Rotamer Jumps, Proton Exchange, and Amine Inversion Dynamics of Dimethylated Lysine Residues in Proteins Resolved by pH-Dependent 1H and 13C NMR Relaxation Dispersion-Reference-Cited by-同舟云学术

Rotamer Jumps, Proton Exchange, and Amine Inversion Dynamics of Dimethylated Lysine Residues in Proteins Resolved by pH-Dependent 1H and 13C NMR Relaxation Dispersion

Published:2019-10-03 Issue:46 Volume:123 Page:9742-9750
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Weininger Ulrich¹^ORCID,Modig Kristofer¹,Ishida Hiroaki²,Vogel Hans J.²,Akke Mikael¹^ORCID

Affiliation:

1. Biophysical Chemistry, Center for Molecular Protein Science, Department of Chemistry, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden

2. Department of Biological Sciences, Biochemistry Research Group, University of Calgary, 2500 University Drive NW, Calgary, Alberta, T2N 1N4 Canada

Funder

Vetenskapsr?det

G?ran Gustafssons Stiftelse f?r Naturvetenskaplig och Medicinsk Forskning

Natural Sciences and Engineering Research Council of Canada

European Molecular Biology Organization

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

http://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.9b06408

Reference37 articles.

1. Histone methylation: a dynamic mark in health, disease and inheritance

2. Regulation of nucleosome dynamics by histone modifications

3. Chemical and Biochemical Perspectives of Protein Lysine Methylation

4. How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers

5. Chemical Inhibitors of Epigenetic Methyllysine Reader Proteins

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