Why is binding of a divalent metal cation to a structural motif containing four carboxylate residues not accompanied by a conformational change?

Lushchekina S, Weiner L, Ashani Y, Emrizal R, Firdaus-Raih M, Silman I, Sussman JL

Open source

DOI
10.1002/pro.5206
Published
2024 Dec
Container
Protein science : a publication of the Protein Society
Publisher
Not recorded
Open access
yes

Credibility signals

limited evidence Score 45/100 under policy 1.0.0. This is a metadata assessment, not a judgment of the paper's conclusions.

Show all credibility signals

Cite this work

BibTeX

@article{allodium:10.1002/pro.5206,
  title = {Why is binding of a divalent metal cation to a structural motif containing four carboxylate residues not accompanied by a conformational change?},
  author = {Lushchekina S and Weiner L and Ashani Y and Emrizal R and Firdaus-Raih M and Silman I and Sussman JL},
  year = {2024},
  journal = {Protein science : a publication of the Protein Society},
  doi = {10.1002/pro.5206},
  url = {https://doi.org/10.1002/pro.5206}
}

RIS

TY  - JOUR
TI  - Why is binding of a divalent metal cation to a structural motif containing four carboxylate residues not accompanied by a conformational change?
AU  - Lushchekina S
AU  - Weiner L
AU  - Ashani Y
AU  - Emrizal R
AU  - Firdaus-Raih M
AU  - Silman I
AU  - Sussman JL
PY  - 2024
JO  - Protein science : a publication of the Protein Society
DO  - 10.1002/pro.5206
UR  - https://doi.org/10.1002/pro.5206
ER  - 

APA

S, L., L, W., Y, A., R, E., M, F., I, S., & JL, S. (2024). Why is binding of a divalent metal cation to a structural motif containing four carboxylate residues not accompanied by a conformational change?. Protein science : a publication of the Protein Society. https://doi.org/10.1002/pro.5206

Source records