Site-specific modification and segmental isotope labelling of HMGN1 reveals long-range conformational perturbations caused by posttranslational modifications-Reference-Cited by-同舟云学术

Site-specific modification and segmental isotope labelling of HMGN1 reveals long-range conformational perturbations caused by posttranslational modifications

Published:2021 Issue:2 Volume:2 Page:537-550
ISSN:2633-0679
Container-title:RSC Chemical Biology
language:en
Short-container-title:RSC Chem. Biol.

Author:

Niederacher Gerhard¹²³⁴⁵,Urwin Debra⁶⁷⁸⁹^ORCID,Dijkwel Yasmin⁶⁷⁸⁹^ORCID,Tremethick David J.⁶⁷⁸⁹^ORCID,Rosengren K. Johan¹⁰¹¹¹²⁹^ORCID,Becker Christian F. W.¹²³⁴⁵^ORCID,Conibear Anne C.¹⁰¹¹¹²⁹^ORCID

Affiliation:

1. Faculty of Chemistry

2. Institute of Biological Chemistry

3. University of Vienna

4. 1090 Vienna

5. Austria

6. John Curtin School of Medical Research

7. Department of Genome Sciences

8. The Australian National University

9. Australia

10. School of Biomedical Sciences

11. The University of Queensland

12. Brisbane

Abstract

Using protein semi-synthesis, segmentally isotope-labelled variants of nucleosome-binding protein HMGN1 were generated with site-specific posttranslational modifications to explore their structural and functional effects.

Funder

Vienna Science and Technology Fund

University of Queensland

Publisher

Royal Society of Chemistry (RSC)

Subject

Biochemistry, Genetics and Molecular Biology (miscellaneous),Molecular Biology,Biochemistry,Chemistry (miscellaneous)

Link

http://pubs.rsc.org/en/content/articlepdf/2021/CB/D0CB00175A

Reference68 articles.

1. New insights into nucleosome and chromatin structure: an ordered state or a disordered affair?

2. Nucleosome structure and dynamics are coming of age