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site-specific mutations of hca ii  (GenScript corporation)
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GenScript corporation site-specific mutations of hca ii
Ribbon diagram of <t>HCA</t> <t>II</t> with the active site and mutated surface residues indicated in ball-and-stick. (a) HCA II in blue with the mutated Leu residues in red, the zinc is shown as a magenta sphere with the hydrophilic residues involved with catalysis shown in yellow ball and stick. For panels (b)–(d) wild type and TS2 was superimposed to show the differences, wild type is in blue and TS2 is in yellow ball-and-stick; (b) Leu100His variant and inferred H-bonds (based on distance and angles) are shown as black dashed lines, (c) Leu224Ser, (d) Leu240Pro and waters and H-bonds. This figure was generated and rendered in PyMOL (DeLano, 2002).
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Ribbon diagram of HCA II with the active site and mutated surface residues indicated in ball-and-stick. (a) HCA II in blue with the mutated Leu residues in red, the zinc is shown as a magenta sphere with the hydrophilic residues involved with catalysis shown in yellow ball and stick. For panels (b)–(d) wild type and TS2 was superimposed to show the differences, wild type is in blue and TS2 is in yellow ball-and-stick; (b) Leu100His variant and inferred H-bonds (based on distance and angles) are shown as black dashed lines, (c) Leu224Ser, (d) Leu240Pro and waters and H-bonds. This figure was generated and rendered in PyMOL (DeLano, 2002).

Journal: Protein Engineering, Design and Selection

Article Title: Kinetic and structural characterization of thermostabilized mutants of human carbonic anhydrase II

doi: 10.1093/protein/gzs027

Figure Lengend Snippet: Ribbon diagram of HCA II with the active site and mutated surface residues indicated in ball-and-stick. (a) HCA II in blue with the mutated Leu residues in red, the zinc is shown as a magenta sphere with the hydrophilic residues involved with catalysis shown in yellow ball and stick. For panels (b)–(d) wild type and TS2 was superimposed to show the differences, wild type is in blue and TS2 is in yellow ball-and-stick; (b) Leu100His variant and inferred H-bonds (based on distance and angles) are shown as black dashed lines, (c) Leu224Ser, (d) Leu240Pro and waters and H-bonds. This figure was generated and rendered in PyMOL (DeLano, 2002).

Article Snippet: Crystallization and X-ray crystal structure determination Site-specific mutations of HCA II were made by GenScript.

Techniques: Variant Assay, Generated

Differential scanning calorimetry measurements of the major unfolding transition ( T M in °C) of each TS mutant compared with wild-type HCA II and the Y7F mutant

Journal: Protein Engineering, Design and Selection

Article Title: Kinetic and structural characterization of thermostabilized mutants of human carbonic anhydrase II

doi: 10.1093/protein/gzs027

Figure Lengend Snippet: Differential scanning calorimetry measurements of the major unfolding transition ( T M in °C) of each TS mutant compared with wild-type HCA II and the Y7F mutant

Article Snippet: Crystallization and X-ray crystal structure determination Site-specific mutations of HCA II were made by GenScript.

Techniques: Differential Scanning Calorimetry, Mutagenesis

Ball-and-stick diagrams of wild type and stabilized variants of HCA II active sites. The Zn is shown as a magenta sphere and all the hydrophilic active site residues (and their counterparts in the mutants) are shown as sticks, waters are shown as red spheres. Residues and waters are as labeled and inferred H-bonds are shown as black dashed lines. Maps are omitted for clarity. Figures were generated and rendered with PyMOL (DeLano, 2002).

Journal: Protein Engineering, Design and Selection

Article Title: Kinetic and structural characterization of thermostabilized mutants of human carbonic anhydrase II

doi: 10.1093/protein/gzs027

Figure Lengend Snippet: Ball-and-stick diagrams of wild type and stabilized variants of HCA II active sites. The Zn is shown as a magenta sphere and all the hydrophilic active site residues (and their counterparts in the mutants) are shown as sticks, waters are shown as red spheres. Residues and waters are as labeled and inferred H-bonds are shown as black dashed lines. Maps are omitted for clarity. Figures were generated and rendered with PyMOL (DeLano, 2002).

Article Snippet: Crystallization and X-ray crystal structure determination Site-specific mutations of HCA II were made by GenScript.

Techniques: Labeling, Generated

Maximal, pH independent values of the kinetic constants for catalysis by variants of HCA II measured by 18 O exchange

Journal: Protein Engineering, Design and Selection

Article Title: Kinetic and structural characterization of thermostabilized mutants of human carbonic anhydrase II

doi: 10.1093/protein/gzs027

Figure Lengend Snippet: Maximal, pH independent values of the kinetic constants for catalysis by variants of HCA II measured by 18 O exchange

Article Snippet: Crystallization and X-ray crystal structure determination Site-specific mutations of HCA II were made by GenScript.

Techniques:

The rate constant R1/[E] (s−1) as a function of temperature for the interconversion of CO2 and bicarbonate catalyzed by variants of HCA II. Wild type = black filled square; TS1 = red filled rhombus; TS2 = dark blue triangle; TS3 = brown square; TS4 = light blue filled square and TS5 = green filled triangle. Data have been separated on the ordinate to avoid superposition of points. Solutions contained 10 mM of all species of CO2 and 100 mM HEPES at pH 7.6.

Journal: Protein Engineering, Design and Selection

Article Title: Kinetic and structural characterization of thermostabilized mutants of human carbonic anhydrase II

doi: 10.1093/protein/gzs027

Figure Lengend Snippet: The rate constant R1/[E] (s−1) as a function of temperature for the interconversion of CO2 and bicarbonate catalyzed by variants of HCA II. Wild type = black filled square; TS1 = red filled rhombus; TS2 = dark blue triangle; TS3 = brown square; TS4 = light blue filled square and TS5 = green filled triangle. Data have been separated on the ordinate to avoid superposition of points. Solutions contained 10 mM of all species of CO2 and 100 mM HEPES at pH 7.6.

Article Snippet: Crystallization and X-ray crystal structure determination Site-specific mutations of HCA II were made by GenScript.

Techniques: