A suite of amino acid residue type classification pulse sequences for 13C-detected NMR of proteins

Pantoja-Uceda, David; Santoro, Jorge

doi:10.1016/j.jmr.2013.06.023

Cited by 7 publications

(3 citation statements)

References 45 publications

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“…A second approach, based on the CBCACO sequence, proposed the use of a selection method based on the 13 C β topology to distinguish the different amino acid types. 83 From a single experiment recorded with a sequence that includes several selective pulses cleverly chosen, it is possible to generate subspectra in which the residue signals can be grouped in six classes according to their topology. The classification is coarse but useful for specific purposes.…”

Section: Sequence-specific Assignmentmentioning

confidence: 99%

¹³C Direct Detected NMR for Challenging Systems

Felli

Pierattelli

2022

Chem. Rev.

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Thanks to recent improvements in NMR spectrometer hardware and pulse sequence design, modern 13 C NMR has become a useful tool for biomolecular applications. The complete assignment of a protein can be accomplished by using 13 C detected multinuclear experiments and it can provide unique information relevant for the study of a variety of different biomolecules including paramagnetic proteins and intrinsically disordered proteins. A wide range of NMR observables can be measured, concurring to the structural and dynamic characterization of a protein in isolation, as part of a larger complex, or even inside a living cell. We present the different properties of 13 C with respect to 1 H, which provide the rationale for the experiments developed and their application, the technical aspects that need to be faced, and the many experimental variants designed to address different cases. Application areas where these experiments successfully complement proton NMR are also described.

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Section: Sequence-specific Assignmentmentioning

confidence: 99%

¹³C Direct Detected NMR for Challenging Systems

Felli

Pierattelli

2022

Chem. Rev.

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“…4). We envision new amino acid typeselective schemes 40,41 in ssNMR based on rotational resonance at few spinning rates could be established to complement common assignment pulse sequences. Such experiments would remove ambiguity or eliminate the need for selective labeling procedures for large protein systems.…”

Section: Effects In Common and Emerging Measurementsmentioning

confidence: 99%

Magic angle spinning effects on longitudinal NMR relaxation: 15N in L-histidine

Afrough,

Christensen,

Jensen

et al. 2023

AIP Advances

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Solid-state magnetic resonance is a unique technique that can reveal the dynamics of complex biological systems with atomic resolution. Longitudinal relaxation is a mechanism that returns longitudinal nuclear magnetization to its thermal equilibrium by incoherent processes. The measured longitudinal relaxation rate constant however represents the combination of both incoherent and coherent contributions to the change of nuclear magnetization. This work demonstrates the effect of magic angle spinning rate on the longitudinal relaxation rate constant in two model compounds: L-histidine hydrochloride monohydrate and glycine serving as proxies for isotopically-enriched biological materials. Most notably, it is demonstrated that the longitudinal N15 relaxation of the two nitrogen nuclei in the imidazole ring in histidine is reduced by almost three orders of magnitude at the condition of rotational resonance with the amine, while the amine relaxation rate constant is increased at these conditions. The observed phenomenon may have radical implications for the solid-state magnetic resonance in biophysics and materials, especially in the proper measurement of dynamics and as a selective serial transfer step in dynamic nuclear polarization.

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“…In a paper published in the Journal of Magnetic Resonance, these authors introduced a collection of pulse sequences to classify CACO and CON spectra by amino acid residue type. 58 In the Journal of Biomolecular NMR, Pantoja-Uceda and Santoro proposed a pair of 3D correlation experiments that use the 3D hNcocaNCO and hnCOcaNCO spectra in combination with the 2D CON spectrum and demonstrate this method on Nupr1, a 93 residue IDP. 59 …”

Section: Experimental Approaches In Idp/idpr Analysismentioning

confidence: 99%

Digested disorder

Reddy

DeForte

Uversky

2014

Intrinsically Disordered Proteins

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The current literature on intrinsically disordered proteins grows fast. To keep interested readers up to speed with this literature, we continue a “Digested Disorder” project and represent a new issue of reader’s digest of the research papers and reviews on intrinsically disordered proteins. The only 2 criteria for inclusion in this digest are the publication date (a paper should be published within the covered time frame) and topic (a paper should be dedicated to any aspect of protein intrinsic disorder). The current digest issue covers papers published during the third quarter of 2013; i.e., during the period of June, July, and September of 2013. Similar to previous issues, the papers are grouped hierarchically by topics they cover, and for each of the included paper a short description is given on its major findings.

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A suite of amino acid residue type classification pulse sequences for 13C-detected NMR of proteins

Cited by 7 publications

References 45 publications

¹³C Direct Detected NMR for Challenging Systems

¹³C Direct Detected NMR for Challenging Systems

Magic angle spinning effects on longitudinal NMR relaxation: 15N in L-histidine

Digested disorder

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A suite of amino acid residue type classification pulse sequences for 13C-detected NMR of proteins

Cited by 7 publications

References 45 publications

13C Direct Detected NMR for Challenging Systems

13C Direct Detected NMR for Challenging Systems

Magic angle spinning effects on longitudinal NMR relaxation: 15N in L-histidine

Digested disorder

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Product

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¹³C Direct Detected NMR for Challenging Systems

¹³C Direct Detected NMR for Challenging Systems