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17 hits found for Borges

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, 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, 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

SASDC75 – Leishmania braziliensis SGT co-chaperone

SGT protein experimental SAS data
DAMFILT model
Sample: SGT protein dimer, 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, 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

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, 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, 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, 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

SASDC65 – Plasmodium falciparum p23B

Co-chaperone p23 experimental SAS data
DAMFILT model
Sample: Co-chaperone p23 monomer, Plasmodium falciparum (isolate ... 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

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, 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

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, 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

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, 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

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, 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

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, 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, Plasmodium falciparum (isolate ... 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

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, 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, 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

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, 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