The Experts below are selected from a list of 96 Experts worldwide ranked by ideXlab platform

Lech Kozerski - One of the best experts on this subject based on the ideXlab platform.

  • Identification of Lysine Misincorporation at Asparagine Position in Recombinant Insulin Analogs Produced in E. coli.
    Pharmaceutical research, 2019
    Co-Authors: Dorota Stadnik, Anna Bierczynska-krzysik, Joanna Zielińska, Jarosław Antosik, Piotr Borowicz, Elżbieta Bednarek, Wojciech Bocian, Jerzy Sitkowski, Lech Kozerski
    Abstract:

    Identification of human Insulin analogs’ impurity with a mass shift +14 Da in comparison to a parent protein. The protein sequence variant was detected and identified with the application of peptide mapping, liquid chromatography, tandem mass spectrometric analysis, nuclear magnetic resonance spectroscopy (NMR) and Edman sequencing. The misincorporated lysine (Lys) at asparagine (Asn) position A21 was detected in recombinant human Insulin and its analogs. Although there are three asparagine residues in the Insulin Derivative, the misincorporation of lysine occurred only at position A21. The process involves G/U or A/U wobble base pairing.

  • Identification of Lysine Misincorporation at Asparagine Position in Recombinant Insulin Analogs Produced in E. coli
    Pharmaceutical Research, 2019
    Co-Authors: Dorota Stadnik, Anna Bierczynska-krzysik, Joanna Zielińska, Jarosław Antosik, Piotr Borowicz, Elżbieta Bednarek, Wojciech Bocian, Jerzy Sitkowski, Lech Kozerski
    Abstract:

    Purpose Identification of human Insulin analogs’ impurity with a mass shift +14 Da in comparison to a parent protein. Methods The protein sequence variant was detected and identified with the application of peptide mapping, liquid chromatography, tandem mass spectrometric analysis, nuclear magnetic resonance spectroscopy (NMR) and Edman sequencing. Results The misincorporated lysine (Lys) at asparagine (Asn) position A21 was detected in recombinant human Insulin and its analogs. Conclusions Although there are three asparagine residues in the Insulin Derivative, the misincorporation of lysine occurred only at position A21. The process involves G/U or A/U wobble base pairing.

Dorota Stadnik - One of the best experts on this subject based on the ideXlab platform.

  • Identification of Lysine Misincorporation at Asparagine Position in Recombinant Insulin Analogs Produced in E. coli.
    Pharmaceutical research, 2019
    Co-Authors: Dorota Stadnik, Anna Bierczynska-krzysik, Joanna Zielińska, Jarosław Antosik, Piotr Borowicz, Elżbieta Bednarek, Wojciech Bocian, Jerzy Sitkowski, Lech Kozerski
    Abstract:

    Identification of human Insulin analogs’ impurity with a mass shift +14 Da in comparison to a parent protein. The protein sequence variant was detected and identified with the application of peptide mapping, liquid chromatography, tandem mass spectrometric analysis, nuclear magnetic resonance spectroscopy (NMR) and Edman sequencing. The misincorporated lysine (Lys) at asparagine (Asn) position A21 was detected in recombinant human Insulin and its analogs. Although there are three asparagine residues in the Insulin Derivative, the misincorporation of lysine occurred only at position A21. The process involves G/U or A/U wobble base pairing.

  • Identification of Lysine Misincorporation at Asparagine Position in Recombinant Insulin Analogs Produced in E. coli
    Pharmaceutical Research, 2019
    Co-Authors: Dorota Stadnik, Anna Bierczynska-krzysik, Joanna Zielińska, Jarosław Antosik, Piotr Borowicz, Elżbieta Bednarek, Wojciech Bocian, Jerzy Sitkowski, Lech Kozerski
    Abstract:

    Purpose Identification of human Insulin analogs’ impurity with a mass shift +14 Da in comparison to a parent protein. Methods The protein sequence variant was detected and identified with the application of peptide mapping, liquid chromatography, tandem mass spectrometric analysis, nuclear magnetic resonance spectroscopy (NMR) and Edman sequencing. Results The misincorporated lysine (Lys) at asparagine (Asn) position A21 was detected in recombinant human Insulin and its analogs. Conclusions Although there are three asparagine residues in the Insulin Derivative, the misincorporation of lysine occurred only at position A21. The process involves G/U or A/U wobble base pairing.

Pernille Harris - One of the best experts on this subject based on the ideXlab platform.

  • Towards accurate structural characterization of metal centres in protein crystals: the structures of Ni and Cu T6 bovine Insulin Derivatives
    Acta Crystallographica Section D Biological Crystallography, 2013
    Co-Authors: Christian Grundahl Frankær, Susanne Mossin, Kenny Ståhl, Pernille Harris
    Abstract:

    Using synchrotron radiation (SR), the crystal structures of T6 bovine Insulin complexed with Ni2+ and Cu2+ were solved to 1.50 and 1.45 A resolution, respectively. The level of detail around the metal centres in these structures was highly limited, and the coordination of water in Cu site II of the copper Insulin Derivative was deteriorated as a consequence of radiation damage. To provide more detail, X-ray absorption spectroscopy (XAS) was used to improve the information level about metal coordination in each Derivative. The nickel Derivative contains hexacoordinated Ni2+ with trigonal symmetry, whereas the copper Derivative contains tetragonally distorted hexacoordinated Cu2+ as a result of the Jahn–Teller effect, with a significantly longer coordination distance for one of the three water molecules in the coordination sphere. That the copper centre is of type II was further confirmed by electron paramagnetic resonance (EPR). The coordination distances were refined from EXAFS with standard deviations within 0.01 A. The Insulin Derivative containing Cu2+ is sensitive towards photoreduction when exposed to SR. During the reduction of Cu2+ to Cu+, the coordination geometry of copper changes towards lower coordination numbers. Primary damage, i.e. photoreduction, was followed directly by XANES as a function of radiation dose, while secondary damage in the form of structural changes around the Cu atoms after exposure to different radiation doses was studied by crystallography using a laboratory diffractometer. Protection against photoreduction and subsequent radiation damage was carried out by solid embedment of Cu Insulin in a saccharose matrix. At 100 K the photoreduction was suppressed by ∼15%, and it was suppressed by a further ∼30% on cooling the samples to 20 K.

  • Towards accurate structural characterization of metal centres in protein crystals: the structures of Ni and Cu T(6) bovine Insulin Derivatives.
    Acta crystallographica. Section D Biological crystallography, 2013
    Co-Authors: Christian Grundahl Frankær, Susanne Mossin, Kenny Ståhl, Pernille Harris
    Abstract:

    Using synchrotron radiation (SR), the crystal structures of T6 bovine Insulin complexed with Ni(2+) and Cu(2+) were solved to 1.50 and 1.45 Å resolution, respectively. The level of detail around the metal centres in these structures was highly limited, and the coordination of water in Cu site II of the copper Insulin Derivative was deteriorated as a consequence of radiation damage. To provide more detail, X-ray absorption spectroscopy (XAS) was used to improve the information level about metal coordination in each Derivative. The nickel Derivative contains hexacoordinated Ni(2+) with trigonal symmetry, whereas the copper Derivative contains tetragonally distorted hexacoordinated Cu(2+) as a result of the Jahn-Teller effect, with a significantly longer coordination distance for one of the three water molecules in the coordination sphere. That the copper centre is of type II was further confirmed by electron paramagnetic resonance (EPR). The coordination distances were refined from EXAFS with standard deviations within 0.01 Å. The Insulin Derivative containing Cu(2+) is sensitive towards photoreduction when exposed to SR. During the reduction of Cu(2+) to Cu(+), the coordination geometry of copper changes towards lower coordination numbers. Primary damage, i.e. photoreduction, was followed directly by XANES as a function of radiation dose, while secondary damage in the form of structural changes around the Cu atoms after exposure to different radiation doses was studied by crystallography using a laboratory diffractometer. Protection against photoreduction and subsequent radiation damage was carried out by solid embedment of Cu Insulin in a saccharose matrix. At 100 K the photoreduction was suppressed by ∼15%, and it was suppressed by a further ∼30% on cooling the samples to 20 K.

Jarosław Antosik - One of the best experts on this subject based on the ideXlab platform.

  • Identification of Lysine Misincorporation at Asparagine Position in Recombinant Insulin Analogs Produced in E. coli.
    Pharmaceutical research, 2019
    Co-Authors: Dorota Stadnik, Anna Bierczynska-krzysik, Joanna Zielińska, Jarosław Antosik, Piotr Borowicz, Elżbieta Bednarek, Wojciech Bocian, Jerzy Sitkowski, Lech Kozerski
    Abstract:

    Identification of human Insulin analogs’ impurity with a mass shift +14 Da in comparison to a parent protein. The protein sequence variant was detected and identified with the application of peptide mapping, liquid chromatography, tandem mass spectrometric analysis, nuclear magnetic resonance spectroscopy (NMR) and Edman sequencing. The misincorporated lysine (Lys) at asparagine (Asn) position A21 was detected in recombinant human Insulin and its analogs. Although there are three asparagine residues in the Insulin Derivative, the misincorporation of lysine occurred only at position A21. The process involves G/U or A/U wobble base pairing.

  • Identification of Lysine Misincorporation at Asparagine Position in Recombinant Insulin Analogs Produced in E. coli
    Pharmaceutical Research, 2019
    Co-Authors: Dorota Stadnik, Anna Bierczynska-krzysik, Joanna Zielińska, Jarosław Antosik, Piotr Borowicz, Elżbieta Bednarek, Wojciech Bocian, Jerzy Sitkowski, Lech Kozerski
    Abstract:

    Purpose Identification of human Insulin analogs’ impurity with a mass shift +14 Da in comparison to a parent protein. Methods The protein sequence variant was detected and identified with the application of peptide mapping, liquid chromatography, tandem mass spectrometric analysis, nuclear magnetic resonance spectroscopy (NMR) and Edman sequencing. Results The misincorporated lysine (Lys) at asparagine (Asn) position A21 was detected in recombinant human Insulin and its analogs. Conclusions Although there are three asparagine residues in the Insulin Derivative, the misincorporation of lysine occurred only at position A21. The process involves G/U or A/U wobble base pairing.

Jerzy Sitkowski - One of the best experts on this subject based on the ideXlab platform.

  • Identification of Lysine Misincorporation at Asparagine Position in Recombinant Insulin Analogs Produced in E. coli.
    Pharmaceutical research, 2019
    Co-Authors: Dorota Stadnik, Anna Bierczynska-krzysik, Joanna Zielińska, Jarosław Antosik, Piotr Borowicz, Elżbieta Bednarek, Wojciech Bocian, Jerzy Sitkowski, Lech Kozerski
    Abstract:

    Identification of human Insulin analogs’ impurity with a mass shift +14 Da in comparison to a parent protein. The protein sequence variant was detected and identified with the application of peptide mapping, liquid chromatography, tandem mass spectrometric analysis, nuclear magnetic resonance spectroscopy (NMR) and Edman sequencing. The misincorporated lysine (Lys) at asparagine (Asn) position A21 was detected in recombinant human Insulin and its analogs. Although there are three asparagine residues in the Insulin Derivative, the misincorporation of lysine occurred only at position A21. The process involves G/U or A/U wobble base pairing.

  • Identification of Lysine Misincorporation at Asparagine Position in Recombinant Insulin Analogs Produced in E. coli
    Pharmaceutical Research, 2019
    Co-Authors: Dorota Stadnik, Anna Bierczynska-krzysik, Joanna Zielińska, Jarosław Antosik, Piotr Borowicz, Elżbieta Bednarek, Wojciech Bocian, Jerzy Sitkowski, Lech Kozerski
    Abstract:

    Purpose Identification of human Insulin analogs’ impurity with a mass shift +14 Da in comparison to a parent protein. Methods The protein sequence variant was detected and identified with the application of peptide mapping, liquid chromatography, tandem mass spectrometric analysis, nuclear magnetic resonance spectroscopy (NMR) and Edman sequencing. Results The misincorporated lysine (Lys) at asparagine (Asn) position A21 was detected in recombinant human Insulin and its analogs. Conclusions Although there are three asparagine residues in the Insulin Derivative, the misincorporation of lysine occurred only at position A21. The process involves G/U or A/U wobble base pairing.