atomic force microscopy Search Results


mode atomic force microscopy in air  (Oxford Instruments)
96
Oxford Instruments mode atomic force microscopy in air
A) Atomic force <t>microscopy</t> image of a sample wsMUR-TM_v2 after stored at 4 °C for about 2 months. Protein concentration is 7.5 mg/mL. Buffer is 20mM sodium phosphate, 130mM NaCl, 0.02% sodium dodecyl sulfate, 5mM 2ME, pH=7.0. Monomer, dimer, and large aggregates are present. B) Histogram of the feature of the protein in the solution. The estimated number of features present on surface consistent with the dimensions of the monomer is ~70%. wsMUR-TM = first variant of the water-soluble human μ opioid receptor transmembrane portion; wsMUR-TM_v2 = modified (second) variant of the water-soluble human μ opioid receptor transmembrane portion.
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atomic force microscopy triangular silicon nitride cantilevers  (Veeco)
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Veeco atomic force microscopy triangular silicon nitride cantilevers
A) Atomic force <t>microscopy</t> image of a sample wsMUR-TM_v2 after stored at 4 °C for about 2 months. Protein concentration is 7.5 mg/mL. Buffer is 20mM sodium phosphate, 130mM NaCl, 0.02% sodium dodecyl sulfate, 5mM 2ME, pH=7.0. Monomer, dimer, and large aggregates are present. B) Histogram of the feature of the protein in the solution. The estimated number of features present on surface consistent with the dimensions of the monomer is ~70%. wsMUR-TM = first variant of the water-soluble human μ opioid receptor transmembrane portion; wsMUR-TM_v2 = modified (second) variant of the water-soluble human μ opioid receptor transmembrane portion.
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atomic force microscopy images  (NT MDT America Inc)
90
NT MDT America Inc atomic force microscopy images
A) Atomic force <t>microscopy</t> image of a sample wsMUR-TM_v2 after stored at 4 °C for about 2 months. Protein concentration is 7.5 mg/mL. Buffer is 20mM sodium phosphate, 130mM NaCl, 0.02% sodium dodecyl sulfate, 5mM 2ME, pH=7.0. Monomer, dimer, and large aggregates are present. B) Histogram of the feature of the protein in the solution. The estimated number of features present on surface consistent with the dimensions of the monomer is ~70%. wsMUR-TM = first variant of the water-soluble human μ opioid receptor transmembrane portion; wsMUR-TM_v2 = modified (second) variant of the water-soluble human μ opioid receptor transmembrane portion.
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atomic force microscopy nscriptor dpn system  (NanoInk Inc)
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NanoInk Inc atomic force microscopy nscriptor dpn system
A) Atomic force <t>microscopy</t> image of a sample wsMUR-TM_v2 after stored at 4 °C for about 2 months. Protein concentration is 7.5 mg/mL. Buffer is 20mM sodium phosphate, 130mM NaCl, 0.02% sodium dodecyl sulfate, 5mM 2ME, pH=7.0. Monomer, dimer, and large aggregates are present. B) Histogram of the feature of the protein in the solution. The estimated number of features present on surface consistent with the dimensions of the monomer is ~70%. wsMUR-TM = first variant of the water-soluble human μ opioid receptor transmembrane portion; wsMUR-TM_v2 = modified (second) variant of the water-soluble human μ opioid receptor transmembrane portion.
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atomic force microscope  (JPK Instruments AG)
90
JPK Instruments AG atomic force microscope
A) Atomic force <t>microscopy</t> image of a sample wsMUR-TM_v2 after stored at 4 °C for about 2 months. Protein concentration is 7.5 mg/mL. Buffer is 20mM sodium phosphate, 130mM NaCl, 0.02% sodium dodecyl sulfate, 5mM 2ME, pH=7.0. Monomer, dimer, and large aggregates are present. B) Histogram of the feature of the protein in the solution. The estimated number of features present on surface consistent with the dimensions of the monomer is ~70%. wsMUR-TM = first variant of the water-soluble human μ opioid receptor transmembrane portion; wsMUR-TM_v2 = modified (second) variant of the water-soluble human μ opioid receptor transmembrane portion.
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intermittentcontact atomic force microscopy—it-afm ntegra prima  (NT MDT America Inc)
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NT MDT America Inc intermittentcontact atomic force microscopy—it-afm ntegra prima
A) Atomic force <t>microscopy</t> image of a sample wsMUR-TM_v2 after stored at 4 °C for about 2 months. Protein concentration is 7.5 mg/mL. Buffer is 20mM sodium phosphate, 130mM NaCl, 0.02% sodium dodecyl sulfate, 5mM 2ME, pH=7.0. Monomer, dimer, and large aggregates are present. B) Histogram of the feature of the protein in the solution. The estimated number of features present on surface consistent with the dimensions of the monomer is ~70%. wsMUR-TM = first variant of the water-soluble human μ opioid receptor transmembrane portion; wsMUR-TM_v2 = modified (second) variant of the water-soluble human μ opioid receptor transmembrane portion.
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atomic force microscopy afm  (Nanoman Industries)
90
Nanoman Industries atomic force microscopy afm
A) Atomic force <t>microscopy</t> image of a sample wsMUR-TM_v2 after stored at 4 °C for about 2 months. Protein concentration is 7.5 mg/mL. Buffer is 20mM sodium phosphate, 130mM NaCl, 0.02% sodium dodecyl sulfate, 5mM 2ME, pH=7.0. Monomer, dimer, and large aggregates are present. B) Histogram of the feature of the protein in the solution. The estimated number of features present on surface consistent with the dimensions of the monomer is ~70%. wsMUR-TM = first variant of the water-soluble human μ opioid receptor transmembrane portion; wsMUR-TM_v2 = modified (second) variant of the water-soluble human μ opioid receptor transmembrane portion.
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atomic force microscopy  (Nanomechanics Inc)
90
Nanomechanics Inc atomic force microscopy
A) Atomic force <t>microscopy</t> image of a sample wsMUR-TM_v2 after stored at 4 °C for about 2 months. Protein concentration is 7.5 mg/mL. Buffer is 20mM sodium phosphate, 130mM NaCl, 0.02% sodium dodecyl sulfate, 5mM 2ME, pH=7.0. Monomer, dimer, and large aggregates are present. B) Histogram of the feature of the protein in the solution. The estimated number of features present on surface consistent with the dimensions of the monomer is ~70%. wsMUR-TM = first variant of the water-soluble human μ opioid receptor transmembrane portion; wsMUR-TM_v2 = modified (second) variant of the water-soluble human μ opioid receptor transmembrane portion.
Atomic Force Microscopy, supplied by Nanomechanics Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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atomic force microscopy (afm)  (Measurand Inc)
90
Measurand Inc atomic force microscopy (afm)
A) Atomic force <t>microscopy</t> image of a sample wsMUR-TM_v2 after stored at 4 °C for about 2 months. Protein concentration is 7.5 mg/mL. Buffer is 20mM sodium phosphate, 130mM NaCl, 0.02% sodium dodecyl sulfate, 5mM 2ME, pH=7.0. Monomer, dimer, and large aggregates are present. B) Histogram of the feature of the protein in the solution. The estimated number of features present on surface consistent with the dimensions of the monomer is ~70%. wsMUR-TM = first variant of the water-soluble human μ opioid receptor transmembrane portion; wsMUR-TM_v2 = modified (second) variant of the water-soluble human μ opioid receptor transmembrane portion.
Atomic Force Microscopy (Afm), supplied by Measurand Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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afm nanosurf mobile  (Nanosurf Inc)
90
Nanosurf Inc afm nanosurf mobile
A) Atomic force <t>microscopy</t> image of a sample wsMUR-TM_v2 after stored at 4 °C for about 2 months. Protein concentration is 7.5 mg/mL. Buffer is 20mM sodium phosphate, 130mM NaCl, 0.02% sodium dodecyl sulfate, 5mM 2ME, pH=7.0. Monomer, dimer, and large aggregates are present. B) Histogram of the feature of the protein in the solution. The estimated number of features present on surface consistent with the dimensions of the monomer is ~70%. wsMUR-TM = first variant of the water-soluble human μ opioid receptor transmembrane portion; wsMUR-TM_v2 = modified (second) variant of the water-soluble human μ opioid receptor transmembrane portion.
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atomic force microscopy  (Nature Biotechnology)
90
Nature Biotechnology atomic force microscopy
A) Atomic force <t>microscopy</t> image of a sample wsMUR-TM_v2 after stored at 4 °C for about 2 months. Protein concentration is 7.5 mg/mL. Buffer is 20mM sodium phosphate, 130mM NaCl, 0.02% sodium dodecyl sulfate, 5mM 2ME, pH=7.0. Monomer, dimer, and large aggregates are present. B) Histogram of the feature of the protein in the solution. The estimated number of features present on surface consistent with the dimensions of the monomer is ~70%. wsMUR-TM = first variant of the water-soluble human μ opioid receptor transmembrane portion; wsMUR-TM_v2 = modified (second) variant of the water-soluble human μ opioid receptor transmembrane portion.
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muscovite mica for atomic force microscopy (afm)  (NT MDT America Inc)
90
NT MDT America Inc muscovite mica for atomic force microscopy (afm)
A) Atomic force <t>microscopy</t> image of a sample wsMUR-TM_v2 after stored at 4 °C for about 2 months. Protein concentration is 7.5 mg/mL. Buffer is 20mM sodium phosphate, 130mM NaCl, 0.02% sodium dodecyl sulfate, 5mM 2ME, pH=7.0. Monomer, dimer, and large aggregates are present. B) Histogram of the feature of the protein in the solution. The estimated number of features present on surface consistent with the dimensions of the monomer is ~70%. wsMUR-TM = first variant of the water-soluble human μ opioid receptor transmembrane portion; wsMUR-TM_v2 = modified (second) variant of the water-soluble human μ opioid receptor transmembrane portion.
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Image Search Results


A) Atomic force microscopy image of a sample wsMUR-TM_v2 after stored at 4 °C for about 2 months. Protein concentration is 7.5 mg/mL. Buffer is 20mM sodium phosphate, 130mM NaCl, 0.02% sodium dodecyl sulfate, 5mM 2ME, pH=7.0. Monomer, dimer, and large aggregates are present. B) Histogram of the feature of the protein in the solution. The estimated number of features present on surface consistent with the dimensions of the monomer is ~70%. wsMUR-TM = first variant of the water-soluble human μ opioid receptor transmembrane portion; wsMUR-TM_v2 = modified (second) variant of the water-soluble human μ opioid receptor transmembrane portion.

Journal: Anesthesiology

Article Title: Characterization of a Computationally Designed Water-soluble Human μ Opioid Receptor Variant Using X-ray Structural Information

doi: 10.1097/ALN.0000000000000308

Figure Lengend Snippet: A) Atomic force microscopy image of a sample wsMUR-TM_v2 after stored at 4 °C for about 2 months. Protein concentration is 7.5 mg/mL. Buffer is 20mM sodium phosphate, 130mM NaCl, 0.02% sodium dodecyl sulfate, 5mM 2ME, pH=7.0. Monomer, dimer, and large aggregates are present. B) Histogram of the feature of the protein in the solution. The estimated number of features present on surface consistent with the dimensions of the monomer is ~70%. wsMUR-TM = first variant of the water-soluble human μ opioid receptor transmembrane portion; wsMUR-TM_v2 = modified (second) variant of the water-soluble human μ opioid receptor transmembrane portion.

Article Snippet: High-resolution atomic force microscopy Tapping mode atomic force microscopy in air (MFP-3D, Asylum Research, CA) was used to visualize the protein particles under various solution conditions as we described previously.

Techniques: Microscopy, Protein Concentration, Variant Assay, Modification