Related ArticlesIntermolecular Interactions and Protein Dynamics by Solid-State NMR Spectroscopy.
Angew Chem Int Ed Engl. 2015 Nov 2;
Authors: Lamley JM, Öster C, Stevens RA, Lewandowski JR
Abstract
Understanding the dynamics of interacting proteins is a crucial step toward describing many biophysical processes. Here we investigate the backbone dynamics for protein GB1 in two different assemblies: crystalline GB1 and the precipitated GB1-antibody complex with a molecular weight of more than 300 kDa. We perform these measurements on samples containing as little as eight nanomoles of GB1. From measurements of site-specific (15) N relaxation rates including relaxation dispersion we obtain snapshots of dynamics spanning nine orders of magnitude in terms of the time scale. A comparison of measurements for GB1 in either environment reveals that while many of the dynamic features of the protein are conserved between them (in particular for the fast picosecond-nanosecond motions), much greater differences occur for slow motions with motions in the >500 ns range being more prevalent in the complex. The data suggest that GB1 can potentially undergo a small-amplitude overall anisotropic motion sampling the interaction interface in the complex.
PMID: 26537742 [PubMed - as supplied by publisher]
[NMR paper] Direct Evidence of Imino Acid-Aromatic Interactions in Native Collagen Protein by DNP-Enhanced Solid-State NMR Spectroscopy.
Direct Evidence of Imino Acid-Aromatic Interactions in Native Collagen Protein by DNP-Enhanced Solid-State NMR Spectroscopy.
Related Articles Direct Evidence of Imino Acid-Aromatic Interactions in Native Collagen Protein by DNP-Enhanced Solid-State NMR Spectroscopy.
J Phys Chem Lett. 2014 Nov 20;5(22):4044-8
Authors: Singh C, Rai RK, Aussenac F, Sinha N
Abstract
Aromatic amino acids (AAAs) have rare presence (~1.4% abundance of Phe) inside of collagen protein, which is the most abundant animal protein playing a functional role in...
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Direct Evidence of Imino Acid–Aromatic Interactions in Native Collagen Protein by DNP-Enhanced Solid-State NMR Spectroscopy
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Direct Evidence of Imino Acid–Aromatic Interactions in Native Collagen Protein by DNP-Enhanced Solid-State NMR Spectroscopy
Singh, C., et al., Direct Evidence of Imino Acid–Aromatic Interactions in Native Collagen Protein by DNP-Enhanced Solid-State NMR Spectroscopy. The Journal of Physical Chemistry Letters, 2014. 5(22): p. 4044-4048.
http://dx.doi.org/10.1021/jz502081j
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11-24-2014 04:15 PM
[NMR paper] Solid-state NMR Spectroscopy to Study Protein-Lipid Interactions.
Solid-state NMR Spectroscopy to Study Protein-Lipid Interactions.
Related Articles Solid-state NMR Spectroscopy to Study Protein-Lipid Interactions.
Biochim Biophys Acta. 2013 Dec 11;
Authors: Huster D
Abstract
The appropriate lipid environment is crucial for the proper function of membrane proteins. There is a tremendous variety of lipid molecules in the membrane and so far it is often unclear which component of the lipid matrix is essential for the function of a respective protein. Lipid molecules and proteins mutually influence...
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12-18-2013 04:00 PM
Solid-state NMR Spectroscopy to Study Protein-Lipid Interactions
Solid-state NMR Spectroscopy to Study Protein-Lipid Interactions
Publication date: Available online 12 December 2013
Source:Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids</br>
Author(s): Daniel Huster</br>
The appropriate lipid environment is crucial for the proper function of membrane proteins. There is a tremendous variety of lipid molecules in the membrane and so far it is often unclear which component of the lipid matrix is essential for the function of a respective protein. Lipid molecules and proteins mutually influence each other;...
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[NMR paper] Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state.
Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state.
Related Articles Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state.
J Mol Biol. 2013 Nov 15;
Authors: Sackett K, Nethercott MJ, Zheng Z, Weliky DP
Abstract
The HIV gp41 protein catalyzes fusion between viral and target cell membranes. Although...
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Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state
Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state
Publication date: Available online 16 November 2013
Source:Journal of Molecular Biology</br>
Author(s): Kelly Sackett , Matthew J. Nethercott , Zhaoxiong Zheng , David P. Weliky</br>
The HIV gp41 protein catalyzes fusion between viral and target cell membranes. Although the ~20-residue N-terminal fusion peptide (FP) region is critical for fusion, the structure of this region is not...
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Intermolecular Alignment in Y145Stop Human Prion Protein Amyloid Fibrils Probed by Solid-State NMR Spectroscopy
Intermolecular Alignment in Y145Stop Human Prion Protein Amyloid Fibrils Probed by Solid-State NMR Spectroscopy
Jonathan J. Helmus, Krystyna Surewicz, Marcin I. Apostol, Witold K. Surewicz and Christopher P. Jaroniec
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja206469q/aop/images/medium/ja-2011-06469q_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja206469q
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/e9F1wuu5168
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Intermolecular Alignment in Y145Stop Human Prion Protein Amyloid Fibrils Probed by Solid-State NMR Spectroscopy.
Intermolecular Alignment in Y145Stop Human Prion Protein Amyloid Fibrils Probed by Solid-State NMR Spectroscopy.
Intermolecular Alignment in Y145Stop Human Prion Protein Amyloid Fibrils Probed by Solid-State NMR Spectroscopy.
J Am Chem Soc. 2011 Aug 10;
Authors: Helmus JJ, Surewicz K, Apostol MI, Surewicz WK, Jaroniec CP
The Y145Stop mutant of human prion protein, huPrP23-144, has been linked to PrP cerebral amyloid angiopathy, an inherited amyloid disease, and also serves as a valuable in vitro model for investigating the molecular basis of...
Intermolecular Interactions and Protein Dynamics by Solid-State NMR Spectroscopy.
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