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.
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 1H?13C heteronuclear correlation (HETCOR) performed on a native collagen sample. The natural abundance 13C 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.
[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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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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12-12-2013 11:39 PM
[NMR paper] Water scaffolding in collagen: Implications on protein dynamics as revealed by solid-state NMR.
Water scaffolding in collagen: Implications on protein dynamics as revealed by solid-state NMR.
Water scaffolding in collagen: Implications on protein dynamics as revealed by solid-state NMR.
Biopolymers. 2013 Jun 19;
Authors: Aliev AE, Courtier-Murias D
Abstract
Solid-state NMR studies of collagen samples of various origin confirm that the amplitude of collagen backbone and sidechain motions increases significantly on increasing the water content. This conclusion is supported by the changes observed in three different NMR...
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06-21-2013 01:10 PM
[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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02-03-2013 10:19 AM
Direct detection of nitrogen-14 in solid-state NMR spectroscopy
Direct detection of nitrogen-14 in solid-state NMR spectroscopy
November 2011
Publication year: 2011
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 59, Issue 4</br>
</br>
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Direct detection of nitrogen-14 in solid-state NMR spectroscopy
Direct detection of nitrogen-14 in solid-state NMR spectroscopy
November 2011
Publication year: 2011
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 59, Issue 4</br>
</br>
Highlights
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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
Linear Mode
