Triple resonance NMR relaxation experiments for studies of intrinsically disordered proteins

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F17%3A00095497" target="_blank" >RIV/00216224:14740/17:00095497 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.1007/s10858-017-0138-1" target="_blank" >http://dx.doi.org/10.1007/s10858-017-0138-1</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s10858-017-0138-1" target="_blank" >10.1007/s10858-017-0138-1</a>

Result language

angličtina

Original language name

Triple resonance NMR relaxation experiments for studies of intrinsically disordered proteins

Original language description

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.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2017

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Biomolecular NMR

ISSN

0925-2738

e-ISSN

—

Volume of the periodical

69

Issue of the periodical within the volume

3

Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

14

Pages from-to

133-146

UT code for WoS article

000416856600003

EID of the result in the Scopus database

—