Review



site-specific mutations of hca ii  (GenScript corporation)

 
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 90
      Buy from Supplier

    Structured Review

    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).
    Site Specific Mutations Of Hca Ii, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/site-specific mutations of hca ii/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    site-specific mutations of hca ii - by Bioz Stars, 2026-04
    90/100 stars

    Images

    1) Product Images from "Kinetic and structural characterization of thermostabilized mutants of human carbonic anhydrase II"

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

    Journal: Protein Engineering, Design and Selection

    doi: 10.1093/protein/gzs027

    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).
    Figure Legend 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).

    Techniques Used: 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
    Figure Legend 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

    Techniques Used: 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).
    Figure Legend 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).

    Techniques Used: Labeling, Generated

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

    Techniques Used:

    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.
    Figure Legend 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.

    Techniques Used:



    Similar Products

    site-specific mutations of hca ii  (GenScript corporation)
    90
    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).
    Site Specific Mutations Of Hca Ii, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/site-specific mutations of hca ii/product/GenScript corporation
    Average 90 stars, based on 1 article reviews
    site-specific mutations of hca ii - by Bioz Stars, 2026-04
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    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: