By applying [1-13C]- and [2-13C]-glucose labeling schemes to the folded globular protein ubiquitin, a strong reduction of spectral crowding and increase in resolution in solid-state NMR (ssNMR) spectra could be achieved. This allowed spectral resonance assignment in a straightforward manner and the collection of a wealth of long-range distance information. A high precision solid-state NMR structure of microcrystalline ubiquitin was calculated with a backbone rmsd of 1.57 to the X-ray structure and 1.32 Å to the solution NMR structure. Interestingly, we can resolve structural heterogeneity as the presence of three slightly different conformations. Structural heterogeneity is most significant for the loop regions ?1-?2 but also for ?-strands ?1, ?2, ?3 and ?5 as well as for the loop connecting ?1 and ?3. This structural polymorphism observed in the solid-state NMR spectra coincides with regions that showed dynamics in solution NMR experiments on different timescales. This article is protected by copyright. All rights reserved.
[NMR paper] Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin.
Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin.
J Biomol NMR. 2013 Oct 9;
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Structure Calculation from Unambiguous Long-Range Amide and Methyl (1)H-(1)H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy.
Structure Calculation from Unambiguous Long-Range Amide and Methyl (1)H-(1)H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy.
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J Am Chem Soc. 2011 Mar 24;
Authors: Linser R, Bardiaux B, Higman V, Fink U, Reif B
Magic-angle spinning (MAS) solid-state NMR becomes an increasingly important tool for the determination of structures of membrane...
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Structure Calculation from Unambiguous Long-Range Amide and Methyl 1H-1H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy
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http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja110222h/aop/images/medium/ja-2010-10222h_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja110222h
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[NMR paper] Structural role of tyrosine in Bombyx mori silk fibroin, studied by solid-state NMR a
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The influence of the bulky and H-bonding Tyr side-chain on its Ala- and Gly-rich environment in Bombyx mori silk fibroin was...
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Using solid-state NMR carbon-proton dipolar correlation spectroscopy, we observed hydrogen exchange on the millisecond time scale between water molecules and protein protons in a solid sample. These interactions are shown to be related to important structural...
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Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by S
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J Am Chem Soc. 2010 Oct 26;
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Characterization of protein dynamics by solid-state NMR spectroscopy requires robust and accurate measurement protocols, which are not yet fully developed. In this study, we investigate the backbone dynamics of microcrystalline ubiquitin...
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Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by S
Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy
Paul Schanda, Beat H. Meier and Matthias Ernst
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Journal of the American Chemical Society
DOI: 10.1021/ja100726a
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Ubiquitin structure by solid-state NMR
Protein Structure Determination by High-Resolution Solid-State NMR Spectroscopy: Application to Microcrystalline Ubiquitin
Stephan G. Zech,* A. Joshua Wand, and Ann E. McDermott*
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Contribution from the Department of Chemistry, Columbia University, 3000 Broadway Mail Code 3113, New York, New York 10027, and Department of Biochemistry and Biophysics, University of Pennsylvania, The Johnson Research Foundation, Philadelphia, Pennsylvania 19104
J. Am. Chem. Soc., 127 (24), 8618 -8626, 2005.
Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR
Linear Mode
