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11 hits found for Iqbal

SASDRS2 – Collagen-like peptide Mannan-binding lectin (MBL) center

Ac-(POG)4-QG-(POG)5-NH2 experimental SAS data
PYMOL model
Sample: Ac-(POG)4-QG-(POG)5-NH2 trimer, 11 kDa synthetic construct protein
Buffer: 20 mM L-histidine, 138 mM NaCl, 2.7 mM KCL,, pH: 6
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Feb 1
A solution structure analysis reveals a bent collagen triple helix in the complement activation recognition molecule mannan-binding lectin. J Biol Chem 299(2):102799 (2023)
Iqbal H, Fung KW, Gor J, Bishop AC, Makhatadze GI, Brodsky B, Perkins SJ
RgGuinier 2.1 nm
Dmax 8.7 nm
VolumePorod 7 nm3

SASDRT2 – Collagen-like peptide Mannan-binding Lectin (MBL) native

Ac-(POG)4-QG-(POG)5-NH2 experimental SAS data
PYMOL model
Sample: Ac-(POG)4-QG-(POG)5-NH2 trimer, 11 kDa synthetic construct protein
Buffer: 20 mM L-histidine, 138 mM NaCl, 2.7 mM KCL,, pH: 6
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Feb 1
A solution structure analysis reveals a bent collagen triple helix in the complement activation recognition molecule mannan-binding lectin. J Biol Chem 299(2):102799 (2023)
Iqbal H, Fung KW, Gor J, Bishop AC, Makhatadze GI, Brodsky B, Perkins SJ
RgGuinier 1.7 nm
Dmax 7.1 nm
VolumePorod 4 nm3

SASDUT2 – Recombinant short complement regulator SCR-17/18H (produced in Pichia pastoris with PNGase F treatment)

Complement factor H experimental SAS data
PYMOL model
Sample: Complement factor H monomer, 17 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 137 mM NaCl, pH: 7.4
Experiment: SAXS data collected at B21, Diamond Light Source on 2020 Jan 20
The SCR-17 and SCR-18 glycans in human complement Factor H enhance its regulatory function. J Biol Chem :107624 (2024)
...Iqbal H, Yu DQ, Gor J, Coker AR, Perkins SJ
RgGuinier 3.1 nm
Dmax 10.5 nm
VolumePorod 46 nm3

SASDRU2 – Collagen-like peptide Mannan-binding lectin (MBL) with EOG sequence

Ac-(POG)5-EOGQGLRG-(POG)3-NH2 experimental SAS data
PYMOL model
Sample: Ac-(POG)5-EOGQGLRG-(POG)3-NH2 trimer, 12 kDa synthetic construct protein
Buffer: 20 mM L-histidine, 138 mM NaCl, 2.7 mM KCL,, pH: 6
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Feb 1
A solution structure analysis reveals a bent collagen triple helix in the complement activation recognition molecule mannan-binding lectin. J Biol Chem 299(2):102799 (2023)
Iqbal H, Fung KW, Gor J, Bishop AC, Makhatadze GI, Brodsky B, Perkins SJ
RgGuinier 2.3 nm
Dmax 10.0 nm
VolumePorod 6 nm3

SASDUU2 – Recombinant short complement regulator SCR-17/18, without glycan (produced in Escherichia coli)

Complement factor H experimental SAS data
PYMOL model
Sample: Complement factor H monomer, 14 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 137 mM NaCl, pH: 7.4
Experiment: SAXS data collected at B21, Diamond Light Source on 2020 Jan 20
The SCR-17 and SCR-18 glycans in human complement Factor H enhance its regulatory function. J Biol Chem :107624 (2024)
...Iqbal H, Yu DQ, Gor J, Coker AR, Perkins SJ
RgGuinier 2.3 nm
Dmax 7.0 nm
VolumePorod 19 nm3

SASDRV2 – Collagen-like peptide Mannan-binding lectin (MBL) 12 triplets

Ac-(POG)5-EPGQGLRG-(POG)5-NH2 experimental SAS data
PYMOL model
Sample: Ac-(POG)5-EPGQGLRG-(POG)5-NH2 trimer, 14 kDa synthetic construct protein
Buffer: 20 mM L-histidine, 138 mM NaCl, 2.7 mM KCL,, pH: 6
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Feb 1
A solution structure analysis reveals a bent collagen triple helix in the complement activation recognition molecule mannan-binding lectin. J Biol Chem 299(2):102799 (2023)
Iqbal H, Fung KW, Gor J, Bishop AC, Makhatadze GI, Brodsky B, Perkins SJ
RgGuinier 2.8 nm
Dmax 12.5 nm
VolumePorod 16 nm3

SASDRW2 – [(Pro-Hyp-Gly)10]3

Ac-(POG)10-NH2 experimental SAS data
PYMOL model
Sample: Ac-(POG)10-NH2 trimer, 12 kDa synthetic construct protein
Buffer: 20 mM L-histidine, 138 mM NaCl, 2.7 mM KCL,, pH: 6
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Feb 1
A solution structure analysis reveals a bent collagen triple helix in the complement activation recognition molecule mannan-binding lectin. J Biol Chem 299(2):102799 (2023)
Iqbal H, Fung KW, Gor J, Bishop AC, Makhatadze GI, Brodsky B, Perkins SJ
RgGuinier 2.2 nm
Dmax 8.5 nm
VolumePorod 7 nm3

SASDRX2 – [(Pro-Hyp-Gly)13]3

Ac-(POG)13-NH2 experimental SAS data
PYMOL model
Sample: Ac-(POG)13-NH2 trimer, 15 kDa synthetic construct protein
Buffer: 20 mM L-histidine, 138 mM NaCl, 2.7 mM KCL,, pH: 6
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Feb 1
A solution structure analysis reveals a bent collagen triple helix in the complement activation recognition molecule mannan-binding lectin. J Biol Chem 299(2):102799 (2023)
Iqbal H, Fung KW, Gor J, Bishop AC, Makhatadze GI, Brodsky B, Perkins SJ
RgGuinier 2.8 nm
Dmax 9.5 nm
VolumePorod 14 nm3

SASDRY2 – [(Pro-Pro-Gly)10]3

[(Pro-Pro-Gly)10]3 experimental SAS data
PYMOL model
Sample: [(Pro-Pro-Gly)10]3 trimer, 8 kDa synthetic construct protein
Buffer: 20 mM L-histidine, 138 mM NaCl, 2.7 mM KCL,, pH: 6
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Feb 1
A solution structure analysis reveals a bent collagen triple helix in the complement activation recognition molecule mannan-binding lectin. J Biol Chem 299(2):102799 (2023)
Iqbal H, Fung KW, Gor J, Bishop AC, Makhatadze GI, Brodsky B, Perkins SJ
RgGuinier 2.3 nm
Dmax 9.7 nm
VolumePorod 9 nm3

SASDRZ2 – [(Pro-Hyp-Gly)4-POA-(Pro-Hyp-Gly)5]3

Ac-(POG)4-POA-(POG)5-NH2 experimental SAS data
PYMOL model
Sample: Ac-(POG)4-POA-(POG)5-NH2 trimer, 12 kDa protein
Buffer: 20 mM L-histidine, 138 mM NaCl, 2.7 mM KCL,, pH: 6
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Feb 1
A solution structure analysis reveals a bent collagen triple helix in the complement activation recognition molecule mannan-binding lectin. J Biol Chem 299(2):102799 (2023)
Iqbal H, Fung KW, Gor J, Bishop AC, Makhatadze GI, Brodsky B, Perkins SJ
RgGuinier 2.3 nm
Dmax 11.0 nm
VolumePorod 10 nm3

SASDR23 – [(POG)3-ITGARGLAG-(POG)4]3

Ac-(POG)3-ITGARGLAG-(POG)4-NH2 experimental SAS data
PYMOL model
Sample: Ac-(POG)3-ITGARGLAG-(POG)4-NH2 trimer, 11 kDa synthetic construct protein
Buffer: 20 mM L-histidine, 138 mM NaCl, 2.7 mM KCL,, pH: 6
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Feb 1
A solution structure analysis reveals a bent collagen triple helix in the complement activation recognition molecule mannan-binding lectin. J Biol Chem 299(2):102799 (2023)
Iqbal H, Fung KW, Gor J, Bishop AC, Makhatadze GI, Brodsky B, Perkins SJ
RgGuinier 2.2 nm
Dmax 10.0 nm
VolumePorod 9 nm3