Related ArticlesMicrosecond timescale protein dynamics: a combined solid-state NMR approach.
Chemphyschem. 2017 Nov 17;:
Authors: Rovó P, Linser R
Abstract
Conformational exchange in proteins is a major determinant in protein functionality. In particular, the ?s-ms timescale is associated with enzymatic activity and interactions between biological molecules. We show here that a comprehensive data set of R1? relaxation dispersion profiles employing multiple effective fields and tilt angles can be easily obtained in perdeuterated, partly back-exchanged proteins at fast magic-angle spinning and further complemented with chemical-exchange saturation transfer NMR experiments. The approach exploits complementary sources of information and enables the extraction of multiple exchange parameters for ?s-ms timescale conformational exchange, most notably including the sign of the chemical shift differences between the ground and excited states.
PMID: 29149466 [PubMed - as supplied by publisher]
Investigating Sodium Storage Mechanisms in Tin Anodes: A Combined Pair Distribution Function Analysis, Density Functional Theory, and Solid-State NMR Approach
Investigating Sodium Storage Mechanisms in Tin Anodes: A Combined Pair Distribution Function Analysis, Density Functional Theory, and Solid-State NMR Approach
Joshua M. Stratford, Martin Mayo, Phoebe K. Allan, Oliver Pecher, Olaf J. Borkiewicz, Kamila M. Wiaderek, Karena W. Chapman, Chris J. Pickard, Andrew J. Morris and Clare P. Grey
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.7b01398/20170516/images/medium/ja-2017-01398w_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.7b01398
...
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[NMR paper] Microsecond dynamics in ubiquitin probed by solid-state NMR 15N R1rho relaxation experiments under fast MAS (60-110 kHz).
Microsecond dynamics in ubiquitin probed by solid-state NMR 15N R1rho relaxation experiments under fast MAS (60-110 kHz).
Related Articles Microsecond dynamics in ubiquitin probed by solid-state NMR 15N R1rho relaxation experiments under fast MAS (60-110 kHz).
Chemistry. 2017 Apr 20;:
Authors: Lakomek NA, Penzel S, Lends A, Cadalbert R, Ernst M, Meier BH
Abstract
15N R1? relaxation experiments in solid-state NMR are sensitive to timescales and amplitudes of internal protein motions in the hundreds of ns to µs time window,...
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04-21-2017 03:35 PM
[NMR paper] Unraveling the complexity of protein backbone dynamics with combined (13)C and (15)N solid-state NMR relaxation measurements.
Unraveling the complexity of protein backbone dynamics with combined (13)C and (15)N solid-state NMR relaxation measurements.
Related Articles Unraveling the complexity of protein backbone dynamics with combined (13)C and (15)N solid-state NMR relaxation measurements.
Phys Chem Chem Phys. 2015 Aug 3;
Authors: Lamley JM, Lougher MJ, Sass HJ, Rogowski M, Grzesiek S, Lewandowski JR
Abstract
Typically, protein dynamics involve a complex hierarchy of motions occurring on different time scales between conformations separated by a range...
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08-04-2015 03:00 PM
[NMR paper] Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach.
Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach.
Related Articles Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach.
J Biomol NMR. 2015 Jan 8;
Authors: Sinnige T, Houben K, Pritisanac I, Renault M, Boelens R, Baldus M
Abstract
The ?-barrel assembly machinery (BAM) is involved in folding and insertion of outer membrane proteins in Gram-negative bacteria, a process that is still poorly...
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01-09-2015 03:58 PM
Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach
Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach
Abstract
The β-barrel assembly machinery (BAM) is involved in folding and insertion of outer membrane proteins in Gram-negative bacteria, a process that is still poorly understood. With its 790 residues, BamA presents a challenge to current NMR methods. We utilized a â??divide and conquerâ?? approach in which we first obtained resonance assignments for BamAâ??s periplasmic POTRA domains 4 and 5 by solution NMR. Comparison of...
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01-08-2015 01:02 AM
[NMR paper] Structure and Topology of the Huntingtin 1-17 Membrane Anchor by*a*Combined Solution and Solid-State NMR Approach.
Structure and Topology of the Huntingtin 1-17 Membrane Anchor by*a*Combined Solution and Solid-State NMR Approach.
Structure and Topology of the Huntingtin 1-17 Membrane Anchor by*a*Combined Solution and Solid-State NMR Approach.
Biophys J. 2013 Aug 6;105(3):699-710
Authors: Michalek M, Salnikov ES, Bechinger B
Abstract
The very amino-terminal domain of the huntingtin protein is directly located upstream of the protein's polyglutamine tract, plays a decisive role in several important properties of this large protein and in the development...
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An ensemble dynamics approach to decipher solid-state NMR observables of membrane proteins
An ensemble dynamics approach to decipher solid-state NMR observables of membrane proteins
February 2012
Publication year: 2012
Source:Biochimica et Biophysica Acta (BBA) - Biomembranes, Volume 1818, Issue 2</br>
</br>
Solid-state NMR (SSNMR) is an invaluable tool for determining orientations of membrane proteins and peptides in lipid bilayers. Such orientational descriptions provide essential information about membrane protein functions. However, when a semi-static single conformer model is used to interpret various SSNMR observables, important dynamics information can...
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[NMR paper] Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR
Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR R1rho relaxation experiments.
Related Articles Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR R1rho relaxation experiments.
Protein Sci. 2005 Mar;14(3):735-42
Authors: Massi F, Grey MJ, Palmer AG
NMR spin relaxation experiments are used to characterize the dynamics of the backbone of ubiquitin. Chemical exchange processes affecting residues Ile 23, Asn 25, Thr 55, and Val 70 are characterized using on- and off-resonance...
Microsecond timescale protein dynamics: a combined solid-state NMR approach.
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