Related ArticlesDirect 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 skin, bone, and connective tissues. The role of AAAs is very crucial and has been debated. We present here experimental results depicting interaction of AAAs with imino acids in a native collagen protein sample. The interaction is probed by solid-state NMR (ssNMR) spectroscopy experiments such as (1)H-(13)C heteronuclear correlation (HETCOR) performed on a native collagen sample. The natural abundance (13)C spectrum was obtained by dynamic nuclear polarization (DNP) sensitivity enhancement coupled with ssNMR, providing ~30-fold signal enhancement. Our results also open up new avenues of probing collagen structure/dynamics closest to the native state by ssNMR experiments coupled with DNP.
Visualizing Specific Cross-Protomer Interactions in the Homo-Oligomeric Membrane Protein Proteorhodopsin by Dynamic-Nuclear-Polarization-Enhanced Solid-State NMR
Visualizing Specific Cross-Protomer Interactions in the Homo-Oligomeric Membrane Protein Proteorhodopsin by Dynamic-Nuclear-Polarization-Enhanced Solid-State NMR
Jakob Maciejko, Michaela Mehler, Jagdeep Kaur, Tobias Lieblein, Nina Morgner, Olivier Ouari, Paul Tordo, Johanna Becker-Baldus and Clemens Glaubitz
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.5b03606/20150713/images/medium/ja-2015-03606j_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.5b03606
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[NMR paper] Visualizing specific Cross-Protomer Interactions in the Homo-Oligomeric Membrane Protein Proteorhodopsin by DNP-enhanced Solid-state NMR.
Visualizing specific Cross-Protomer Interactions in the Homo-Oligomeric Membrane Protein Proteorhodopsin by DNP-enhanced Solid-state NMR.
Visualizing specific Cross-Protomer Interactions in the Homo-Oligomeric Membrane Protein Proteorhodopsin by DNP-enhanced Solid-state NMR.
J Am Chem Soc. 2015 Jun 23;
Authors: Maciejko J, Mehler M, Kaur J, Lieblein T, Morgner N, Ouari O, Tordo P, Becker-Baldus J, Glaubitz C
Abstract
Membrane proteins often form oligomeric complexes within the lipid bilayer but factors controlling their assembly...
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Direct Evidence of Imino Acid–Aromatic Interactions in Native Collagen Protein by DNP-Enhanced Solid-State NMR Spectroscopy
From The DNP-NMR Blog:
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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[NMR paper] Solid-state NMR study reveals Collagen I structural modifications of amino-acid side chains upon fibrillogenesis.
Solid-state NMR study reveals Collagen I structural modifications of amino-acid side chains upon fibrillogenesis.
Related Articles Solid-state NMR study reveals Collagen I structural modifications of amino-acid side chains upon fibrillogenesis.
J Biol Chem. 2013 Jan 22;
Authors: De Sa Peixoto P, Laurent G, Azais T, Mosser G
Abstract
In vivo, collagen I, the major structural protein in human body, is found assembled into fibrils. In the present work, we study a high concentrated collagen sample in its soluble, fibrillar and denatured states...
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[NMR paper] Direct evidence for a two-state protein unfolding transition from hydrogen-deuterium
Direct evidence for a two-state protein unfolding transition from hydrogen-deuterium exchange, mass spectrometry, and NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Direct evidence for a two-state protein unfolding transition from hydrogen-deuterium exchange, mass spectrometry, and NMR.
Protein Sci. 1996 Jun;5(6):1060-6
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[NMR paper] Imino proton exchange provides an 1H-NMR footprint of protein-DNA interactions: gener
Imino proton exchange provides an 1H-NMR footprint of protein-DNA interactions: general strategy and application to the SRY HMG box.
Related Articles Imino proton exchange provides an 1H-NMR footprint of protein-DNA interactions: general strategy and application to the SRY HMG box.
J Biomol Struct Dyn. 1995 Oct;13(2):261-8
Authors: Weiss MA, King CY
A novel 1H nuclear magnetic resonance (NMR) strategy for "footprinting" specific protein-DNA target sites is demonstrated. Relative rates of site-specifc imino-proton exchange in the free and bound...
Direct Evidence of Imino Acid-Aromatic Interactions in Native Collagen Protein by DNP-Enhanced Solid-State NMR Spectroscopy.
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