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29 hits found for Borges

SASDL42 – Human Heat Shock Cognate 71 kDa Protein (HSPA8 / Hsc70)

Heat shock cognate 71 kDa protein experimental SAS data
Human Heat Shock Cognate 71 kDa Protein (HSPA8 / Hsc70) Rg histogram
Sample: Heat shock cognate 71 kDa protein monomer, 71 kDa Homo sapiens protein
Buffer: 25 mM Tris HCl, 50 mM NaCl, 5 mM Sodium Phosphate, 5 mM KCl, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2018 May 18
Structural, thermodynamic and functional studies of human 71 kDa heat shock cognate protein (HSPA8/hHsc70) Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics :140719 (2021)
...Borges J
RgGuinier 3.7 nm
Dmax 11.5 nm
VolumePorod 111 nm3

SASDL52 – Human Heat Shock 70 kDa Protein 1A (Hsp70-1A/HSPA1A)

Heat shock 70 kDa protein 1A experimental SAS data
DAMMIN model
Sample: Heat shock 70 kDa protein 1A monomer, 70 kDa Homo sapiens protein
Buffer: 25 mM Tris HCl, 50 mM NaCl, 5 mM Sodium Phosphate, 5 mM KCl, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2018 May 18
Structural, thermodynamic and functional studies of human 71 kDa heat shock cognate protein (HSPA8/hHsc70) Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics :140719 (2021)
...Borges J
RgGuinier 3.7 nm
Dmax 11.0 nm
VolumePorod 138 nm3

SASDBD3 – Leishmania braziliensis heat shock protein 90 (Hsp90).

Leishmania braziliensis heat shock protein 90 (Hsp90) experimental SAS data
DAMMIN model
Sample: Leishmania braziliensis heat shock protein 90 (Hsp90) dimer, 166 kDa Leishmania braziliensis protein
Buffer: 25 Tris mM 100 mM NaCl 1 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2011 Sep 1
Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering. Int J Biol Macromol 97:503-512 (2017)
...Borges JC
RgGuinier 5.3 nm
Dmax 21.0 nm
VolumePorod 380 nm3

SASDBE3 – Leishmania braziliensis heat shock protein 90 (Hsp90) N domain.

Leishmania braziliensis heat shock protein 90 (Hsp90) N domain experimental SAS data
DAMMIN model
Sample: Leishmania braziliensis heat shock protein 90 (Hsp90) N domain monomer, 26 kDa Leishmania braziliensis protein
Buffer: 25 Tris mM 100 mM NaCl 1 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2011 Sep 1
Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering. Int J Biol Macromol 97:503-512 (2017)
...Borges JC
RgGuinier 2.0 nm
Dmax 7.5 nm
VolumePorod 40 nm3

SASDBF3 – Leishmania braziliensis heat shock protein 90 (Hsp90) N and M domains.

Leishmania braziliensis heat shock protein 90 (Hsp90) N and M domains experimental SAS data
DAMMIN model
Sample: Leishmania braziliensis heat shock protein 90 (Hsp90) N and M domains monomer, 62 kDa Leishmania braziliensis protein
Buffer: 25 Tris mM 100 mM NaCl 1 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2011 Sep 1
Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering. Int J Biol Macromol 97:503-512 (2017)
...Borges JC
RgGuinier 3.2 nm
Dmax 13.0 nm
VolumePorod 89 nm3

SASDB54 – Leishmania braziliensis stress-induced protein sti1 (LbHop), full length construct

Stress-induced protein sti1 experimental SAS data
DAMFILT model
Sample: Stress-induced protein sti1 monomer, 62 kDa Leishmania braziliensis protein
Buffer: 25 mM Tris 100 mM NaCl 1 mM EDTA 1 mM β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2016 Feb 21
Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis. Arch Biochem Biophys 600:12-22 (2016)
...Borges JC
RgGuinier 4.5 nm
Dmax 18.0 nm
VolumePorod 94 nm3

SASDB64 – Leishmania braziliensis stress-induced protein sti1 (LbHop TPR2A-TPR2B-DP2 construct)

Stress-induced protein sti1 (Hop TPR2A-TPR2B-DP2 construct) experimental SAS data
DAMFILT model
Sample: Stress-induced protein sti1 (Hop TPR2A-TPR2B-DP2 construct) monomer, 44 kDa Leishmania braziliensis protein
Buffer: 25 mM Tris 100 mM NaCl 1 mM EDTA 1 mM β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2016 Feb 21
Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis. Arch Biochem Biophys 600:12-22 (2016)
...Borges JC
RgGuinier 3.8 nm
Dmax 14.0 nm
VolumePorod 65 nm3

SASDBR4 – Leishmania braziliensis Activator of Hsp90 ATPase-1 (LbAha1)

Activator of Hsp90 ATPase-1 experimental SAS data
Leishmania braziliensis Activator of Hsp90 ATPase-1 (LbAha1) Rg histogram
Sample: Activator of Hsp90 ATPase-1 monomer, 38 kDa Leishmania braziliensis protein
Buffer: 25 mM Sodium phosphate, 50 mM NaCl, 2 mM EDTA, 1 mM β-mercaptoethanol, pH: 7
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2013 Jun 1
Low resolution structural studies indicate that the activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis has an elongated shape which allows its interaction with both N- and M-domains of Hsp9... PLoS One 8(6):e66822 (2013)
...Borges JC
RgGuinier 3.6 nm
Dmax 14.5 nm

SASDC55 – Plasmodium falciparum p23A

CS domain protein, putative experimental SAS data
DAMFILT model
Sample: CS domain protein, putative monomer, 19 kDa Plasmodium falciparum protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 2 mM EDTA, 1 mM B-mercaptoethanol, pH: 7.4
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2015 May 26
Comparative studies of the low-resolution structure of two p23 co-chaperones for Hsp90 identified in Plasmodium falciparum genome. Int J Biol Macromol 108:193-204 (2018)
...Borges JC
RgGuinier 2.5 nm
Dmax 8.5 nm

SASDC65 – Plasmodium falciparum p23B

Co-chaperone p23 experimental SAS data
DAMFILT model
Sample: Co-chaperone p23 monomer, 31 kDa Plasmodium falciparum protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 2 mM EDTA, 1 mM B-mercaptoethanol, pH: 7.4
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2015 May 26
Comparative studies of the low-resolution structure of two p23 co-chaperones for Hsp90 identified in Plasmodium falciparum genome. Int J Biol Macromol 108:193-204 (2018)
...Borges JC
RgGuinier 3.7 nm
Dmax 13.0 nm

SASDC75 – Leishmania braziliensis SGT co-chaperone

SGT protein experimental SAS data
DAMFILT model
Sample: SGT protein dimer, 92 kDa Leishmania braziliensis protein
Buffer: 20 mM Potassium Phosphate, 100 mM KCl, 10 mM EDTA, 1 mM B-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2014 May 14
Structural and functional studies of the Leishmania braziliensis SGT co-chaperone indicate that it shares structural features with HIP and can interact with both Hsp90 and Hsp70 with similar affinitie... Int J Biol Macromol 118(Pt A):693-706 (2018)
...Borges JC
RgGuinier 4.5 nm
Dmax 17.0 nm

SASDC85 – Leishmania braziliensis p23B

Leishmania braziliensis p23 isoform B experimental SAS data
DAMFILT model
Sample: Leishmania braziliensis p23 isoform B monomer, 23 kDa Leishmania braziliensis protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 8
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2012 Mar 26
Identification of two p23 co-chaperone isoforms in Leishmania braziliensis exhibiting similar structures and Hsp90 interaction properties despite divergent stabilities. FEBS J 282(2):388-406 (2015)
...Borges JC
RgGuinier 3.0 nm
Dmax 13.0 nm

SASDFL5 – Plasmodium falciparum Hsp70/Hsp90 organizing protein, Hop

STI1-like protein experimental SAS data
DAMFILT model
Sample: STI1-like protein dimer, 136 kDa Plasmodium falciparum protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, 1 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2016 Aug 3
Structural studies of the Hsp70/Hsp90 organizing protein of Plasmodium falciparum and its modulation of Hsp70 and Hsp90 ATPase activities. Biochim Biophys Acta Proteins Proteom :140282 (2019)
...Borges JC
RgGuinier 6.3 nm
Dmax 24.0 nm
VolumePorod 557 nm3

SASDET5 – Old Yellow Enzyme of Leishmania braziliensis

Old Yellow Enzyme of Leishmania braziliensis experimental SAS data
DAMMIN model
Sample: Old Yellow Enzyme of Leishmania braziliensis monomer, 42 kDa Leishmania braziliensis protein
Buffer: 25 mM Tris-HCl 100 mM NaCl and 1 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2015 May 26
Structural studies of Old Yellow Enzyme of Leishmania braziliensis in solution. Arch Biochem Biophys (2018)
...Borges JC
RgGuinier 2.7 nm
Dmax 9.5 nm
VolumePorod 73 nm3

SASDCV5 – Leishmania braziliensis p23A

Uncharacterized protein experimental SAS data
DAMFILT model
Sample: Uncharacterized protein monomer, 22 kDa Leishmania braziliensis protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 8
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2012 Mar 26
Identification of two p23 co-chaperone isoforms in Leishmania braziliensis exhibiting similar structures and Hsp90 interaction properties despite divergent stabilities. FEBS J 282(2):388-406 (2015)
...Borges JC
RgGuinier 3.3 nm
Dmax 13.0 nm

SASDR96 – Human DjC20/DnaJC20/HscB iron-sulfur cluster co-chaperone protein

Iron-sulfur cluster co-chaperone protein HscB experimental SAS data
DAMMIF model
Sample: Iron-sulfur cluster co-chaperone protein HscB monomer, 25 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 50 mM NaCl, 5 mM KCl, 2 mM β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2018 Aug 14
Structural characterization of the human DjC20/HscB cochaperone in solution Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics :140970 (2023)
...Borges J
RgGuinier 2.5 nm
Dmax 9.0 nm
VolumePorod 40 nm3

SASDBY6 – Leishmania braziliensis Mitochondrial heat shock protein 70 (LbmtHSP70)

Mitochondrial heat shock protein 70 experimental SAS data
DAMMIN model
Sample: Mitochondrial heat shock protein 70 monomer, 71 kDa Leishmania braziliensis protein
Buffer: 25 mM Tris-HCl, 50 mM NacL, 5 mM KCl, 5 mM sodium phosphate, 2 mM B-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2012 Jun 22
Structural and functional studies of the Leishmania braziliensis mitochondrial Hsp70: Similarities and dissimilarities to human orthologues. Arch Biochem Biophys 613:43-52 (2017)
...Borges JC
RgGuinier 3.6 nm
Dmax 14.0 nm
VolumePorod 118 nm3

SASDHL8 – Aquifex aeolicus McoA metaloxidase evolved variant (2F4)

McoA evolved variant 2F4 (Periplasmic cell division protein (SufI)) experimental SAS data
OTHER model
Sample: McoA evolved variant 2F4 (Periplasmic cell division protein (SufI)) monomer, 55 kDa Aquifex aeolicus VF5 protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2017 Sep 25
Distal Mutations Shape Substrate-Binding Sites during Evolution of a Metallo-Oxidase into a Laccase ACS Catalysis :5022-5035 (2022)
...Borges P, Núñez-Franco R, Lucas M, Frazão C, Monza E, Masgrau L, Cordeiro T, Martins L
RgGuinier 2.3 nm
Dmax 6.8 nm
VolumePorod 78 nm3

SASDHM8 – Aquifex aeolicus McoA metaloxidase ∆328-352 evolved variant (2F4∆328-352)

Aquifex aeolicus McoA metaloxidase ∆328-352 evolved variant (2F4∆328-352) experimental SAS data
DAMMIF model
Sample: Aquifex aeolicus McoA metaloxidase ∆328-352 evolved variant (2F4∆328-352) monomer, 53 kDa Aquifex aeolicus protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Jul 18
Distal Mutations Shape Substrate-Binding Sites during Evolution of a Metallo-Oxidase into a Laccase ACS Catalysis :5022-5035 (2022)
...Borges P, Núñez-Franco R, Lucas M, Frazão C, Monza E, Masgrau L, Cordeiro T, Martins L
RgGuinier 2.2 nm
Dmax 6.6 nm
VolumePorod 74 nm3

SASDHD9 – Full-length Plasmodium falciparum Heat shock protein 90 (PfHsp90)

Plasmodium falciparum Heat shock protein 90 experimental SAS data
DAMMIN model
Sample: Plasmodium falciparum Heat shock protein 90 dimer, 177 kDa Plasmodium falciparum protein
Buffer: 25 mM Tris-HCl, 100 mM KCl, 1 mM β-mercaptoethanol, 1 mM EDTA, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2018 May 11
Solution structure of Plasmodium falciparum Hsp90 indicates a high flexible dimer Archives of Biochemistry and Biophysics :108468 (2020)
...Borges J
RgGuinier 5.7 nm
Dmax 19.0 nm
VolumePorod 350 nm3

SASDHE9 – Plasmodium falciparum Heat shock protein 90 (PfHsp90) N- and M-domains

Plasmodium falciparum Heat shock protein 90 N-terminal and Middle domains experimental SAS data
Plasmodium falciparum Heat shock protein 90 (PfHsp90) N- and M-domains Rg histogram
Sample: Plasmodium falciparum Heat shock protein 90 N-terminal and Middle domains monomer, 68 kDa Plasmodium falciparum protein
Buffer: 25 mM Tris-HCl, 100 mM KCl, 1 mM β-mercaptoethanol, 1 mM EDTA, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2018 May 11
Solution structure of Plasmodium falciparum Hsp90 indicates a high flexible dimer Archives of Biochemistry and Biophysics :108468 (2020)
...Borges J
RgGuinier 3.9 nm
Dmax 14.0 nm
VolumePorod 106 nm3

SASDHF9 – Plasmodium falciparum Heat shock protein 90 (PfHsp90) M-domain

Plasmodium falciparum Heat shock protein 90 middle domain experimental SAS data
DAMMIN model
Sample: Plasmodium falciparum Heat shock protein 90 middle domain monomer, 33 kDa Plasmodium falciparum protein
Buffer: 25 mM Tris-HCl, 100 mM KCl, 1 mM β-mercaptoethanol, 1 mM EDTA, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2018 May 11
Solution structure of Plasmodium falciparum Hsp90 indicates a high flexible dimer Archives of Biochemistry and Biophysics :108468 (2020)
...Borges J
RgGuinier 2.4 nm
Dmax 8.5 nm
VolumePorod 47 nm3

SASDBH6 – Full-length human p23 (1-160)

Prostaglandin E synthase 3 experimental SAS data
Prostaglandin E synthase 3 Kratky plot
Sample: Prostaglandin E synthase 3 monomer, 19 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2012 Jun 22
The C-terminal region of the human p23 chaperone modulates its structure and function. Arch Biochem Biophys 565:57-67 (2015)
...Borges JC
RgGuinier 2.5 nm
Dmax 10.0 nm
VolumePorod 40 nm3

SASDFY7 – Aquifex aeolicus McoA metaloxidase

Aquifex aeolicus McoA metaloxidase experimental SAS data
DAMFILT model
Sample: Aquifex aeolicus McoA metaloxidase monomer, 55 kDa Aquifex aeolicus protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Apr 15
The Methionine-Rich Loop of Multicopper Oxidase McoA follows Open-To-Close Transitions with a Role in Enzyme Catalysis ACS Catalysis (2020)
Borges P, Brissos V, Hernandez G, Masgrau L, Lucas M, Monza E, Frazão C, Cordeiro T, Martins L
RgGuinier 2.3 nm
Dmax 7.5 nm
VolumePorod 79 nm3

SASDBJ6 – Truncated construct of human p23 (1-142)

Prostaglandin E synthase 3 (1-142) experimental SAS data
Prostaglandin E synthase 3 (1-142) Kratky plot
Sample: Prostaglandin E synthase 3 (1-142) monomer, 17 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2012 Jun 22
The C-terminal region of the human p23 chaperone modulates its structure and function. Arch Biochem Biophys 565:57-67 (2015)
...Borges JC
RgGuinier 2.1 nm
Dmax 8.5 nm
VolumePorod 36 nm3

SASDFX7 – Aquifex aeolicus McoA metaloxidase deletion mutant ∆337-346 (MCoA∆337-346)

Aquifex aeolicus McoA metaloxidase ∆337-346 experimental SAS data
DAMMIF model
Sample: Aquifex aeolicus McoA metaloxidase ∆337-346 monomer, 54 kDa Aquifex aeolicus protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Dec 4
The Methionine-Rich Loop of Multicopper Oxidase McoA follows Open-To-Close Transitions with a Role in Enzyme Catalysis ACS Catalysis (2020)
Borges P, Brissos V, Hernandez G, Masgrau L, Lucas M, Monza E, Frazão C, Cordeiro T, Martins L
RgGuinier 2.3 nm
Dmax 7.0 nm
VolumePorod 78 nm3

SASDBL6 – Truncated construct of human p23 (1-117)

Prostaglandin E synthase 3 (1-117) experimental SAS data
Prostaglandin E synthase 3 (1-117) Kratky plot
Sample: Prostaglandin E synthase 3 (1-117) monomer, 14 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2013 Jun 21
The C-terminal region of the human p23 chaperone modulates its structure and function. Arch Biochem Biophys 565:57-67 (2015)
...Borges JC
RgGuinier 1.9 nm
Dmax 7.0 nm
VolumePorod 29 nm3

SASDFW7 – Aquifex aeolicus McoA metaloxidase deletion mutant ∆328-352 (MCoA∆328-352)

Aquifex aeolicus McoA metaloxidase ∆328-352 (MCoA∆328-352) experimental SAS data
DAMFILT model
Sample: Aquifex aeolicus McoA metaloxidase ∆328-352 (MCoA∆328-352) monomer, 53 kDa Aquifex aeolicus protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2017 Jul 13
The Methionine-Rich Loop of Multicopper Oxidase McoA follows Open-To-Close Transitions with a Role in Enzyme Catalysis ACS Catalysis (2020)
Borges P, Brissos V, Hernandez G, Masgrau L, Lucas M, Monza E, Frazão C, Cordeiro T, Martins L
RgGuinier 2.3 nm
Dmax 6.9 nm
VolumePorod 77 nm3

SASDBK6 – Truncated construct of human p23 (1-131)

Prostaglandin E synthase 3 (1-131) experimental SAS data
Prostaglandin E synthase 3 (1-131) Kratky plot
Sample: Prostaglandin E synthase 3 (1-131) monomer, 16 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2013 Jun 21
The C-terminal region of the human p23 chaperone modulates its structure and function. Arch Biochem Biophys 565:57-67 (2015)
...Borges JC
RgGuinier 1.9 nm
Dmax 7.0 nm
VolumePorod 31 nm3