The mammalian Transient Receptor Potential Vanilloid (TRPV) channels are a family of six tetrameric ion channels localized at the plasma membrane. The group I members of the family, TRPV1 through TRPV4, are heat-activated and exhibit remarkable polymodality. The distal N-termini of group I TRPV channels contain large intrinsically disordered regions (IDRs), ranging from ~ 75 amino acids (TRPV2) to ~ 150 amino acids (TRPV4), the vast majority of which is invisible in the structural models...
[NMR paper] NMR chemical shift assignments of RNA oligonucleotides to expand the RNA chemical shift database
NMR chemical shift assignments of RNA oligonucleotides to expand the RNA chemical shift database
RNAs play myriad functional and regulatory roles in the cell. Despite their significance, three-dimensional structure elucidation of RNA molecules lags significantly behind that of proteins. NMR-based studies are often rate-limited by the assignment of chemical shifts. Automation of the chemical shift assignment process can greatly facilitate structural studies, however, accurate chemical shift predictions rely on a robust and complete chemical shift database for training. We searched the...
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08-28-2021 07:56 AM
[NMR paper] NMR illuminates intrinsic disorder
NMR illuminates intrinsic disorder
Nuclear magnetic resonance (NMR) has long been instrumental in the characterization of intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs). This method continues to offer rich insights into the nature of IDPs in solution, especially in combination with other biophysical methods such as small-angle scattering, single-molecule fluorescence, electron paramagnetic resonance (EPR), and mass spectrometry. Substantial advances have been made in recent years in studies...
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05-06-2021 11:45 PM
Hidden Structural Codes in Protein Intrinsic Disorder
Hidden Structural Codes in Protein Intrinsic Disorder
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00721/20171006/images/medium/bi-2017-00721n_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00721
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/mMCQe_lwg8U
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10-07-2017 11:01 AM
Conformationally selective multidimensional chemical shift ranges in proteins from a PACSY database purged using intrinsic quality criteria
Conformationally selective multidimensional chemical shift ranges in proteins from a PACSY database purged using intrinsic quality criteria
Abstract
We have determined refined multidimensional chemical shift ranges for intra-residue correlations (13Câ??13C, 15Nâ??13C, etc.) in proteins, which can be used to gain type-assignment and/or secondary-structure information from experimental NMR spectra. The chemical-shift ranges are the result of a statistical analysis of the PACSY database of >3000 proteins with 3D structures (1,200,207 13C chemical shifts...
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01-19-2016 07:37 PM
Modulation of allostery by protein intrinsic disorder - Nature.com
Modulation of allostery by protein intrinsic disorder - Nature.com
<img alt="" height="1" width="1" />
Modulation of allostery by protein intrinsic disorder
Nature.com
Previous attempts at measuring dissociation constants (Kd) for E1A complexes with CBP by isothermal titration calorimetry (ITC) and nuclear magnetic resonance (NMR) failed because E1A is highly aggregation-prone. Even at concentrations as low as 10 μM ...
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06-19-2013 08:55 PM
Backbone and Ile-?1, Leu, Val Methyl (1)H, (13)C and (15)N NMR chemical shift assignments for human interferon-stimulated gene 15 protein.
Backbone and Ile-?1, Leu, Val Methyl (1)H, (13)C and (15)N NMR chemical shift assignments for human interferon-stimulated gene 15 protein.
Backbone and Ile-?1, Leu, Val Methyl (1)H, (13)C and (15)N NMR chemical shift assignments for human interferon-stimulated gene 15 protein.
Biomol NMR Assign. 2011 May 5;
Authors: Yin C, Aramini JM, Ma LC, Cort JR, Swapna GV, Krug RM, Montelione GT
Human interferon-stimulated gene 15 protein (ISG15), also called ubiquitin cross-reactive protein (UCRP), is the first identified ubiquitin-like protein containing...
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05-06-2011 12:02 PM
[NMR paper] Chemical shift assignments and folding topology of the Ras-binding domain of human Ra
Chemical shift assignments and folding topology of the Ras-binding domain of human Raf-1 as determined by heteronuclear three-dimensional NMR spectroscopy.
Related Articles Chemical shift assignments and folding topology of the Ras-binding domain of human Raf-1 as determined by heteronuclear three-dimensional NMR spectroscopy.
Biochemistry. 1994 Jun 28;33(25):7745-52
Authors: Emerson SD, Waugh DS, Scheffler JE, Tsao KL, Prinzo KM, Fry DC
Raf-1 is a 74-kDa serine-threonine kinase which serves as the immediate downstream target of Ras in the...
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08-22-2010 03:33 AM
[NMR paper] Chemical shift assignments and folding topology of the Ras-binding domain of human Ra
Chemical shift assignments and folding topology of the Ras-binding domain of human Raf-1 as determined by heteronuclear three-dimensional NMR spectroscopy.
Related Articles Chemical shift assignments and folding topology of the Ras-binding domain of human Raf-1 as determined by heteronuclear three-dimensional NMR spectroscopy.
Biochemistry. 1994 Jun 28;33(25):7745-52
Authors: Emerson SD, Waugh DS, Scheffler JE, Tsao KL, Prinzo KM, Fry DC
Raf-1 is a 74-kDa serine-threonine kinase which serves as the immediate downstream target of Ras in the...