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期刊名:Journal of biomolecular nmr

缩写:J BIOMOL NMR

ISSN:0925-2738

e-ISSN:1573-5001

IF/分区:2.1/Q2

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共收录本刊相关文章索引1194条
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Belén Chaves-Arquero,David Pantoja-Uceda,Alicia Roque et al. Belén Chaves-Arquero et al.
The C-terminal domain of histone H1.0 (C-H1.0) is involved in DNA binding and is a main determinant of the chromatin condensing properties of histone H1.0. Phosphorylation at the (S/T)-P-X-(K/R) motifs affects DNA binding and is crucial for...
Azzurra Carlon,Enrico Ravera,Giacomo Parigi et al. Azzurra Carlon et al.
Data integration in structural biology has become a paradigm for the characterization of biomolecular systems, and it is now accepted that combining different techniques can fill the gaps in each other's blind spots. In this frame, one of t...
Pratibha Kumari,Lukas Frey,Alexander Sobol et al. Pratibha Kumari et al.
15N R2 relaxation measurements are key for the elucidation of the dynamics of both folded and intrinsically disordered proteins (IDPs). Here we show, on the example of the intrinsically disordered protein α-synuclein and the folded domain ...
Anusha B Gopalan,Tairan Yuwen,Lewis E Kay et al. Anusha B Gopalan et al.
Protein conformational changes play crucial roles in enabling function. The Carr-Purcell-Meiboom-Gill (CPMG) experiment forms the basis for studying such dynamics when they involve the interconversion between highly populated and sparsely f...
Heiner N Raum,Matthias Dreydoppel,Ulrich Weininger Heiner N Raum
Aromatic side chains are attractive probes of protein dynamics on the millisecond time scale, because they are often key residues in enzyme active sites and protein binding sites. Further they allow to study specific processes, like histidi...
Alons Lends,Francesco Ravotti,Giorgia Zandomeneghi et al. Alons Lends et al.
The assignment of protein backbone and side-chain NMR chemical shifts is the first step towards the characterization of protein structure. The recent introduction of proton detection in combination with fast MAS has opened up novel opportun...
Michal Rivlin,Gil Navon Michal Rivlin
3-O-Methyl-D-glucose (3OMG) was recently suggested as an agent to image tumors using chemical exchange saturation transfer (CEST) MRI. To characterize the properties of 3OMG in solution, the anomeric equilibrium and the mutarotation rates o...
Tom Aharoni,Amir Goldbourt Tom Aharoni
Determination of chemical shift anisotropy (CSA) in immobilized proteins and protein assemblies is one of several tools to determine protein dynamics on the timescales of microseconds and faster. The large CSA values of C=O groups in the ri...
Liliya Vugmeyster,Aaron Griffin,Dmitry Ostrovsky et al. Liliya Vugmeyster et al.
We investigated correlated µs-ms time scale motions of neighboring 13C'-15N and 13Cα-13Cβ nuclei in both protonated and perdeuterated samples of GB3. The techniques employed, NMR relaxation due to cross-correlated chemical shift modulati...
Lindsay Clark,Igor Dikiy,Daniel M Rosenbaum et al. Lindsay Clark et al.
NMR studies of human integral membrane proteins provide unique opportunities to probe structure and dynamics at specific locations and on multiple timescales, often with significant implications for disease mechanism and drug development. S...