[NMR paper] Longitudinal Spin Order Labeling on Multiple Quantum Coherences Enables NMR Analysis of Intrinsically Disordered Proteins at Ultrahigh Resolution
Longitudinal Spin Order Labeling on Multiple Quantum Coherences Enables NMR Analysis of Intrinsically Disordered Proteins at Ultrahigh Resolution
Intrinsically disordered proteins (IDPs) play an important role in cell signaling, and NMR is well-suited to study conformational ensembles and dynamics of IDPs. However, the intrinsic flexibility of IDPs often results in severe spectral overlap, which hampers accurate NMR data analysis. By labeling the longitudinal spin order of an ? proton (i.e., H^(?)(z)) on multiple quantum coherences of backbone nuclei (e.g., N(y)C'(x)C^(?)(y)), we were able...
[NMR paper] Interpretation of seemingly contradictory data: low NMR S2 order parameters observed in helices and high NMR S2 order parameters in disordered loops of the protein hGH at low pH.
Interpretation of seemingly contradictory data: low NMR S2 order parameters observed in helices and high NMR S2 order parameters in disordered loops of the protein hGH at low pH.
Related Articles Interpretation of seemingly contradictory data: low NMR S2 order parameters observed in helices and high NMR S2 order parameters in disordered loops of the protein hGH at low pH.
Chemistry. 2017 May 15;:
Authors: Smith LJ, Athill R, van Gunsteren WF, Hansen N
Abstract
At low pH human growth hormone (hGH) adopts a partially folded state...
Bringing research on disordered proteins to order - Mirage News
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