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@article{1408290,
author = {Srb, Pavel and Nováček, Jiří and Kadeřávek, Pavel and Rabatinova, A. and Krásný, L. and Žídková, J. and Bobáľová, J. and Sklenář, Vladimír and Žídek, Lukáš},
article_location = {Dordrecht},
article_number = {3},
doi = {http://dx.doi.org/10.1007/s10858-017-0138-1},
keywords = {Nuclear magnetic resonance; Relaxation; Non-uniform sampling; Intrinsically disordered proteins},
language = {eng},
issn = {0925-2738},
journal = {Journal of Biomolecular NMR},
title = {Triple resonance NMR relaxation experiments for studies of intrinsically disordered proteins},
url = {https://link.springer.com/article/10.1007%2Fs10858-017-0138-1},
volume = {69},
year = {2017}
}
TY - JOUR
ID - 1408290
AU - Srb, Pavel - Nováček, Jiří - Kadeřávek, Pavel - Rabatinova, A. - Krásný, L. - Žídková, J. - Bobáľová, J. - Sklenář, Vladimír - Žídek, Lukáš
PY - 2017
TI - Triple resonance NMR relaxation experiments for studies of intrinsically disordered proteins
JF - Journal of Biomolecular NMR
VL - 69
IS - 3
SP - 133-146
EP - 133-146
PB - Springer
SN - 09252738
KW - Nuclear magnetic resonance
KW - Relaxation
KW - Non-uniform sampling
KW - Intrinsically disordered proteins
UR - https://link.springer.com/article/10.1007%2Fs10858-017-0138-1
N2 - Description of protein dynamics is known to be essential in understanding their function. Studies based on a well established NMR relaxation methodology have been applied to a large number of systems. However, the low dispersion of chemical shifts very often observed within intrinsically disordered proteins complicates utilization of standard 2D HN correlated spectra because a limited number of amino acids can be characterized. Here we present a suite of triple resonance HNCO-type NMR experiments for measurements of five relaxation parameters (, , NOE, cross-correlated relaxation rates and ) in doubly ,-labeled proteins. We show that the third spectral dimension combined with non-uniform sampling provides relaxation rates for almost all residues of a protein with extremely poor chemical shift dispersion, the C terminal domain of -subunit of RNA polymerase from Bacillus subtilis. Comparison with data obtained using a sample labeled by only showed that the presence of has a negligible effect on , , and on the cross-relaxation rate (calculated from NOE and ), and that these relaxation rates can be used to calculate accurate spectral density values. Partially -labeled sample was used to test if the observed increase of in the presence of corresponds to the dipole-dipole interactions in the ,-labeled sample.
ER -
SRB, Pavel, Jiří NOVÁČEK, Pavel KADEŘÁVEK, A. RABATINOVA, L. KRÁSNÝ, J. ŽÍDKOVÁ, J. BOBÁĽOVÁ, Vladimír SKLENÁŘ and Lukáš ŽÍDEK. Triple resonance NMR relaxation experiments for studies of intrinsically disordered proteins. \textit{Journal of Biomolecular NMR}. Dordrecht: Springer, 2017, vol.~69, No~3, p.~133-146. ISSN~0925-2738. Available from: https://dx.doi.org/10.1007/s10858-017-0138-1.
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