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 region ?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.
[NMR paper] Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR.
Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR.
Related Articles Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR.
Protein Sci. 2015 Feb 2;
Authors: Fasshuber HK, Lakomek NA, Habenstein B, Loquet A, Shi C, Giller K, Wolff S, Becker S, Lange A
Abstract
By applying - and -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....
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02-04-2015 09:57 PM
Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR
Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR
ABSTRACT
By applying - and -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...
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02-02-2015 09:55 PM
[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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10-10-2013 09:38 PM
[NMR paper] Structural role of tyrosine in Bombyx mori silk fibroin, studied by solid-state NMR a
Structural role of tyrosine in Bombyx mori silk fibroin, studied by solid-state NMR and molecular mechanics on a model peptide prepared as silk I and II.
Related Articles Structural role of tyrosine in Bombyx mori silk fibroin, studied by solid-state NMR and molecular mechanics on a model peptide prepared as silk I and II.
Magn Reson Chem. 2004 Feb;42(2):258-66
Authors: Asakura T, Suita K, Kameda T, Afonin S, Ulrich AS
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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11-24-2010 09:25 PM
[NMR paper] Water-protein interactions in microcrystalline crh measured by 1H-13C solid-state NMR
Water-protein interactions in microcrystalline crh measured by 1H-13C solid-state NMR spectroscopy.
Related Articles Water-protein interactions in microcrystalline crh measured by 1H-13C solid-state NMR spectroscopy.
J Am Chem Soc. 2003 Nov 5;125(44):13336-7
Authors: Lesage A, Böckmann A
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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11-24-2010 09:16 PM
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.
Related Articles Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy.
J Am Chem Soc. 2010 Oct 26;
Authors: Schanda P, Meier BH, Ernst M
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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10-29-2010 07:05 PM
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
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja100726a/aop/images/medium/ja-2010-00726a_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/ja100726a
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/vMvBmzNs148
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10-26-2010 08:48 PM
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*
http://pubs.acs.org/isubscribe/journals/jacsat/127/i24/figures/ja0503128n00001.gif
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
