Abstract
An ultra-high-resolution NMR experiment for the measurement of intraresidue (1)H(i)-(15)N(i)-(13)C'(i) dipolar-chemical shift anisotropy relaxation interference is employed to extract information about local backbone geometries in intrinsically disordered proteins. The study of tumor suppressor BASP1 revealed a population shift of β-turn geometries at low pH conditions and a compaction of the BASP1 structural ensemble.
Highlights
Proteins that lack stable tertiary structures are attracting growing interest because of their involvement in fundamental biological processes.[1]
Intraresidue 1H(i)–15N(i)–13C’(i) dipolar–CSA interference was proposed to determine the orientation of the 1H(i)–15N(i) dipole vector in the principal frame of the intraresidue 13C’(i) CSA tensor and discriminate between type I and type II b turns in proteins.[10]
Applications of multidimensional NMR spectroscopy to intrinsically disordered proteins (IDPs) are challenging because of the limited signal dispersion owing to the lack of stably formed tertiary structures
Summary
Proteins that lack stable tertiary structures are attracting growing interest because of their involvement in fundamental biological processes.[1]. Cross-correlated NMR relaxation (CCR) has attracted considerable interest in the past as it offers unique possibilities to probe structural dynamics in proteins.[9] The method is based on correlated fluctuations of relaxation relevant interaction tensors (for example, dipole–dipole interactions, chemical shift anisotropy (CSA), and quadrupolar interactions).
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