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Medientyp:
E-Artikel
Titel:
High resolution NMR study of T1 magnetic relaxation dispersion. IV. Proton relaxation in amino acids and Met-enkephalin pentapeptide
Beteiligte:
Pravdivtsev, Andrey N.;
Yurkovskaya, Alexandra V.;
Vieth, Hans-Martin;
Ivanov, Konstantin L.
Erschienen:
AIP Publishing, 2014
Erschienen in:The Journal of Chemical Physics
Sprache:
Englisch
DOI:
10.1063/1.4897336
ISSN:
0021-9606;
1089-7690
Entstehung:
Anmerkungen:
Beschreibung:
<jats:p>Nuclear Magnetic Relaxation Dispersion (NMRD) of protons was studied in the pentapeptide Met-enkephalin and the amino acids, which constitute it. Experiments were run by using high-resolution Nuclear Magnetic Resonance (NMR) in combination with fast field-cycling, thus enabling measuring NMRD curves for all individual protons. As in earlier works, Papers I–III, pronounced effects of intramolecular scalar spin-spin interactions, J-couplings, on spin relaxation were found. Notably, at low fields J-couplings tend to equalize the apparent relaxation rates within networks of coupled protons. In Met-enkephalin, in contrast to the free amino acids, there is a sharp increase in the proton T1-relaxation times at high fields due to the changes in the regime of molecular motion. The experimental data are in good agreement with theory. From modelling the relaxation experiments we were able to determine motional correlation times of different residues in Met-enkephalin with atomic resolution. This allows us to draw conclusions about preferential conformation of the pentapeptide in solution, which is also in agreement with data from two-dimensional NMR experiments (rotating frame Overhauser effect spectroscopy). Altogether, our study demonstrates that high-resolution NMR studies of magnetic field-dependent relaxation allow one to probe molecular mobility in biomolecules with atomic resolution.</jats:p>