Stretching the chains: the destabilizing impact of Cu(2+) and Zn(2+) ions on K48-linked diubiquitin.

Mangini V, Grasso G, Belviso BD, Sciacca MFM, Lanza V, Caliandro R, Milardi D
Dalton Trans (2023 Aug 15)
PMID: 37581921
doi: 10.1039/d3dt01815f
Submitted to SASBDB: 2023 May 2
Published in SASBDB:

SASDSF2 – K48-linked diubiquitin

Polyubiquitin-C experimental SAS data
OTHER model
Sample: Polyubiquitin-C monomer, 17 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 100 mM NaCl, pH: 7
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Feb 1
RgGuinier 1.9 nm
Dmax 6.5 nm
VolumePorod 22 nm3

SASDSG2 – K48-linked diubiquitin in the presence of zinc ion

Polyubiquitin-C experimental SAS data
Sample: Polyubiquitin-C monomer, 17 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 100 mM NaCl, pH: 7
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Feb 1
RgGuinier 2.0 nm
Dmax 7.5 nm
VolumePorod 20 nm3

SASDSH2 – K48-linked diubiquitin in the presence of copper (II) ion

Polyubiquitin-C experimental SAS data
Sample: Polyubiquitin-C monomer, 17 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 100 mM NaCl, pH: 7
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Feb 1
RgGuinier 1.9 nm
Dmax 6.3 nm
VolumePorod 20 nm3