Related ArticlesUnraveling 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 of different energy barriers. NMR relaxation can in principle provide a site-specific picture of both the time scales and amplitudes of these motions, but independent relaxation rates sensitive to fluctuations in different time scale ranges are required to obtain a faithful representation of the underlying dynamic complexity. This is especially pertinent for relaxation measurements in the solid state, which report on dynamics in a broader window of time scales by more than 3 orders of magnitudes compared to solution NMR relaxation. To aid in unraveling the intricacies of biomolecular dynamics we introduce (13)C spin-lattice relaxation in the rotating frame (R1?) as a probe of backbone nanosecond-microsecond motions in proteins in the solid state. We present measurements of (13)C' R1? rates in fully protonated crystalline protein GB1 at 600 and 850 MHz (1)H Larmor frequencies and compare them to (13)C' R1, (15)N R1 and R1? measured under the same conditions. The addition of carbon relaxation data to the model free analysis of nitrogen relaxation data leads to greatly improved characterization of time scales of protein backbone motions, minimizing the occurrence of fitting artifacts that may be present when (15)N data is used alone. We also discuss how internal motions characterized by different time scales contribute to (15)N and (13)C relaxation rates in the solid state and solution state, leading to fundamental differences between them, as well as phenomena such as underestimation of picosecond-range motions in the solid state and nanosecond-range motions in solution.
PMID: 26234369 [PubMed - as supplied by publisher]
[NMR paper] General Order Parameter based Correlation Analysis of Protein Backbone Motions between Experimental NMR Relaxation Measurements and Molecular Dynamics Simulations.
General Order Parameter based Correlation Analysis of Protein Backbone Motions between Experimental NMR Relaxation Measurements and Molecular Dynamics Simulations.
Related Articles General Order Parameter based Correlation Analysis of Protein Backbone Motions between Experimental NMR Relaxation Measurements and Molecular Dynamics Simulations.
Biochem Biophys Res Commun. 2015 Jan 16;
Authors: Liu Q, Shi C, Yu L, Zhang L, Xiong Y, Tian C
Abstract
Internal backbone dynamic motions are essential for different protein functions and...
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01-21-2015 08:39 PM
General Order Parameter based Correlation Analysis of Protein Backbone Motions between Experimental NMR Relaxation Measurements and Molecular Dynamics Simulations
General Order Parameter based Correlation Analysis of Protein Backbone Motions between Experimental NMR Relaxation Measurements and Molecular Dynamics Simulations
Publication date: Available online 16 January 2015
Source:Biochemical and Biophysical Research Communications</br>
Author(s): Qing Liu , Chaowei Shi , Lu Yu , Longhua Zhang , Ying Xiong , Changlin Tian</br>
Internal backbone dynamic motions are essential for different protein functions and occur on a wide range of time scales, from femtoseconds to seconds. Molecular dynamic (MD) simulations and...
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01-17-2015 04:14 PM
[NMR paper] Mapping Membrane Protein Backbone Dynamics: A Comparison of Site-Directed Spin Labeling with NMR (15)N-Relaxation Measurements.
Mapping Membrane Protein Backbone Dynamics: A Comparison of Site-Directed Spin Labeling with NMR (15)N-Relaxation Measurements.
Related Articles Mapping Membrane Protein Backbone Dynamics: A Comparison of Site-Directed Spin Labeling with NMR (15)N-Relaxation Measurements.
Biophys J. 2014 Oct 7;107(7):1697-1702
Authors: Lo RH, Kroncke BM, Solomon TL, Columbus L
Abstract
The ability to detect nanosecond backbone dynamics with site-directed spin labeling (SDSL) in soluble proteins has been well established. However, for membrane...
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10-09-2014 07:31 PM
Mapping Membrane Protein Backbone Dynamics: A Comparison of Site-Directed Spin Labeling with NMR 15N-Relaxation Measurements
Mapping Membrane Protein Backbone Dynamics: A Comparison of Site-Directed Spin Labeling with NMR 15N-Relaxation Measurements
Publication date: 7 October 2014
Source:Biophysical Journal, Volume 107, Issue 7</br>
Author(s): Ryan*H. Lo , Brett*M. Kroncke , Tsega*L. Solomon , Linda Columbus</br>
The ability to detect nanosecond backbone dynamics with site-directed spin labeling (SDSL) in soluble proteins has been well established. However, for membrane proteins, the nitroxide appears to have more interactions with the protein surface, potentially hindering the...
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10-08-2014 04:17 AM
[NMR paper] Backbone dynamics of the olfactory marker protein as studied by 15N NMR relaxation measurements.
Backbone dynamics of the olfactory marker protein as studied by 15N NMR relaxation measurements.
Related Articles Backbone dynamics of the olfactory marker protein as studied by 15N NMR relaxation measurements.
Biochemistry. 2005 Jul 19;44(28):9673-9
Authors: Gitti RK, Wright NT, Margolis JW, Varney KM, Weber DJ, Margolis FL
Nuclear magnetic resonance (NMR) (15)N relaxation measurements of the olfactory marker protein (OMP) including longitudinal relaxation (T(1)), transverse relaxation (T(2)), and (15)N-{(1)H} NOE data were collected at low...
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12-01-2010 06:56 PM
[NMR paper] Thermodynamic interpretation of protein dynamics from NMR relaxation measurements.
Thermodynamic interpretation of protein dynamics from NMR relaxation measurements.
Related Articles Thermodynamic interpretation of protein dynamics from NMR relaxation measurements.
Protein Pept Lett. 2005 Apr;12(3):235-40
Authors: Spyracopoulos L
Protein dynamics and thermodynamics can be characterized through measurements of relaxation rates of side chain (2)H and (13)C, and backbone (15)N nuclei using NMR spectroscopy. The rates reflect protein motions on timescales from picoseconds to milliseconds. Backbone and methyl side chain NMR...
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11-25-2010 08:21 PM
[NMR paper] Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectro
Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy.
Related Articles Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy.
J Am Chem Soc. 2004 Sep 22;126(37):11422-3
Authors: Giraud N, Böckmann A, Lesage A, Penin F, Blackledge M, Emsley L
Site-specific nitrogen-15 longitudinal relaxation rates are measured for the microcrystalline dimeric form of the protein Crh using multidimensional high-resolution solid-state NMR methods. The measured rates are used to provide a...
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11-24-2010 10:01 PM
[NMR paper] Superslow backbone protein dynamics as studied by 1D solid-state MAS exchange NMR spe
Superslow backbone protein dynamics as studied by 1D solid-state MAS exchange NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Superslow backbone protein dynamics as studied by 1D solid-state MAS exchange NMR spectroscopy.
J Magn Reson. 1999 Jun;138(2):244-55
Authors: Krushelnitsky A, Reichert D, Hempel G, Fedotov V, Schneider H, Yagodina L, Schulga A
Superslow backbone dynamics of the protein barstar and the polypeptide polyglycine was studied by...
Unraveling the complexity of protein backbone dynamics with combined (13)C and (15)N solid-state NMR relaxation measurements.
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