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1.
J Chem Phys ; 141(5): 054203, 2014 Aug 07.
Artigo em Inglês | MEDLINE | ID: mdl-25106580

RESUMO

Long-lived coherences (LLC's) are detectable magnetisation modes with favourable relaxation times that translate as sharp resonances upon Fourier transform. The frequency domain of LLC's was previously limited to the range of J-couplings within pairs of homonuclear spins. LLC evolution at high magnetic fields needs to be sustained by radio-frequency irradiation. We show that LLC-based spectral dispersion can be extended beyond the J-couplings domain using adapted carrier offsets and introduce a new reduced-power sustaining method to preserve LLC's within the required range of offsets. Spectral resolution is enhanced as the natively narrow lines of LLC's are further dispersed, making them potential probes for the study of biomolecules featuring strong resonance overlap and for media where NMR spectroscopy is commonly hindered by line broadening.


Assuntos
Algoritmos , Dipeptídeos/química , Dipeptídeos/efeitos da radiação , Espectroscopia de Prótons por Ressonância Magnética/métodos , Ubiquitina/química , Ubiquitina/efeitos da radiação , Fótons
2.
Magn Reson Chem ; 51(11): 729-33, 2013 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-25941036

RESUMO

Long-lived states (LLS) are relaxation-favored spin population distributions of J-coupled magnetic nuclei. LLS were measured, along with classical (1)H and (15)N relaxation rate constants, in amino acids of the N-terminal Unique domain of the c-Src kinase, which is disordered in vitro under physiological conditions. The relaxation rates of LLS can probe motions and interactions in biomolecules. LLS of the aliphatic protons of glycines, with lifetimes approximately four times longer than their spin-lattice relaxation times, are reported for the first time in an intrinsically disordered protein domain. LLS relaxation experiments were integrated with 2D spectroscopy methods, further adapting them for studies on proteins.


Assuntos
Glicina/química , Proteínas Intrinsicamente Desordenadas/química , Prótons , Quinases da Família src/química , Proteína Tirosina Quinase CSK , Humanos , Isótopos de Nitrogênio , Ressonância Magnética Nuclear Biomolecular , Estrutura Terciária de Proteína , Fatores de Tempo
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