Temperature-Induced Misfolding in Prion Protein: Evidenceof Multiple Partially Disordered States Stabilized by Non-Native HydrogenBonds
Temperature-Induced Misfolding in Prion Protein: Evidenceof Multiple Partially Disordered States Stabilized by Non-Native HydrogenBonds
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b01042/20170202/images/medium/bi-2016-01042c_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b01042
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/U_hltRN32V8
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02-03-2017 05:43 AM
[NMR paper] Determination of Structure and Micellar Interactions of Small Antimicrobial Peptides by Solution-State NMR.
Determination of Structure and Micellar Interactions of Small Antimicrobial Peptides by Solution-State NMR.
Related Articles Determination of Structure and Micellar Interactions of Small Antimicrobial Peptides by Solution-State NMR.
Methods Mol Biol. 2017;1548:73-88
Authors: Wimmer R, Uggerhøj LE
Abstract
NMR spectroscopy is a well-established technique to determine the structure of peptides and small proteins in solution, also when bound to detergent micelles or phospholipid bicelles. The structure of the peptide alone is,...
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12-26-2016 12:50 PM
Site-specific tagging proteins with a rigid, small and stable transition metal chelator, 8-hydroxyquinoline, for paramagnetic NMR analysis
Site-specific tagging proteins with a rigid, small and stable transition metal chelator, 8-hydroxyquinoline, for paramagnetic NMR analysis
Abstract
Design of a paramagnetic metal binding motif in a protein is a valuable way for understanding the function, dynamics and interactions of a protein by paramagnetic NMR spectroscopy. Several strategies have been proposed to site-specifically tag proteins with paramagnetic lanthanide ions. Here we report a simple approach of engineering a transition metal binding motif via site-specific labelling of a...
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01-06-2016 09:48 AM
[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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08-16-2015 07:01 PM
[NMR paper] Protein structural studies by paramagnetic solid-state NMR spectroscopy aided by a compact cyclen-type Cu(II) binding tag.
Protein structural studies by paramagnetic solid-state NMR spectroscopy aided by a compact cyclen-type Cu(II) binding tag.
Protein structural studies by paramagnetic solid-state NMR spectroscopy aided by a compact cyclen-type Cu(II) binding tag.
J Biomol NMR. 2014 Nov 29;
Authors: Sengupta I, Gao M, Arachchige RJ, Nadaud PS, Cunningham TF, Saxena S, Schwieters CD, Jaroniec CP
Abstract
Paramagnetic relaxation enhancements (PREs) are a rich source of structural information in protein solid-state NMR spectroscopy. Here we...
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11-30-2014 09:41 PM
Protein structural studies by paramagnetic solid-state NMR spectroscopy aided by a compact cyclen-type Cu(II) binding tag
Protein structural studies by paramagnetic solid-state NMR spectroscopy aided by a compact cyclen-type Cu(II) binding tag
Abstract
Paramagnetic relaxation enhancements (PREs) are a rich source of structural information in protein solid-state NMR spectroscopy. Here we demonstrate that PRE measurements in natively diamagnetic proteins are facilitated by a thiol-reactive compact, cyclen-based, high-affinity Cu2+ binding tag, 1--1,4,7,10-tetraazacyclododecane (TETAC), that overcomes the key shortcomings associated with the use of larger, more flexible...
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11-29-2014 12:09 AM
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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11-24-2014 04:15 PM
[NMR paper] Screening protein-small molecule interactions by NMR.
Screening protein-small molecule interactions by NMR.
Related Articles Screening protein-small molecule interactions by NMR.
Methods Mol Biol. 2013;1008:389-413
Authors: Davis B
Abstract
Nuclear magnetic resonance (NMR) is well suited to probing the interactions between ligands and macromolecular receptors. It is a truly label-free technique, requiring only the presence of atoms (usually (1)H or (19)F) which give rise to observable resonances on either the ligand or the receptor. A number of parameters associated with these resonances can...
A Dry Transition State More Compact Than the NativeState Is Stabilized by Non-Native Interactions during the Unfoldingof a Small Protein
Linear Mode
