Structural plasticity and thermal stability of the histone-like protein from Spiroplasma melliferum are due to phenylalanine insertions into the conservative scaffold-Reference-Cited by-同舟云学术

Structural plasticity and thermal stability of the histone-like protein from Spiroplasma melliferum are due to phenylalanine insertions into the conservative scaffold

Published:2018-01-07 Issue:16 Volume:36 Page:4392-4404
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Timofeev Vladimir I.¹²,Altukhov Dmitry A.¹,Talyzina Anna A.³,Agapova Yulia K.¹,Vlaskina Anna V.¹,Korzhenevskiy Dmitry A.¹,Kleymenov Sergey Yu.⁴⁵,Bocharov Eduard V.¹⁶,Rakitina Tatiana V.¹⁶^ORCID

Affiliation:

1. National Research Centre ‘Kurchatov Institute’, Kurchatov Complex of NBICS-Technologies, Akad. Kurchatova sqr., 1, Moscow 123182, Russian Federation

2. Federal Scientific Research Center ‘Crystallography and Photonics’ RAS, Leninskii pr., 59, Moscow 119333, Russian Federation

3. Moscow Institute of Physics and Technology, Institutskiy per., 9, Dolgoprudny, Moscow Region 141700, Russian Federation

4. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Leninsky Prospekt. 33, bld. 2, Moscow 119071, Russian Federation

5. Russian Academy of Sciences, Koltzov Institute of Developmental Biology, ul. Vavilova, 26, Moscow 119334, Russian Federation

6. Shemyakin&Ovchinnikov Institute of Bioorganic Chemistry RAS, str. Miklukho-Maklaya 16/10, Moscow 117997, Russian Federation

Funder

Russian Science Foundation

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/07391102.2017.1417162

Reference46 articles.

1. Preparation of the recombinant НU-proteins from S. melliferum and M. gallisepticum and of their complexes with DS-DNA for structural NMR experiments