR paper] The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of co
The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein.
Related Articles The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein.
Nat Struct Biol. 2000 Apr;7(4):329-35
Authors: Varani L, Gunderson SI, Mattaj IW, Kay LE, Neuhaus D, Varani G
The status of the poly(A) tail at the 3'-end of mRNAs controls the expression of numerous genes in response to...
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11-18-2010 09:15 PM
Solid-state NMR and SAXS studies provide a structural basis for the activation of alp
Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers.
Related Articles Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers.
Nat Struct Mol Biol. 2010 Aug 29;
Authors: Jehle S, Rajagopal P, Bardiaux B, Markovic S, Kühne R, Stout JR, Higman VA, Klevit RE, van Rossum BJ, Oschkinat H
The small heat shock protein alphaB-crystallin (alphaB) contributes to cellular protection against stress. For decades, high-resolution structural studies on...
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08-31-2010 09:42 PM
[Ryan's blog] Structure 2010, The Faulkner Rules, and a Philosophical Basis of Structural Elucidati
Source: Ryan's blog
Structure 2010, The Faulkner Rules, and a Philosophical Basis of Structural Elucidation
I was fortunate enough to attend the inaugural Structure 2010 conference in Leicestershire, UK last week. This was a terrific event that focused on the structure elucidation of small molecules. The program for this conference was outstanding. Unfortunately I didn't...
Combination of NMR spectroscopy and X-ray crystallography offers unique advantages for elucidation of the structural basis of protein complex assembly.
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