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13 hits found for Blumenthal

SASDH62 – Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2F-DB08

Isoform 3 of Rap guanine nucleotide exchange factor 4 experimental SAS data
Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2F-DB08 Rg histogram
Sample: Isoform 3 of Rap guanine nucleotide exchange factor 4 monomer, 114 kDa Mus musculus protein
Buffer: 150 mM NaCl, 1 mM EDTA, 1 mM DTT, and 10 mM Tris-HCl, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSess, University of Utah on 2008 Aug 7
Mechanism of Epac activation: structural and functional analyses of Epac2 hinge mutants with constitutive and reduced activities. J Biol Chem 284(35):23644-51 (2009)
...Blumenthal DK, Mei FC, White MA, Cheng X
RgGuinier 3.2 nm
Dmax 10.7 nm
VolumePorod 123 nm3

SASDH72 – Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2G-DB08

Isoform 3 of Rap guanine nucleotide exchange factor 4 experimental SAS data
Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2G-DB08 Rg histogram
Sample: Isoform 3 of Rap guanine nucleotide exchange factor 4 monomer, 114 kDa Mus musculus protein
Buffer: 150 mM NaCl, 1 mM EDTA, 1 mM DTT, and 10 mM Tris-HCl, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSess, University of Utah on 2008 Aug 8
Mechanism of Epac activation: structural and functional analyses of Epac2 hinge mutants with constitutive and reduced activities. J Biol Chem 284(35):23644-51 (2009)
...Blumenthal DK, Mei FC, White MA, Cheng X
RgGuinier 3.8 nm
Dmax 12.5 nm
VolumePorod 151 nm3

SASDH82 – Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2W-DB08

Isoform 3 of Rap guanine nucleotide exchange factor 4 experimental SAS data
Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2W-DB08 Rg histogram
Sample: Isoform 3 of Rap guanine nucleotide exchange factor 4 monomer, 114 kDa Mus musculus protein
Buffer: 150 mM NaCl, 1 mM EDTA, 1 mM DTT, and 10 mM Tris-HCl, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSess, University of Utah on 2008 Aug 11
Mechanism of Epac activation: structural and functional analyses of Epac2 hinge mutants with constitutive and reduced activities. J Biol Chem 284(35):23644-51 (2009)
...Blumenthal DK, Mei FC, White MA, Cheng X
RgGuinier 3.6 nm
Dmax 11.4 nm
VolumePorod 145 nm3

SASDL82 – Human acetylcholinesterase, apo

acetylcholinesteraseacetylcholinesterase experimental SAS data
OTHER model
Sample: acetylcholinesterase dimer, 120 kDa Homo sapiens protein
acetylcholinesterase monomer, 60 kDa Homo sapiens protein
Buffer: 50 mM Tris/HCl, 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 May 29
Covalent inhibition of hAChE by organophosphates causes homodimer dissociation through long-range allosteric effects. J Biol Chem :101007 (2021)
Blumenthal DK, Cheng X, Fajer M, Ho KY, Rohrer J, Gerlits O, Taylor P, Juneja P, Kovalevsky A, Radić Z
RgGuinier 3.9 nm
Dmax 13.0 nm
VolumePorod 162 nm3

SASDL92 – Human acetylcholinesterase, covalently bound to paraoxon

acetylcholinesteraseacetylcholinesterase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: acetylcholinesterase dimer, 120 kDa Homo sapiens protein
acetylcholinesterase monomer, 60 kDa Homo sapiens protein
Buffer: 50 mM Tris/HCl, 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 May 29
Covalent inhibition of hAChE by organophosphates causes homodimer dissociation through long-range allosteric effects. J Biol Chem :101007 (2021)
Blumenthal DK, Cheng X, Fajer M, Ho KY, Rohrer J, Gerlits O, Taylor P, Juneja P, Kovalevsky A, Radić Z
RgGuinier 3.4 nm
Dmax 12.0 nm
VolumePorod 142 nm3

SASDDS4 – cGMP-dependent protein kinase 1: ∆53 PKG Iα

cGMP-dependent protein kinase 1 experimental SAS data
DAMFILT model
Sample: cGMP-dependent protein kinase 1 monomer, 70 kDa Bos taurus protein
Buffer: 50 mM MES, 300 mM NaCl, 1 mM TCEP, 5 mM DTT, pH: 6.9
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Jun 6
An N-terminally truncated form of cyclic GMP-dependent protein kinase Iα (PKG Iα) is monomeric and autoinhibited and provides a model for activation. J Biol Chem 293(21):7916-7929 (2018)
...Blumenthal DK, Dostmann WR
RgGuinier 3.0 nm
Dmax 9.7 nm
VolumePorod 105 nm3

SASDQF5 – Zinc finger protein 410 (ZNF410 full length)

Zinc finger protein 410 experimental SAS data
BILBOMD model
Sample: Zinc finger protein 410 monomer, 52 kDa Homo sapiens protein
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 30
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
...Blumenthal RM, Zhang X, Cheng X
RgGuinier 3.6 nm
Dmax 12.3 nm
VolumePorod 108 nm3

SASDQG5 – DNA (Zinc finger protein 410 recognition sequence)

DNA (Zinc finger protein 410 recognition sequence) experimental SAS data
DNA (Zinc finger protein 410 recognition sequence) Kratky plot
Sample: DNA (Zinc finger protein 410 recognition sequence) monomer, 11 kDa DNA
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 30
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
...Blumenthal RM, Zhang X, Cheng X
RgGuinier 1.8 nm
Dmax 5.8 nm
VolumePorod 16 nm3

SASDQH5 – Zinc finger protein 410 (ZNF410 full length) bound to DNA

Zinc finger protein 410DNA (Zinc finger protein 410 recognition sequence) experimental SAS data
BILBOMD model
Sample: Zinc finger protein 410 monomer, 52 kDa Homo sapiens protein
DNA (Zinc finger protein 410 recognition sequence) monomer, 11 kDa DNA
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 30
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
...Blumenthal RM, Zhang X, Cheng X
RgGuinier 4.4 nm
Dmax 14.3 nm
VolumePorod 76 nm3

SASDQJ5 – Zinc finger protein 410 (ZNF410): N-terminal region with 1-5 zinc fingers

Zinc finger protein 410 experimental SAS data
BILBOMD model
Sample: Zinc finger protein 410 monomer, 40 kDa Homo sapiens protein
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 30
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
...Blumenthal RM, Zhang X, Cheng X
RgGuinier 3.2 nm
Dmax 10.7 nm
VolumePorod 78 nm3

SASDQK5 – Zinc finger protein 410 (ZNF410): N-terminal region with 1-5 zinc fingers bound to DNA

DNA (Zinc finger protein 410 recognition sequence)Zinc finger protein 410 experimental SAS data
BILBOMD model
Sample: DNA (Zinc finger protein 410 recognition sequence) monomer, 11 kDa DNA
Zinc finger protein 410 monomer, 40 kDa Homo sapiens protein
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2021 Apr 25
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
...Blumenthal RM, Zhang X, Cheng X
RgGuinier 3.1 nm
Dmax 14.1 nm
VolumePorod 63 nm3

SASDQL5 – Zinc finger protein 410 (ZNF410): C-terminal region with 1-5 zinc fingers

Zinc finger protein 410 experimental SAS data
BILBOMD model
Sample: Zinc finger protein 410 monomer, 29 kDa Homo sapiens protein
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 30
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
...Blumenthal RM, Zhang X, Cheng X
RgGuinier 3.0 nm
Dmax 9.6 nm
VolumePorod 58 nm3

SASDQM5 – Zinc finger protein 410 (ZNF410): C-terminal region with 1-5 zinc fingers bound to DNA

DNA (Zinc finger protein 410 recognition sequence)Zinc finger protein 410 experimental SAS data
BILBOMD model
Sample: DNA (Zinc finger protein 410 recognition sequence) monomer, 11 kDa DNA
Zinc finger protein 410 monomer, 29 kDa Homo sapiens protein
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 30
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
...Blumenthal RM, Zhang X, Cheng X
RgGuinier 3.1 nm
Dmax 11.9 nm
VolumePorod 52 nm3