[NMR paper] Identification of Dynamic Modes in an Intrinsically Disordered Protein using Temperature-dependent NMR Relaxation.
Identification of Dynamic Modes in an Intrinsically Disordered Protein using Temperature-dependent NMR Relaxation.
Related Articles Identification of Dynamic Modes in an Intrinsically Disordered Protein using Temperature-dependent NMR Relaxation.
J Am Chem Soc. 2016 Apr 26;
Authors: Abyzov A, Salvi N, Schneider R, Maurin D, Ruigrok RW, Jensen MR, Blackledge M
Abstract
[NMR paper] Partially unfolded forms of the prion protein populated under misfolding-promoting conditions: characterization by hydrogen exchange mass spectrometry and NMR.
Partially unfolded forms of the prion protein populated under misfolding-promoting conditions: characterization by hydrogen exchange mass spectrometry and NMR.
Partially unfolded forms of the prion protein populated under misfolding-promoting conditions: characterization by hydrogen exchange mass spectrometry and NMR.
J Biol Chem. 2015 Aug 25;
Authors: Moulick R, Das R, Udgaonkar JB
Abstract
The susceptibility of the cellular prion protein (PrP(C)) to convert to an alternative misfolded conformation (PrP(Sc)), which is the key...
nmrlearner
Journal club
0
08-26-2015 10:21 AM
[NMR paper] Characterization of the near native conformational states of the SAM domain of Ste11 protein by NMR spectroscopy.
Characterization of the near native conformational states of the SAM domain of Ste11 protein by NMR spectroscopy.
Related Articles Characterization of the near native conformational states of the SAM domain of Ste11 protein by NMR spectroscopy.
Proteins. 2014 Jul 26;
Authors: Gupta S, Bhattacharjya S
Abstract
The sterile alpha motif or SAM domain is one of the most frequently present protein interaction modules with diverse functional attributions. SAM domain of the Ste11 protein of budding yeast plays important roles in...
nmrlearner
Journal club
0
07-30-2014 10:22 AM
Evidenceof Entropy-Driven Bistability through 15N NMR Analysisof a Temperature- and Solvent-Induced, ChiropticalSwitching Polycarbodiimide
Evidenceof Entropy-Driven Bistability through 15N NMR Analysisof a Temperature- and Solvent-Induced, ChiropticalSwitching Polycarbodiimide
James F. Reuther and Bruce M. Novak
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja4098803/aop/images/medium/ja-2013-098803_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja4098803
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/ogd4bIIAgFU
nmrlearner
Journal club
0
12-17-2013 12:56 AM
[NMR paper] Probing early misfolding events in prion protein mutants by NMR spectroscopy.
Probing early misfolding events in prion protein mutants by NMR spectroscopy.
Related Articles Probing early misfolding events in prion protein mutants by NMR spectroscopy.
Molecules. 2013;18(8):9451-76
Authors: Giachin G, Biljan I, Ilc G, Plavec J, Legname G
Abstract
The post-translational conversion of the ubiquitously expressed cellular form of the prion protein, PrPC, into its misfolded and pathogenic isoform, known as prion or PrPSc, plays a key role in prion diseases. These maladies are denoted transmissible spongiform...
nmrlearner
Journal club
0
08-24-2013 04:53 PM
Methods to determine slow diffusion coefficients of biomolecules. Applications to Engrailed 2, a partially disordered protein
Methods to determine slow diffusion coefficients of biomolecules. Applications to Engrailed 2, a partially disordered protein
Abstract We present new NMR methods to measure slow translational diffusion coefficients of biomolecules. Like the heteronuclear stimulated echo experiment (XSTE), these new methods rely on the storage of information about spatial localization during the diffusion delay as longitudinal polarization of nuclei with long T1 such as nitrogen-15. The new BEST-XSTE sequence combines features of Band-selective Excitation Short-Transient (BEST) and XSTE methods. By...
nmrlearner
Journal club
0
05-24-2011 10:00 AM
[NMR paper] Dynamical characterization of residual and non-native structures in a partially folde
Dynamical characterization of residual and non-native structures in a partially folded protein by (15)N NMR relaxation using a model based on a distribution of correlation times.
Related Articles Dynamical characterization of residual and non-native structures in a partially folded protein by (15)N NMR relaxation using a model based on a distribution of correlation times.
Protein Sci. 2002 Apr;11(4):957-64
Authors: Ochsenbein F, Neumann JM, Guittet E, van Heijenoort C
A spectral density model based on a truncated lorentzian distribution of...
Temperature-Induced Misfolding in Prion Protein: Evidenceof Multiple Partially Disordered States Stabilized by Non-Native HydrogenBonds
Linear Mode
