H H de Jongh

Summary

Country: The Netherlands

Publications

  1. ncbi request reprint The helix nucleation site and propensity of the synthetic mitochondrial presequence of ornithine carbamoyltransferase
    H H de Jongh
    Wageningen Centre for Food Sciences and Centre for Protein Technology, Wageningen University, The Netherlands
    Eur J Biochem 267:5796-804. 2000
  2. ncbi request reprint Mild isolation procedure discloses new protein structural properties of beta-lactoglobulin
    H H de Jongh
    Wageningen Centre for Food Sciences, Department of Food Technology, Wageningen University, The Netherlands
    J Dairy Sci 84:562-71. 2001
  3. ncbi request reprint Proteins at air-water interfaces studied using external reflection circular dichroism
    Harmen H J De Jongh
    Wageningen Centre for Food Sciences, Department of Biopolymer Stability and Functionality, Diedenweg 20, Wageningen, The Netherlands
    Spectrochim Acta A Mol Biomol Spectrosc 58:3197-204. 2002
  4. ncbi request reprint Effects of pH and heat treatments on the structure and solubility of potato proteins in different preparations
    G A van Koningsveld
    Centre for Protein Technology, TNO-WU, Wageningen, The Netherlands
    J Agric Food Chem 49:4889-97. 2001
  5. ncbi request reprint Adsorption properties of proteins at and near the air/water interface from IRRAS spectra of protein solutions
    M B Meinders
    Department of Structure and Functionality, Wageningen Centre for Food Sciences, The Netherlands
    Eur Biophys J 30:256-67. 2001

Collaborators

Detail Information

Publications5

  1. ncbi request reprint The helix nucleation site and propensity of the synthetic mitochondrial presequence of ornithine carbamoyltransferase
    H H de Jongh
    Wageningen Centre for Food Sciences and Centre for Protein Technology, Wageningen University, The Netherlands
    Eur J Biochem 267:5796-804. 2000
    ..The findings are discussed in relation to the molecular recognition events at different stages of the transport process of this protein into mitochondria...
  2. ncbi request reprint Mild isolation procedure discloses new protein structural properties of beta-lactoglobulin
    H H de Jongh
    Wageningen Centre for Food Sciences, Department of Food Technology, Wageningen University, The Netherlands
    J Dairy Sci 84:562-71. 2001
    ..The addition of 20% glycerol could prevent this irreversible conformational change. The effect of the low temperature transition on the protein's functionality remains to be investigated...
  3. ncbi request reprint Proteins at air-water interfaces studied using external reflection circular dichroism
    Harmen H J De Jongh
    Wageningen Centre for Food Sciences, Department of Biopolymer Stability and Functionality, Diedenweg 20, Wageningen, The Netherlands
    Spectrochim Acta A Mol Biomol Spectrosc 58:3197-204. 2002
    ....
  4. ncbi request reprint Effects of pH and heat treatments on the structure and solubility of potato proteins in different preparations
    G A van Koningsveld
    Centre for Protein Technology, TNO-WU, Wageningen, The Netherlands
    J Agric Food Chem 49:4889-97. 2001
    ..The tertiary structure of patatin was irreversibly altered by precipitation at pH 5. At mildly acidic pH the overall potato protein solubility was dependent on ionic strength and the presence of unfolded patatin...
  5. ncbi request reprint Adsorption properties of proteins at and near the air/water interface from IRRAS spectra of protein solutions
    M B Meinders
    Department of Structure and Functionality, Wageningen Centre for Food Sciences, The Netherlands
    Eur Biophys J 30:256-67. 2001
    ..At an initial concentration of 10 mg/mL, the concentration in the surface layer is about 15 times higher than in the subphase, while the thickness is about 30 nm...