Backbone and sidechain NMR assignments of residues 1–81 from yeast Sis1 in complex with an Hsp70 C-terminal EEVD peptide-Reference-Cited by-同舟云学术

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Backbone and sidechain NMR assignments of residues 1–81 from yeast Sis1 in complex with an Hsp70 C-terminal EEVD peptide

Published:2023-08-17 Issue:2 Volume:17 Page:239-242
ISSN:1874-2718
Container-title:Biomolecular NMR Assignments
language:en
Short-container-title:Biomol NMR Assign

Author:

Matos Carolina O.,Pinheiro Glaucia M.S.,Ramos Carlos H. I.,Almeida Fabio C. L.

Funder

Fundação de Amparo à Pesquisa do Estado de São Paulo

Conselho Nacional de Desenvolvimento Científico e Tecnológico

Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro

Publisher

Springer Science and Business Media LLC

Subject

Biochemistry,Structural Biology

Link

https://link.springer.com/content/pdf/10.1007/s12104-023-10148-0.pdf

Reference23 articles.

1. Berjanskii Mv, Wishart DS (2005) A simple method to predict protein flexibility using secondary Chemical Shifts. J Am Chem Soc 127(43):14970–14971. https://doi.org/10.1021/ja054842f

2. Borges JC, Seraphim Tv, Mokry DZ, Almeida FCL, Cyr DM, Ramos CHI (2012) Identification of regions involved in substrate binding and Dimer stabilization within the central domains of yeast Hsp40 Sis1. PLoS ONE 7(12):1–15. https://doi.org/10.1371/journal.pone.0050927

3. Delaglio F, Grzesiek S, Vuister GeertenW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6(3). https://doi.org/10.1007/BF00197809

4. Freeman BC, Myers MP, Schumacher R, Morimoto RI (1995) Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. EMBO J 14(10):2281–2292

5. Gal M, Edmonds KA, Milbradt AG, Takeuchi K, Wagner G (2011) Speeding up direct 15 N detection: hCaN 2D NMR experiment. J Biomol NMR 51(4):497–504. https://doi.org/10.1007/s10858-011-9580-7

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